| Year |
Citation |
Score |
| 2022 |
Manathunga L, Akter R, Zhyvoloup A, Simmerling C, Raleigh DP. On the Plasticity of Amyloid Formation: The Impact of Destabilizing Small to Large Substitutions on IAPP Amyloid Formation. Protein Science : a Publication of the Protein Society. e4539. PMID 36484106 DOI: 10.1002/pro.4539 |
0.325 |
|
| 2022 |
Miller MET, Li MH, Baghai A, Peetz VH, Zhyvoloup A, Raleigh DP. Analysis of Sheep and Goat IAPP Provides Insight into IAPP Amyloidogenicity and Cytotoxicity. Biochemistry. 61: 2531-2545. PMID 36286531 DOI: 10.1021/acs.biochem.2c00470 |
0.303 |
|
| 2021 |
Zou J, Xiao S, Simmerling C, Raleigh DP. Quantitative Analysis of Protein Unfolded State Energetics: Experimental and Computational Studies Demonstrate That Non-Native Side-Chain Interactions Stabilize Local Native Backbone Structure. The Journal of Physical Chemistry. B. PMID 33779182 DOI: 10.1021/acs.jpcb.0c08922 |
0.601 |
|
| 2020 |
Stenzoski NE, Zou J, Piserchio A, Ghose R, Holehouse AS, Raleigh DP. The Cold-Unfolded State is Expanded but Contains Long- and Medium-range Contacts and Is Poorly Described by Homopolymer Models. Biochemistry. PMID 32786415 DOI: 10.1021/Acs.Biochem.0C00469 |
0.432 |
|
| 2020 |
Templin AT, Mellati M, Meier DT, Esser N, Hogan MF, Castillo JJ, Akter R, Raleigh DP, Zraika S, Hull RL, Kahn SE. Low concentration IL-1β promotes islet amyloid formation by increasing hIAPP release from humanised mouse islets in vitro. Diabetologia. PMID 32728889 DOI: 10.1007/S00125-020-05232-2 |
0.33 |
|
| 2020 |
Noh D, Bower RL, Hay DL, Zhyvoloup A, Raleigh DP. Analysis of Amylin Consensus Sequences Suggests that Human Amylin is Not Optimized to Minimize Amyloid Formation and Provides Clues to Factors that Modulate Amyloidogenicity. Acs Chemical Biology. PMID 32364695 DOI: 10.1021/Acschembio.9B01050 |
0.345 |
|
| 2020 |
Ridgway Z, Lee KH, Zhyvoloup A, Wong A, Eldrid C, Hannaberry E, Thalassinos K, Abedini A, Raleigh DP. Analysis of Baboon IAPP Provides Insight into Amyloidogenicity and Cytotoxicity of Human IAPP. Biophysical Journal. PMID 32105649 DOI: 10.1016/J.Bpj.2019.12.027 |
0.629 |
|
| 2020 |
Ridgway Z, Eldrid CFS, Zhyvoloup A, Ben-Younis A, Noh D, Thalassinos K, Raleigh DP. Analysis of Proline Substitutions Reveals the Plasticity and Sequence Sensitivity of Human IAPP Amyloidogenicity and Toxicity. Biochemistry. PMID 31922743 DOI: 10.1021/Acs.Biochem.9B01109 |
0.377 |
|
| 2020 |
Esser N, Hogan MF, Templin AT, Castillo JJ, Raleigh D, Edgar JS, Zraika S, Hull RL, Kahn SE. 2039-P: Plasmin-Mediated Cleavage of Human Islet Amyloid Polypeptide (hIAPP) Protects ß-Cells from Amyloid-Induced Toxicity Diabetes. 69. DOI: 10.2337/Db20-2039-P |
0.348 |
|
| 2019 |
Lee KH, Noh D, Zhyvoloup A, Raleigh DP. Analysis of Prairie Vole Amylin Reveals the Importance of the N-terminus and Residue-22 in Amyloidogenicity and Cytotoxicity. Biochemistry. PMID 31777253 DOI: 10.1021/Acs.Biochem.9B00952 |
0.427 |
|
| 2019 |
Lee KH, Zhyvoloup A, Raleigh D. Amyloidogenicity and cytotoxicity of des-Lys-1 human amylin provides insight into amylin self-assembly and highlights the difficulties of defining amyloidogenicity. Protein Engineering, Design & Selection : Peds. PMID 31768548 DOI: 10.1093/Protein/Gzz036 |
0.405 |
|
| 2019 |
Akter R, Zou J, Raleigh DP. Differential effects of serine side-chain interactions in amyloid formation by islet amyloid polypeptide. Protein Science : a Publication of the Protein Society. PMID 31705766 DOI: 10.1002/Pro.3782 |
0.44 |
|
| 2019 |
Zou J, Simmerling C, Raleigh DP. Dissecting the Energetics of Intrinsically Disordered Proteins via a Hybrid Experimental and Computational Approach. The Journal of Physical Chemistry. B. PMID 31702919 DOI: 10.1021/Acs.Jpcb.9B08323 |
0.384 |
|
| 2019 |
Akter R, Zhyvoloup A, Zheng B, Bhatia SR, Raleigh DP. The triphenylmethane dye brilliant blue G is only moderately effective at inhibiting amyloid formation by human amylin or at disaggregating amylin amyloid fibrils, but interferes with amyloid assays; Implications for inhibitor design. Plos One. 14: e0219130. PMID 31404073 DOI: 10.1371/Journal.Pone.0219130 |
0.364 |
|
| 2019 |
Peran I, Holehouse AS, Carrico IS, Pappu RV, Bilsel O, Raleigh DP. Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions. Proceedings of the National Academy of Sciences of the United States of America. PMID 31167941 DOI: 10.1073/Pnas.1818206116 |
0.43 |
|
| 2019 |
Zhang S, Zhang Y, Stenzoski NE, Zou J, Peran I, McCallum SA, Raleigh DP, Royer CA. Pressure-Temperature Analysis of the Stability of the CTL9 Domain Reveals Hidden Intermediates. Biophysical Journal. PMID 30685054 DOI: 10.1016/J.Bpj.2019.01.002 |
0.392 |
|
| 2019 |
ESSER N, HOGAN MF, APLIN A, TEMPLIN AT, EL-OSTA S, RALEIGH D, EDGAR JS, ZRAIKA S, HULL RL, KAHN SE. 2124-P: The Tissue Plasminogen Activator (tPA)/Plasmin System Reduces Amyloid Formation by Cleaving Human Islet Amyloid Polypeptide (hIAPP) Diabetes. 68: 2124-P. DOI: 10.2337/Db19-2124-P |
0.325 |
|
| 2019 |
Holehouse AS, Peran I, Stenzoski NE, Zou J, Piserchio A, Ghose R, Carrico IS, Bilsel O, Raleigh DP, Pappu RV. Protein Unfolded States are Characterized by the Duality of Sequence-Specific Conformational Preferences and Ensemble-Averaged Features of Canonical Random Coils Biophysical Journal. 116: 199a-200a. DOI: 10.1016/J.Bpj.2018.11.1104 |
0.388 |
|
| 2018 |
Nagarajan S, Xiao S, Raleigh DP, Dyer RB. Heterogeneity in the Folding of Villin Headpiece Subdomain HP36. The Journal of Physical Chemistry. B. PMID 30118232 DOI: 10.1021/Acs.Jpcb.8B07683 |
0.593 |
|
| 2018 |
Stenzoski NE, Luan B, Holehouse AS, Raleigh DP. The Unfolded State of the C-Terminal Domain of L9 Expands at Low but Not at Elevated Temperatures. Biophysical Journal. PMID 30098729 DOI: 10.1016/J.Bpj.2018.07.013 |
0.585 |
|
| 2018 |
Akter R, Bower RL, Abedini A, Schmidt AM, Hay DL, Raleigh DP. Amyloidogenicity, Cytotoxicity and Receptor Activity of Bovine Amylin; Implications for Xenobiotic Transplantation and the Design of Non-toxic Amylin Variants. Acs Chemical Biology. PMID 30086232 DOI: 10.1021/Acschembio.8B00690 |
0.609 |
|
| 2018 |
Baum J, Raleigh D. Protein Aggregation. Protein Science : a Publication of the Protein Society. 27: 1149-1150. PMID 29975010 DOI: 10.1002/Pro.3446 |
0.575 |
|
| 2018 |
Ridgway Z, Zhang X, Wong AG, Abedini A, Schmidt AM, Raleigh DP. Analysis of the role of the conserved disulfide in amyloid formation by human IAPP in homogenous and heterogeneous environments. Biochemistry. PMID 29697253 DOI: 10.1021/Acs.Biochem.8B00017 |
0.638 |
|
| 2018 |
Abedini A, Cao P, Plesner A, Zhang J, He M, Derk J, Patil SA, Rosario R, Lonier J, Song F, Koh H, Li H, Raleigh DP, Schmidt AM. RAGE binds preamyloid IAPP intermediates and mediates pancreatic β cell proteotoxicity. The Journal of Clinical Investigation. PMID 29337308 DOI: 10.1172/Jci85210 |
0.569 |
|
| 2017 |
Akter R, Abedini A, Ridgway Z, Zhang X, Kleinberg J, Schmidt AM, Raleigh DP. Evolutionary Adaptation and Amyloid Formation: Does the Reduced Amyloidogenicity and Cytotoxicity of Ursine Amylin Contribute to the Metabolic Adaption of Bears and Polar Bears? Israel Journal of Chemistry. 57: 750-761. PMID 29955200 DOI: 10.1002/Ijch.201600081 |
0.577 |
|
| 2017 |
Serrano AL, Lomont JP, Tu LH, Raleigh DP, Zanni MT. A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP. Journal of the American Chemical Society. PMID 29072444 DOI: 10.1021/Jacs.7B08830 |
0.418 |
|
| 2017 |
Young LM, Tu LH, Raleigh DP, Ashcroft AE, Radford SE. Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers. Chemical Science. 8: 5030-5040. PMID 28970890 DOI: 10.1039/C7Sc00620A |
0.396 |
|
| 2017 |
Raleigh D, Zhang X, Hastoy B, Clark A. The β-cell assassin: IAPP cytotoxicity. Journal of Molecular Endocrinology. PMID 28811318 DOI: 10.1530/Jme-17-0105 |
0.388 |
|
| 2017 |
Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP. The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State. Biophysical Journal. 112: 1797-1806. PMID 28494951 DOI: 10.1016/J.Bpj.2017.01.034 |
0.738 |
|
| 2017 |
Watson MD, Peran I, Zou J, Bilsel O, Raleigh DP. Selenomethionine Quenching of Tryptophan Fluorescence Provides a Simple Probe of Protein Structure. Biochemistry. PMID 28124899 DOI: 10.1021/Acs.Biochem.6B01000 |
0.387 |
|
| 2017 |
Zhang X, St Clair JR, London E, Raleigh DP. Islet Amyloid Polypeptide Membrane Interactions: Effects of Membrane Composition. Biochemistry. PMID 28054763 DOI: 10.1021/Acs.Biochem.6B01016 |
0.311 |
|
| 2017 |
Zhang Y, Kitazawa S, Peran I, Stenzoski N, McCallum S, Raleigh D, Royer C. Using High Pressure NMR to Study Folding Cooperativity and Kinetics of Protein L9 Biophysical Journal. 112: 168a. DOI: 10.1016/J.Bpj.2016.11.926 |
0.461 |
|
| 2017 |
Holehouse AS, Perana I, Carrico IS, Bilsel O, Raleigh DP, Pappu RV. Simulations and Experiments Provide a Convergent View of Protein Unfolded States under Folding Conditions Biophysical Journal. 112: 315a. DOI: 10.1016/J.Bpj.2016.11.1709 |
0.449 |
|
| 2016 |
Zou J, Song B, Simmerling C, Raleigh D. Experimental and Computational Analysis of Protein Stabilization by Gly-to-d-Ala Substitution: A Convolution of Native State and Unfolded State Effects. Journal of the American Chemical Society. 138: 15682-15689. PMID 27934019 DOI: 10.1021/Jacs.6B09511 |
0.43 |
|
| 2016 |
Zhang Y, Kitazawa S, Peran I, Stenzoski N, McCallum SA, Raleigh DP, Royer CA. High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States. Journal of the American Chemical Society. PMID 27781428 DOI: 10.1021/Jacs.6B09887 |
0.438 |
|
| 2016 |
Wong AG, Raleigh DP. The Dye SYPRO Orange Binds to Amylin Amyloid Fibrils but Not Pre-fibrillar Intermediates. Protein Science : a Publication of the Protein Society. PMID 27479186 DOI: 10.1002/Pro.2992 |
0.401 |
|
| 2016 |
Watson MD, Peran I, Raleigh DP. A Non-perturbing Probe of Coiled Coil Formation Based on Electron Transfer Mediated Fluorescence Quenching. Biochemistry. PMID 27258904 DOI: 10.1021/Acs.Biochem.6B00270 |
0.361 |
|
| 2016 |
Abedini A, Plesner A, Cao P, Ridgway Z, Zhang J, Tu LH, Middleton CT, Chao B, Sartori D, Meng F, Wang H, Wong AG, Zanni MT, Verchere CB, Raleigh DP, et al. Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics. Elife. 5. PMID 27213520 DOI: 10.7554/Elife.12977 |
0.692 |
|
| 2016 |
Sengupta R, Pantel A, Cheng X, Shkel I, Peran I, Stenzoski N, Raleigh DP, Record MT. Positioning the Intracellular Salt Potassium Glutamate in the Hofmeister Series by Chemical Unfolding Studies of NTL9. Biochemistry. PMID 27054379 DOI: 10.1021/Acs.Biochem.6B00173 |
0.351 |
|
| 2016 |
Ilitchev AI, Giammona MJ, Do TD, Wong AG, Buratto SK, Shea JE, Raleigh DP, Bowers MT. Human Islet Amyloid Polypeptide N-Terminus Fragment Self-Assembly: Effect of Conserved Disulfide Bond on Aggregation Propensity. Journal of the American Society For Mass Spectrometry. PMID 26894887 DOI: 10.1007/S13361-016-1347-7 |
0.396 |
|
| 2016 |
Akter R, Cao P, Noor H, Ridgway Z, Tu LH, Wang H, Wong AG, Zhang X, Abedini A, Schmidt AM, Raleigh DP. Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology. Journal of Diabetes Research. 2016: 2798269. PMID 26649319 DOI: 10.1155/2016/2798269 |
0.594 |
|
| 2016 |
Abedini A, Cao P, Raleigh DP. Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins. Methods in Molecular Biology (Clifton, N.J.). 1345: 55-66. PMID 26453205 DOI: 10.1007/978-1-4939-2978-8_4 |
0.658 |
|
| 2016 |
Abedini A, Plesner A, Cao P, Ridgway Z, Zhang J, Tu L, Middleton CT, Chao B, Sartori DJ, Meng F, Wang H, Wong AG, Zanni MT, Verchere CB, Raleigh DP, et al. Author response: Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics Elife. DOI: 10.7554/Elife.12977.045 |
0.658 |
|
| 2015 |
Wong AG, Wu C, Hannaberry E, Watson MD, Shea JE, Raleigh DP. Analysis of the Amyloidogenic Potential of Pufferfish (Takifugu rubripes) Islet Amyloid Polypeptide Highlights the Limitations of Thioflavin-T Assays and the Difficulties in Defining Amyloidogenicity. Biochemistry. PMID 26694855 DOI: 10.1021/Acs.Biochem.5B01107 |
0.392 |
|
| 2015 |
Peran I, Watson MD, Bilsel O, Raleigh DP. Selenomethionine, p-cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure. Chemical Communications (Cambridge, England). PMID 26686928 DOI: 10.1039/C5Cc08232C |
0.347 |
|
| 2015 |
Lee CC, Julian MC, Tiller KE, Meng F, DuConge SE, Akter R, Raleigh DP, Tessier PM. Design and Optimization of Anti-Amyloid Domain Antibodies Specific for β-Amyloid and Islet Amyloid Polypeptide. The Journal of Biological Chemistry. PMID 26601942 DOI: 10.1074/Jbc.M115.682336 |
0.634 |
|
| 2015 |
Meier DT, Tu LH, Zraika S, Hogan MF, Templin AT, Hull RL, Raleigh DP, Kahn SE. Matrix Metalloproteinase-9 Protects Islets From Amyloid-Induced Toxicity. The Journal of Biological Chemistry. PMID 26483547 DOI: 10.1074/Jbc.M115.676692 |
0.311 |
|
| 2015 |
Wang H, Ridgway Z, Cao P, Ruzsicska BP, Raleigh DP. Analysis of the Ability of Pramlintide to Inhibit Amyloid Formation by Human Islet Amyloid Polypeptide Reveals a Balance between Optimum Recognition and Reduced Amyloidgenicity. Biochemistry. PMID 26407043 DOI: 10.1021/Acs.Biochem.5B00567 |
0.393 |
|
| 2015 |
Young LM, Mahood RA, Saunders JC, Tu LH, Raleigh DP, Radford SE, Ashcroft AE. Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry. The Analyst. 140: 6990-9. PMID 26193839 DOI: 10.1039/C5An00865D |
0.416 |
|
| 2015 |
Tu LH, Young LM, Wong AG, Ashcroft AE, Radford SE, Raleigh DP. Mutational analysis of the ability of resveratrol to inhibit amyloid formation by islet amyloid polypeptide: critical evaluation of the importance of aromatic-inhibitor and histidine-inhibitor interactions. Biochemistry. 54: 666-76. PMID 25531836 DOI: 10.1021/Bi501016R |
0.426 |
|
| 2015 |
Young LM, Saunders JC, Mahood RA, Revill CH, Foster RJ, Tu LH, Raleigh DP, Radford SE, Ashcroft AE. Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry. Nature Chemistry. 7: 73-81. PMID 25515893 DOI: 10.1038/Nchem.2129 |
0.361 |
|
| 2014 |
Wang H, Raleigh DP. General amyloid inhibitors? A critical examination of the inhibition of IAPP amyloid formation by inositol stereoisomers. Plos One. 9: e104023. PMID 25260075 DOI: 10.1371/Journal.Pone.0104023 |
0.401 |
|
| 2014 |
Susa AC, Wu C, Bernstein SL, Dupuis NF, Wang H, Raleigh DP, Shea JE, Bowers MT. Defining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide-insulin interactions. Journal of the American Chemical Society. 136: 12912-9. PMID 25144879 DOI: 10.1021/Ja504031D |
0.333 |
|
| 2014 |
Wang H, Abedini A, Ruzsicska B, Raleigh DP. Rationally designed, nontoxic, nonamyloidogenic analogues of human islet amyloid polypeptide with improved solubility. Biochemistry. 53: 5876-84. PMID 25140605 DOI: 10.1021/Bi500592P |
0.562 |
|
| 2014 |
Cho JH, Meng W, Sato S, Kim EY, Schindelin H, Raleigh DP. Energetically significant networks of coupled interactions within an unfolded protein. Proceedings of the National Academy of Sciences of the United States of America. 111: 12079-84. PMID 25099351 DOI: 10.1073/Pnas.1402054111 |
0.802 |
|
| 2014 |
Raleigh DP. Guilt by Association: The Physical Chemistry and Biology of Protein Aggregation. The Journal of Physical Chemistry Letters. 5: 2012-2014. PMID 24932381 DOI: 10.1021/Jz501011W |
0.421 |
|
| 2014 |
Peran I, Oudenhoven T, Woys AM, Watson MD, Zhang TO, Carrico I, Zanni MT, Raleigh DP. General strategy for the bioorthogonal incorporation of strongly absorbing, solvation-sensitive infrared probes into proteins. The Journal of Physical Chemistry. B. 118: 7946-53. PMID 24749542 DOI: 10.7490/F1000Research.1097006.1 |
0.361 |
|
| 2014 |
Tu LH, Serrano AL, Zanni MT, Raleigh DP. Mutational analysis of preamyloid intermediates: the role of his-tyr interactions in islet amyloid formation. Biophysical Journal. 106: 1520-7. PMID 24703313 DOI: 10.1016/J.Bpj.2013.12.052 |
0.479 |
|
| 2014 |
Wang H, Raleigh DP. The ability of insulin to inhibit the formation of amyloid by pro-islet amyloid polypeptide processing intermediates is significantly reduced in the presence of sulfated glycosaminoglycans. Biochemistry. 53: 2605-14. PMID 24654599 DOI: 10.1021/Bi4015488 |
0.384 |
|
| 2014 |
Lahiri T, Luan B, Raleigh DP, Boon EM. A structural basis for the regulation of an H-NOX-associated cyclic-di-GMP synthase/phosphodiesterase enzyme by nitric oxide-bound H-NOX. Biochemistry. 53: 2126-35. PMID 24628400 DOI: 10.1021/Bi401597M |
0.551 |
|
| 2014 |
Young LM, Cao P, Raleigh DP, Ashcroft AE, Radford SE. Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitors. Journal of the American Chemical Society. 136: 660-70. PMID 24372466 DOI: 10.1021/Ja406831N |
0.341 |
|
| 2014 |
Luan B, Lyle N, Pappu RV, Raleigh DP. Denatured state ensembles with the same radii of gyration can form significantly different long-range contacts. Biochemistry. 53: 39-47. PMID 24280003 DOI: 10.1021/Bi4008337 |
0.643 |
|
| 2013 |
Buchanan LE, Dunkelberger EB, Tran HQ, Cheng PN, Chiu CC, Cao P, Raleigh DP, de Pablo JJ, Nowick JS, Zanni MT. Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet. Proceedings of the National Academy of Sciences of the United States of America. 110: 19285-90. PMID 24218609 DOI: 10.1073/Pnas.1314481110 |
0.416 |
|
| 2013 |
Cao P, Abedini A, Wang H, Tu LH, Zhang X, Schmidt AM, Raleigh DP. Islet amyloid polypeptide toxicity and membrane interactions. Proceedings of the National Academy of Sciences of the United States of America. 110: 19279-84. PMID 24218607 DOI: 10.1073/Pnas.1305517110 |
0.576 |
|
| 2013 |
Xiao S, Patsalo V, Shan B, Bi Y, Green DF, Raleigh DP. Rational modification of protein stability by targeting surface sites leads to complicated results. Proceedings of the National Academy of Sciences of the United States of America. 110: 11337-42. PMID 23798426 DOI: 10.1073/Pnas.1222245110 |
0.697 |
|
| 2013 |
Meng W, Luan B, Lyle N, Pappu RV, Raleigh DP. The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9. Biochemistry. 52: 2662-71. PMID 23480024 DOI: 10.1021/Bi301667U |
0.761 |
|
| 2013 |
Luan B, Shan B, Baiz C, Tokmakoff A, Raleigh DP. Cooperative cold denaturation: the case of the C-terminal domain of ribosomal protein L9. Biochemistry. 52: 2402-9. PMID 23461364 DOI: 10.1021/Bi3016789 |
0.723 |
|
| 2013 |
Cao P, Marek P, Noor H, Patsalo V, Tu LH, Wang H, Abedini A, Raleigh DP. Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity. Febs Letters. 587: 1106-18. PMID 23380070 DOI: 10.1016/J.Febslet.2013.01.046 |
0.793 |
|
| 2013 |
Meng W, Lyle N, Luan B, Raleigh DP, Pappu RV. Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure. Proceedings of the National Academy of Sciences of the United States of America. 110: 2123-8. PMID 23341588 DOI: 10.1073/Pnas.1216979110 |
0.728 |
|
| 2013 |
Cao P, Abedini A, Raleigh DP. Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology. Current Opinion in Structural Biology. 23: 82-9. PMID 23266002 DOI: 10.1016/J.Sbi.2012.11.003 |
0.589 |
|
| 2013 |
Tu LH, Raleigh DP. Role of aromatic interactions in amyloid formation by islet amyloid polypeptide. Biochemistry. 52: 333-42. PMID 23256729 DOI: 10.1021/Bi3014278 |
0.425 |
|
| 2013 |
Wang H, Cao P, Raleigh DP. Amyloid formation in heterogeneous environments: islet amyloid polypeptide glycosaminoglycan interactions. Journal of Molecular Biology. 425: 492-505. PMID 23154166 DOI: 10.1016/J.Bpj.2012.11.295 |
0.376 |
|
| 2013 |
Tu L, Raleigh D. Analysis of the Role of Aromatic Interactions in Amyloid Formation by Islet Amyloid Polypeptide Biophysical Journal. 104: 47a. DOI: 10.1016/J.Bpj.2012.11.298 |
0.429 |
|
| 2013 |
Cao P, Abedini A, Plesner A, Marie Schmidt A, Raleigh D. Toxic Intermediates in Islet Amyloid Formation: Analysis of IAPP Mutants Reveals a Correlation between Lag Time and Toxicity Biophysical Journal. 104: 359a. DOI: 10.1016/J.Bpj.2012.11.1995 |
0.629 |
|
| 2012 |
Ladiwala AR, Bhattacharya M, Perchiacca JM, Cao P, Raleigh DP, Abedini A, Schmidt AM, Varkey J, Langen R, Tessier PM. Rational design of potent domain antibody inhibitors of amyloid fibril assembly. Proceedings of the National Academy of Sciences of the United States of America. 109: 19965-70. PMID 23161913 DOI: 10.1073/Pnas.1208797109 |
0.618 |
|
| 2012 |
Marek PJ, Patsalo V, Green DF, Raleigh DP. Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects. Biochemistry. 51: 8478-90. PMID 23016872 DOI: 10.1021/Bi300574R |
0.763 |
|
| 2012 |
Davis CM, Xiao S, Raleigh DP, Dyer RB. Raising the speed limit for β-hairpin formation. Journal of the American Chemical Society. 134: 14476-82. PMID 22873643 DOI: 10.1021/Ja3046734 |
0.642 |
|
| 2012 |
Dunkelberger EB, Buchanan LE, Marek P, Cao P, Raleigh DP, Zanni MT. Deamidation accelerates amyloid formation and alters amylin fiber structure. Journal of the American Chemical Society. 134: 12658-67. PMID 22734583 DOI: 10.1021/Ja3039486 |
0.767 |
|
| 2012 |
Brewer SH, Tang Y, Vu DM, Gnanakaran S, Raleigh DP, Dyer RB. Temperature dependence of water interactions with the amide carbonyls of α-helices. Biochemistry. 51: 5293-9. PMID 22680405 DOI: 10.1021/Bi3006434 |
0.596 |
|
| 2012 |
Patsalo V, Yondola MA, Luan B, Shoshani I, Kisker C, Green DF, Raleigh DP, Hearing P. Biophysical and functional analyses suggest that adenovirus E4-ORF3 protein requires higher-order multimerization to function against promyelocytic leukemia protein nuclear bodies. The Journal of Biological Chemistry. 287: 22573-83. PMID 22573317 DOI: 10.1074/Jbc.M112.344234 |
0.575 |
|
| 2012 |
Gupta R, Kapoor N, Raleigh DP, Sakmar TP. Nucleobindin 1 caps human islet amyloid polypeptide protofibrils to prevent amyloid fibril formation Journal of Molecular Biology. 421: 378-389. PMID 22542527 DOI: 10.1016/J.Jmb.2012.04.017 |
0.381 |
|
| 2012 |
Middleton CT, Marek P, Cao P, Chiu CC, Singh S, Woys AM, de Pablo JJ, Raleigh DP, Zanni MT. Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor. Nature Chemistry. 4: 355-60. PMID 22522254 DOI: 10.1038/Nchem.1293 |
0.761 |
|
| 2012 |
Cao P, Raleigh DP. Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols. Biochemistry. 51: 2670-83. PMID 22409724 DOI: 10.1021/Bi2015162 |
0.383 |
|
| 2012 |
Noor H, Cao P, Raleigh DP. Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers. Protein Science : a Publication of the Protein Society. 21: 373-82. PMID 22238175 DOI: 10.1002/Pro.2023 |
0.371 |
|
| 2012 |
Cao P, Tu LH, Abedini A, Levsh O, Akter R, Patsalo V, Schmidt AM, Raleigh DP. Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20. Journal of Molecular Biology. 421: 282-95. PMID 22206987 DOI: 10.1016/J.Jmb.2011.12.032 |
0.647 |
|
| 2012 |
Lyle NJ, Meng W, Raleigh DP, Pappu RV. Simulations of Denatured Protein Ensembles Reproduce and Rationalize Experimental Observations of Persistent Contacts Between Residues Distal in Protein Sequence Biophysical Journal. 102: 630a. DOI: 10.1016/J.Bpj.2011.11.3433 |
0.646 |
|
| 2011 |
Choi JH, Raleigh D, Cho M. Azido Homoalanine is a Useful Infrared Probe for Monitoring Local Electrostatistics and Sidechain Solvation in Proteins. The Journal of Physical Chemistry Letters. 2: 2158-2162. PMID 22389750 DOI: 10.1021/Jz200980G |
0.362 |
|
| 2011 |
Nagarajan S, Taskent-Sezgin H, Parul D, Carrico I, Raleigh DP, Dyer RB. Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes. Journal of the American Chemical Society. 133: 20335-40. PMID 22039909 DOI: 10.1021/Ja2071362 |
0.404 |
|
| 2011 |
Patsalo V, Raleigh DP, Green DF. Rational and computational design of stabilized variants of cyanovirin-N that retain affinity and specificity for glycan ligands. Biochemistry. 50: 10698-712. PMID 22032696 DOI: 10.1021/Bi201411C |
0.38 |
|
| 2011 |
Wang L, Middleton CT, Singh S, Reddy AS, Woys AM, Strasfeld DB, Marek P, Raleigh DP, de Pablo JJ, Zanni MT, Skinner JL. 2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure. Journal of the American Chemical Society. 133: 16062-71. PMID 21916515 DOI: 10.1021/Ja204035K |
0.767 |
|
| 2011 |
Meng W, Raleigh DP. Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions. Proteins. 79: 3500-10. PMID 21915914 DOI: 10.1002/Prot.23145 |
0.653 |
|
| 2011 |
Cho JH, Muralidharan V, Vila-Perello M, Raleigh DP, Muir TW, Palmer AG. Tuning protein autoinhibition by domain destabilization. Nature Structural & Molecular Biology. 18: 550-5. PMID 21532593 DOI: 10.1038/Nsmb.2039 |
0.64 |
|
| 2011 |
Packer LE, Song B, Raleigh DP, McKnight CJ. Competition between intradomain and interdomain interactions: a buried salt bridge is essential for villin headpiece folding and actin binding. Biochemistry. 50: 3706-12. PMID 21449557 DOI: 10.1021/Bi1020343 |
0.435 |
|
| 2011 |
Meng F, Raleigh DP. Inhibition of glycosaminoglycan-mediated amyloid formation by islet amyloid polypeptide and proIAPP processing intermediates. Journal of Molecular Biology. 406: 491-502. PMID 21195086 DOI: 10.1016/J.Jmb.2010.12.028 |
0.62 |
|
| 2011 |
Meng W, Raleigh D. Backbone 1H,15N,13C and 13CB chemical shifts of folded state and denatured state for the N-terminal domain of ribosomal protein L9 (NTL9) V3AI4A double mutant Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr17675 |
0.627 |
|
| 2011 |
Fierz B, Chatterjee C, McGinty RK, Bar-Dagan M, Raleigh DP, Muir TW. Discrete Mechanisms Govern the Modulation of Chromatin Structure by Ubiquitylation and Acetylation Biophysical Journal. 100: 68a. DOI: 10.1016/J.Bpj.2010.12.570 |
0.304 |
|
| 2011 |
Gupta R, Kapoor N, Raleigh DP, Sakmar TP. Halting the Amyloid March: How a Novel Ca2+-Binding Protein, NUCB1, Prevents the Formation of Amyloid Fibrils Biophysical Journal. 100: 538a. DOI: 10.1016/J.Bpj.2010.12.3138 |
0.391 |
|
| 2010 |
Marek P, Woys AM, Sutton K, Zanni MT, Raleigh DP. Efficient microwave-assisted synthesis of human islet amyloid polypeptide designed to facilitate the specific incorporation of labeled amino acids. Organic Letters. 12: 4848-51. PMID 20931985 DOI: 10.1021/Ol101981B |
0.75 |
|
| 2010 |
Meng F, Raleigh DP, Abedini A. Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation. Journal of the American Chemical Society. 132: 14340-2. PMID 20873820 DOI: 10.1021/Ja1046186 |
0.713 |
|
| 2010 |
Taskent-Sezgin H, Chung J, Banerjee PS, Nagarajan S, Dyer RB, Carrico I, Raleigh DP. Azidohomoalanine: a conformationally sensitive IR probe of protein folding, protein structure, and electrostatics. Angewandte Chemie (International Ed. in English). 49: 7473-5. PMID 20815000 DOI: 10.1002/Anie.201003325 |
0.464 |
|
| 2010 |
Meng F, Abedini A, Plesner A, Verchere CB, Raleigh DP. The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. Biochemistry. 49: 8127-33. PMID 20707388 DOI: 10.1021/Bi100939A |
0.724 |
|
| 2010 |
Marek P, Mukherjee S, Zanni MT, Raleigh DP. Residue-specific, real-time characterization of lag-phase species and fibril growth during amyloid formation: a combined fluorescence and IR study of p-cyanophenylalanine analogs of islet amyloid polypeptide. Journal of Molecular Biology. 400: 878-88. PMID 20630475 DOI: 10.1016/J.Jmb.2010.05.041 |
0.76 |
|
| 2010 |
Xiao S, Raleigh DP. A critical assessment of putative gatekeeper interactions in the villin headpiece helical subdomain. Journal of Molecular Biology. 401: 274-85. PMID 20570680 DOI: 10.1016/J.Jmb.2010.05.070 |
0.642 |
|
| 2010 |
Taskent-Sezgin H, Marek P, Thomas R, Goldberg D, Chung J, Carrico I, Raleigh DP. Modulation of p-cyanophenylalanine fluorescence by amino acid side chains and rational design of fluorescence probes of alpha-helix formation. Biochemistry. 49: 6290-5. PMID 20565125 DOI: 10.1021/Bi100932P |
0.746 |
|
| 2010 |
Meng F, Abedini A, Plesner A, Middleton CT, Potter KJ, Zanni MT, Verchere CB, Raleigh DP. The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation. Journal of Molecular Biology. 400: 555-66. PMID 20452363 DOI: 10.1016/J.Jmb.2010.05.001 |
0.726 |
|
| 2010 |
Zraika S, Aston-Mourney K, Marek P, Hull RL, Green PS, Udayasankar J, Subramanian SL, Raleigh DP, Kahn SE. Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation. The Journal of Biological Chemistry. 285: 18177-83. PMID 20400513 DOI: 10.1074/Jbc.M109.082032 |
0.757 |
|
| 2010 |
Shan B, McClendon S, Rospigliosi C, Eliezer D, Raleigh DP. The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structure. Journal of the American Chemical Society. 132: 4669-77. PMID 20225821 DOI: 10.1021/Ja908104S |
0.648 |
|
| 2010 |
Cao P, Raleigh DP. Ester to amide switch peptides provide a simple method for preparing monomeric islet amyloid polypeptide under physiologically relevant conditions and facilitate investigations of amyloid formation. Journal of the American Chemical Society. 132: 4052-3. PMID 20201512 DOI: 10.1021/Ja910763M |
0.461 |
|
| 2010 |
Zraika S, Hull RL, Verchere CB, Clark A, Potter KJ, Fraser PE, Raleigh DP, Kahn SE. Toxic oligomers and islet beta cell death: guilty by association or convicted by circumstantial evidence? Diabetologia. 53: 1046-56. PMID 20182863 DOI: 10.1007/S00125-010-1671-6 |
0.373 |
|
| 2010 |
Potter KJ, Abedini A, Marek P, Klimek AM, Butterworth S, Driscoll M, Baker R, Nilsson MR, Warnock GL, Oberholzer J, Bertera S, Trucco M, Korbutt GS, Fraser PE, Raleigh DP, et al. Islet amyloid deposition limits the viability of human islet grafts but not porcine islet grafts. Proceedings of the National Academy of Sciences of the United States of America. 107: 4305-10. PMID 20160085 DOI: 10.1073/Pnas.0909024107 |
0.783 |
|
| 2010 |
Cao P, Meng F, Abedini A, Raleigh DP. The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors. Biochemistry. 49: 872-81. PMID 20028124 DOI: 10.1021/Bi901751B |
0.732 |
|
| 2010 |
Cho JH, O'Connell N, Raleigh DP, Palmer AG. Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion. Journal of the American Chemical Society. 132: 450-1. PMID 20028088 DOI: 10.1021/Ja909052H |
0.628 |
|
| 2010 |
Abedini A, Gupta R, Marek P, Meng F, Raleigh DP, Taskent H, Tracz S. Role of Posttranslational Modifications in Amyloid Formation Protein Misfolding Diseases: Current and Emerging Principles and Therapies. 131-144. DOI: 10.1002/9780470572702.ch7 |
0.788 |
|
| 2009 |
Strasfeld DB, Ling YL, Gupta R, Raleigh DP, Zanni MT. Strategies for extracting structural information from 2D IR spectroscopy of amyloid: application to islet amyloid polypeptide. The Journal of Physical Chemistry. B. 113: 15679-91. PMID 19883093 DOI: 10.1021/Jp9072203 |
0.397 |
|
| 2009 |
Taskent-Sezgin H, Chung J, Patsalo V, Miyake-Stoner SJ, Miller AM, Brewer SH, Mehl RA, Green DF, Raleigh DP, Carrico I. Interpretation of p-cyanophenylalanine fluorescence in proteins in terms of solvent exposure and contribution of side-chain quenchers: a combined fluorescence, IR and molecular dynamics study. Biochemistry. 48: 9040-6. PMID 19658436 DOI: 10.1021/Bi900938Z |
0.368 |
|
| 2009 |
O'Connell NE, Grey MJ, Tang Y, Kosuri P, Miloushev VZ, Raleigh DP, Palmer AG. Partially folded equilibrium intermediate of the villin headpiece HP67 defined by 13C relaxation dispersion. Journal of Biomolecular Nmr. 45: 85-98. PMID 19644656 DOI: 10.1007/S10858-009-9340-0 |
0.603 |
|
| 2009 |
Meng W, Shan B, Tang Y, Raleigh DP. Native like structure in the unfolded state of the villin headpiece helical subdomain, an ultrafast folding protein. Protein Science : a Publication of the Protein Society. 18: 1692-701. PMID 19598233 DOI: 10.1002/Pro.152 |
0.797 |
|
| 2009 |
Abedini A, Raleigh DP. A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides. Protein Engineering, Design & Selection : Peds. 22: 453-9. PMID 19596696 DOI: 10.1093/Protein/Gzp036 |
0.676 |
|
| 2009 |
Xiao S, Bi Y, Shan B, Raleigh DP. Analysis of core packing in a cooperatively folded miniature protein: the ultrafast folding villin headpiece helical subdomain. Biochemistry. 48: 4607-16. PMID 19354264 DOI: 10.1021/Bi8021763 |
0.698 |
|
| 2009 |
Shim SH, Gupta R, Ling YL, Strasfeld DB, Raleigh DP, Zanni MT. Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution. Proceedings of the National Academy of Sciences of the United States of America. 106: 6614-9. PMID 19346479 DOI: 10.1073/Pnas.0805957106 |
0.46 |
|
| 2009 |
Shan B, Eliezer D, Raleigh DP. The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure. Biochemistry. 48: 4707-19. PMID 19301913 DOI: 10.1021/Bi802299J |
0.634 |
|
| 2009 |
Abedini A, Raleigh DP. A role for helical intermediates in amyloid formation by natively unfolded polypeptides? Physical Biology. 6: 015005. PMID 19208933 DOI: 10.1088/1478-3975/6/1/015005 |
0.681 |
|
| 2009 |
Ling YL, Strasfeld DB, Shim SH, Raleigh DP, Zanni MT. Two-dimensional infrared spectroscopy provides evidence of an intermediate in the membrane-catalyzed assembly of diabetic amyloid. The Journal of Physical Chemistry. B. 113: 2498-505. PMID 19182939 DOI: 10.1021/Jp810261X |
0.387 |
|
| 2009 |
Cho JH, Raleigh DP. Experimental characterization of the denatured state ensemble of proteins. Methods in Molecular Biology (Clifton, N.J.). 490: 339-51. PMID 19157090 DOI: 10.1007/978-1-59745-367-7_14 |
0.668 |
|
| 2009 |
Raleigh DP, Shan B, Meng W, Cho J, Taskent H. Characterization of the Unfolded State Under Native Conditions: A Missing Piece of the Protein Folding Puzzle Biophysical Journal. 96: 220a. DOI: 10.1016/J.Bpj.2008.12.1921 |
0.797 |
|
| 2008 |
Shan B, Bhattacharya S, Eliezer D, Raleigh DP. The low-pH unfolded state of the C-terminal domain of the ribosomal protein L9 contains significant secondary structure in the absence of denaturant but is no more compact than the low-pH urea unfolded state. Biochemistry. 47: 9565-73. PMID 18707127 DOI: 10.1021/Bi8006862 |
0.626 |
|
| 2008 |
Respicio L, Nair PA, Huang Q, Anil B, Tracz S, Truglio JJ, Kisker C, Raleigh DP, Ojima I, Knudson DL, Tonge PJ, Slayden RA. Characterizing septum inhibition in Mycobacterium tuberculosis for novel drug discovery. Tuberculosis (Edinburgh, Scotland). 88: 420-9. PMID 18479968 DOI: 10.1016/J.Tube.2008.03.001 |
0.791 |
|
| 2008 |
Marek P, Gupta R, Raleigh DP. The fluorescent amino acid p-cyanophenylalanine provides an intrinsic probe of amyloid formation. Chembiochem : a European Journal of Chemical Biology. 9: 1372-4. PMID 18478525 DOI: 10.1002/Cbic.200800052 |
0.726 |
|
| 2008 |
Meng F, Marek P, Potter KJ, Verchere CB, Raleigh DP. Rifampicin does not prevent amyloid fibril formation by human islet amyloid polypeptide but does inhibit fibril thioflavin-T interactions: implications for mechanistic studies of beta-cell death. Biochemistry. 47: 6016-24. PMID 18457428 DOI: 10.1021/Bi702518M |
0.802 |
|
| 2008 |
Taskent H, Cho JH, Raleigh DP. Temperature-dependent Hammond behavior in a protein-folding reaction: analysis of transition-state movement and ground-state effects. Journal of Molecular Biology. 378: 699-706. PMID 18384809 DOI: 10.1016/J.Jmb.2008.02.024 |
0.626 |
|
| 2008 |
Cho JH, Sato S, Horng JC, Anil B, Raleigh DP. Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Archives of Biochemistry and Biophysics. 469: 20-8. PMID 17900519 DOI: 10.1016/J.Abb.2007.08.004 |
0.818 |
|
| 2008 |
Potter K, Abedini A, Butterworth S, Driscoll M, Marek P, Baker R, Korbutt GS, Fraser PE, Raleigh DP, Verchere CB. SPECIES-SPECIFIC SEQUENCE VARIATION OF PORCINE ISLET AMYLOID POLYPEPTIDE REDUCES ITS AMYLOIDOGENICITY AND MAY CONTRIBUTE TO IMPROVED FUNCTION AND SURVIVAL OF PIG ISLET XENOGRAFTS Clinical & Investigative Medicine. 31: 20. DOI: 10.25011/Cim.V31I4.4823 |
0.797 |
|
| 2008 |
Shan B, Bhattacharya S, Eliezer D, Raleigh D. Backbone and 13C and 1H assignments for acid unfolded state and urea unfolded state of CTL9 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr15883 |
0.55 |
|
| 2008 |
Potter K, Abedini A, Baker R, Butterworth S, Driscoll M, Marek P, Korbutt G, Fraser P, Raleigh D, Verchere C. Lack of amyloidogenicity and altered prohormone processing of porcine islet amyloid polypeptide may promote function and survival of pig islet xenografts. Canadian Journal of Diabetes. 32: 365. DOI: 10.1016/S1499-2671(08)24259-0 |
0.774 |
|
| 2007 |
Song B, Cho JH, Raleigh DP. Ionic-strength-dependent effects in protein folding: analysis of rate equilibrium free-energy relationships and their interpretation. Biochemistry. 46: 14206-14. PMID 18001140 DOI: 10.1021/Bi701645G |
0.636 |
|
| 2007 |
Aprilakis KN, Taskent H, Raleigh DP. Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding. Biochemistry. 46: 12308-13. PMID 17924662 DOI: 10.1021/Bi7010674 |
0.461 |
|
| 2007 |
Meng F, Abedini A, Song B, Raleigh DP. Amyloid formation by pro-islet amyloid polypeptide processing intermediates: examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes. Biochemistry. 46: 12091-9. PMID 17924651 DOI: 10.1021/Bi7004834 |
0.737 |
|
| 2007 |
Abedini A, Meng F, Raleigh DP. A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor. Journal of the American Chemical Society. 129: 11300-1. PMID 17722920 DOI: 10.1021/Ja072157Y |
0.728 |
|
| 2007 |
Bi Y, Cho JH, Kim EY, Shan B, Schindelin H, Raleigh DP. Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain. Biochemistry. 46: 7497-505. PMID 17536785 DOI: 10.1021/Bi6026314 |
0.71 |
|
| 2007 |
Sato S, Raleigh DP. Kinetic isotope effects reveal the presence of significant secondary structure in the transition state for the folding of the N-terminal domain of L9. Journal of Molecular Biology. 370: 349-55. PMID 17512540 DOI: 10.1016/J.Jmb.2007.02.084 |
0.591 |
|
| 2007 |
Wickstrom L, Bi Y, Hornak V, Raleigh DP, Simmerling C. Reconciling the solution and X-ray structures of the villin headpiece helical subdomain: molecular dynamics simulations and double mutant cycles reveal a stabilizing cation-pi interaction. Biochemistry. 46: 3624-34. PMID 17338549 DOI: 10.1021/Bi061785+ |
0.362 |
|
| 2007 |
Li Y, Shan B, Raleigh DP. The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9. Journal of Molecular Biology. 368: 256-62. PMID 17337003 DOI: 10.1016/J.Jmb.2007.02.011 |
0.598 |
|
| 2007 |
Marek P, Abedini A, Song B, Kanungo M, Johnson ME, Gupta R, Zaman W, Wong SS, Raleigh DP. Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology. Biochemistry. 46: 3255-61. PMID 17311418 DOI: 10.1021/Bi0621967 |
0.82 |
|
| 2007 |
Khandogin J, Raleigh DP, Brooks CL. Folding intermediate in the villin headpiece domain arises from disruption of a N-terminal hydrogen-bonded network. Journal of the American Chemical Society. 129: 3056-7. PMID 17311386 DOI: 10.1021/Ja0688880 |
0.42 |
|
| 2007 |
Brewer SH, Song B, Raleigh DP, Dyer RB. Residue specific resolution of protein folding dynamics using isotope-edited infrared temperature jump spectroscopy. Biochemistry. 46: 3279-85. PMID 17305369 DOI: 10.1021/Bi602372Y |
0.399 |
|
| 2007 |
Li Y, Gupta R, Cho JH, Raleigh DP. Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry. 46: 1013-21. PMID 17240985 DOI: 10.1021/Bi061516J |
0.671 |
|
| 2006 |
Cho JH, Raleigh DP. Denatured state effects and the origin of nonclassical phi values in protein folding. Journal of the American Chemical Society. 128: 16492-3. PMID 17177385 DOI: 10.1021/Ja0669878 |
0.595 |
|
| 2006 |
Anil B, Li Y, Cho JH, Raleigh DP. The unfolded state of NTL9 is compact in the absence of denaturant. Biochemistry. 45: 10110-6. PMID 16906769 DOI: 10.1021/Bi060636O |
0.804 |
|
| 2006 |
Abedini A, Tracz SM, Cho JH, Raleigh DP. Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation. Biochemistry. 45: 9228-37. PMID 16866369 DOI: 10.1021/Bi0510936 |
0.816 |
|
| 2006 |
Muralidharan V, Dutta K, Cho J, Vila-Perello M, Raleigh DP, Cowburn D, Muir TW. Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II. Biochemistry. 45: 8874-84. PMID 16846230 DOI: 10.1021/Bi060590Z |
0.611 |
|
| 2006 |
Li Y, Horng JC, Raleigh DP. pH dependent thermodynamic and amide exchange studies of the C-terminal domain of the ribosomal protein L9: implications for unfolded state structure. Biochemistry. 45: 8499-506. PMID 16834323 DOI: 10.1021/Bi052534O |
0.614 |
|
| 2006 |
Wickstrom L, Okur A, Song K, Hornak V, Raleigh DP, Simmerling CL. The unfolded state of the villin headpiece helical subdomain: computational studies of the role of locally stabilized structure. Journal of Molecular Biology. 360: 1094-107. PMID 16797585 DOI: 10.1016/J.Jmb.2006.04.070 |
0.457 |
|
| 2006 |
Cho JH, Raleigh DP. Electrostatic interactions in the denatured state and in the transition state for protein folding: effects of denatured state interactions on the analysis of transition state structure. Journal of Molecular Biology. 359: 1437-46. PMID 16787780 DOI: 10.1016/J.Jmb.2006.04.038 |
0.633 |
|
| 2006 |
Tang Y, Goger MJ, Raleigh DP. NMR characterization of a peptide model provides evidence for significant structure in the unfolded state of the villin headpiece helical subdomain. Biochemistry. 45: 6940-6. PMID 16734429 DOI: 10.1021/Bi052484N |
0.658 |
|
| 2006 |
Anil B, Craig-Schapiro R, Raleigh DP. Design of a hyperstable protein by rational consideration of unfolded state interactions. Journal of the American Chemical Society. 128: 3144-5. PMID 16522085 DOI: 10.1021/Ja057874B |
0.733 |
|
| 2006 |
Abedini A, Singh G, Raleigh DP. Recovery and purification of highly aggregation-prone disulfide-containing peptides: application to islet amyloid polypeptide. Analytical Biochemistry. 351: 181-6. PMID 16406209 DOI: 10.1016/J.Ab.2005.11.029 |
0.642 |
|
| 2006 |
Tang Y, Grey MJ, McKnight J, Palmer AG, Raleigh DP. Multistate folding of the villin headpiece domain. Journal of Molecular Biology. 355: 1066-77. PMID 16337228 DOI: 10.1016/J.Jmb.2005.10.066 |
0.637 |
|
| 2006 |
Grey MJ, Tang Y, Alexov E, McKnight CJ, Raleigh DP, Palmer AG. Characterizing a partially folded intermediate of the villin headpiece domain under non-denaturing conditions: contribution of His41 to the pH-dependent stability of the N-terminal subdomain. Journal of Molecular Biology. 355: 1078-94. PMID 16332376 DOI: 10.1016/J.Jmb.2005.11.001 |
0.633 |
|
| 2006 |
Bi Y, Tang Y, Raleigh DP, Cho JH. Efficient high level expression of peptides and proteins as fusion proteins with the N-terminal domain of L9: application to the villin headpiece helical subdomain. Protein Expression and Purification. 47: 234-40. PMID 16325421 DOI: 10.1016/J.Pep.2005.10.023 |
0.733 |
|
| 2006 |
Abedini A, Raleigh DP. Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP? Journal of Molecular Biology. 355: 274-81. PMID 16303136 DOI: 10.1016/J.Jmb.2005.10.052 |
0.657 |
|
| 2005 |
Abedini A, Raleigh DP. The role of His-18 in amyloid formation by human islet amyloid polypeptide. Biochemistry. 44: 16284-91. PMID 16331989 DOI: 10.1021/Bi051432V |
0.632 |
|
| 2005 |
Brewer SH, Vu DM, Tang Y, Li Y, Franzen S, Raleigh DP, Dyer RB. Effect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain. Proceedings of the National Academy of Sciences of the United States of America. 102: 16662-7. PMID 16269546 DOI: 10.1073/Pnas.0505432102 |
0.622 |
|
| 2005 |
Anil B, Sato S, Cho JH, Raleigh DP. Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. Journal of Molecular Biology. 354: 693-705. PMID 16246369 DOI: 10.1016/J.Jmb.2005.08.054 |
0.813 |
|
| 2005 |
Cho JH, Raleigh DP. Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. Journal of Molecular Biology. 353: 174-85. PMID 16165156 DOI: 10.1016/J.Jmb.2005.08.019 |
0.655 |
|
| 2005 |
Li Y, Picart F, Raleigh DP. Direct characterization of the folded, unfolded and urea-denatured states of the C-terminal domain of the ribosomal protein L9. Journal of Molecular Biology. 349: 839-46. PMID 15890362 DOI: 10.1016/J.Jmb.2005.04.017 |
0.382 |
|
| 2005 |
Raleigh DP, Plaxco KW. The protein folding transition state: what are Phi-values really telling us? Protein and Peptide Letters. 12: 117-22. PMID 15723637 DOI: 10.2174/0929866053005809 |
0.599 |
|
| 2005 |
Abedini A, Raleigh DP. Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide. Organic Letters. 7: 693-6. PMID 15704927 DOI: 10.1021/Ol047480+ |
0.602 |
|
| 2005 |
Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallée-Bélisle A, Main ER, Bemporad F, Qiu L, Teilum K, ... ... Raleigh DP, et al. Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Science : a Publication of the Protein Society. 14: 602-16. PMID 15689503 DOI: 10.1110/Ps.041205405 |
0.702 |
|
| 2005 |
Horng JC, Tracz SM, Lumb KJ, Raleigh DP. Slow folding of a three-helix protein via a compact intermediate. Biochemistry. 44: 627-34. PMID 15641788 DOI: 10.1021/Bi048852P |
0.82 |
|
| 2005 |
Chowdhury FA, Raleigh DP. A comparative study of the alpha-subdomains of bovine and human alpha-lactalbumin reveals key differences that correlate with molten globule stability. Protein Science : a Publication of the Protein Society. 14: 89-96. PMID 15576567 DOI: 10.1110/Ps.04977905 |
0.664 |
|
| 2005 |
Horng JC, Cho JH, Raleigh DP. Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding. Journal of Molecular Biology. 345: 163-73. PMID 15567419 DOI: 10.1016/J.Jmb.2004.10.023 |
0.72 |
|
| 2004 |
Tracz SM, Abedini A, Driscoll M, Raleigh DP. Role of aromatic interactions in amyloid formation by peptides derived from human Amylin. Biochemistry. 43: 15901-8. PMID 15595845 DOI: 10.1021/Bi048812L |
0.83 |
|
| 2004 |
Muralidharan V, Cho J, Trester-Zedlitz M, Kowalik L, Chait BT, Raleigh DP, Muir TW. Domain-specific incorporation of noninvasive optical probes into recombinant proteins. Journal of the American Chemical Society. 126: 14004-12. PMID 15506763 DOI: 10.1021/Ja0466199 |
0.616 |
|
| 2004 |
Anil B, Song B, Tang Y, Raleigh DP. Exploiting the right side of the Ramachandran plot: substitution of glycines by D-alanine can significantly increase protein stability. Journal of the American Chemical Society. 126: 13194-5. PMID 15479052 DOI: 10.1021/Ja047119I |
0.765 |
|
| 2004 |
Chowdhury FA, Fairman R, Bi Y, Rigotti DJ, Raleigh DP. Protein dissection experiments reveal key differences in the equilibrium folding of alpha-lactalbumin and the calcium binding lysozymes. Biochemistry. 43: 9961-7. PMID 15287723 DOI: 10.1021/Bi049277S |
0.759 |
|
| 2004 |
Cho JH, Sato S, Raleigh DP. Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state. Journal of Molecular Biology. 338: 827-37. PMID 15099748 DOI: 10.1016/J.Jmb.2004.02.073 |
0.736 |
|
| 2004 |
Tang Y, Rigotti DJ, Fairman R, Raleigh DP. Peptide models provide evidence for significant structure in the denatured state of a rapidly folding protein: the villin headpiece subdomain. Biochemistry. 43: 3264-72. PMID 15023077 DOI: 10.1021/Bi035652P |
0.778 |
|
| 2003 |
Horng JC, Raleigh DP. phi-Values beyond the ribosomally encoded amino acids: kinetic and thermodynamic consequences of incorporating trifluoromethyl amino acids in a globular protein. Journal of the American Chemical Society. 125: 9286-7. PMID 12889945 DOI: 10.1021/Ja0353199 |
0.644 |
|
| 2003 |
Vugmeyster L, Raleigh DP, Palmer AG, Vugmeister BE. Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution. Journal of the American Chemical Society. 125: 8400-4. PMID 12837113 DOI: 10.1021/Ja029480F |
0.638 |
|
| 2003 |
Horng JC, Demarest SJ, Raleigh DP. pH-dependent stability of the human alpha-lactalbumin molten globule state: contrasting roles of the 6 - 120 disulfide and the beta-subdomain at low and neutral pH. Proteins. 52: 193-202. PMID 12833543 DOI: 10.1002/Prot.10406 |
0.77 |
|
| 2003 |
Luisi DL, Snow CD, Lin JJ, Hendsch ZS, Tidor B, Raleigh DP. Surface salt bridges, double-mutant cycles, and protein stability: An experimental and computational analysis of the interaction of the Asp 23 side chain with the N-terminus of the N-terminal domain of the ribosomal protein L9 Biochemistry. 42: 7050-7060. PMID 12795600 DOI: 10.1021/Bi027202N |
0.807 |
|
| 2003 |
Wei Y, Horng JC, Vendel AC, Raleigh DP, Lumb KJ. Contribution to stability and folding of a buried polar residue at the CARM1 methylation site of the KIX domain of CBP. Biochemistry. 42: 7044-9. PMID 12795599 DOI: 10.1021/Bi0343976 |
0.782 |
|
| 2003 |
Wang M, Tang Y, Sato S, Vugmeyster L, McKnight CJ, Raleigh DP. Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. Journal of the American Chemical Society. 125: 6032-3. PMID 12785814 DOI: 10.1021/Ja028752B |
0.794 |
|
| 2003 |
Horng JC, Moroz V, Raleigh DP. Rapid cooperative two-state folding of a miniature alpha-beta protein and design of a thermostable variant. Journal of Molecular Biology. 326: 1261-70. PMID 12589767 DOI: 10.1016/S0022-2836(03)00028-7 |
0.658 |
|
| 2002 |
Horng JC, Moroz V, Rigotti DJ, Fairman R, Raleigh DP. Characterization of large peptide fragments derived from the N-terminal domain of the ribosomal protein L9: definition of the minimum folding motif and characterization of local electrostatic interactions. Biochemistry. 41: 13360-9. PMID 12416980 DOI: 10.1021/Bi026410C |
0.746 |
|
| 2002 |
Vugmeyster L, Trott O, McKnight CJ, Raleigh DP, Palmer AG. Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein. Journal of Molecular Biology. 320: 841-54. PMID 12095260 DOI: 10.1016/S0022-2836(02)00537-5 |
0.683 |
|
| 2002 |
Sato S, Raleigh DP. pH-dependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9. Journal of Molecular Biology. 318: 571-82. PMID 12051860 DOI: 10.1016/S0022-2836(02)00015-3 |
0.618 |
|
| 2002 |
Nilsson MR, Driscoll M, Raleigh DP. Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implications for the study of amyloid formation. Protein Science : a Publication of the Protein Society. 11: 342-9. PMID 11790844 DOI: 10.1110/Ps.48702 |
0.762 |
|
| 2001 |
Sato S, Xiang S, Raleigh DP. On the relationship between protein stability and folding kinetics: a comparative study of the N-terminal domains of RNase HI, E. coli and Bacillus stearothermophilus L9. Journal of Molecular Biology. 312: 569-77. PMID 11563917 DOI: 10.1006/Jmbi.2001.4968 |
0.621 |
|
| 2001 |
Camarero JA, Fushman D, Sato S, Giriat I, Cowburn D, Raleigh DP, Muir TW. Rescuing a destabilized protein fold through backbone cyclization. Journal of Molecular Biology. 308: 1045-62. PMID 11352590 DOI: 10.1006/Jmbi.2001.4631 |
0.617 |
|
| 2001 |
Demarest SJ, Zhou SQ, Robblee J, Fairman R, Chu B, Raleigh DP. A comparative study of peptide models of the alpha-domain of alpha-lactalbumin, lysozyme, and alpha-lactalbumin/lysozyme chimeras allows the elucidation of critical factors that contribute to the ability to form stable partially folded states. Biochemistry. 40: 2138-47. PMID 11329282 DOI: 10.1021/Bi001975Z |
0.782 |
|
| 2001 |
Nilsson MR, Nguyen LL, Raleigh DP. Synthesis and purification of amyloidogenic peptides. Analytical Biochemistry. 288: 76-82. PMID 11141308 DOI: 10.1006/Abio.2000.4887 |
0.747 |
|
| 2001 |
Demarest SJ, Horng JC, Raleigh DP. A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human alpha-lactalbumin. Proteins. 42: 237-42. PMID 11119648 DOI: 10.1002/1097-0134(20010201)42:2<237::Aid-Prot110>3.0.Co;2-B |
0.804 |
|
| 2001 |
Hill RB, Raleigh DP, Lombardi A, Degrado WF. ChemInform Abstract: De novo Design of Helical Bundles as Models for Understanding Protein Folding and Function Cheminform. 32: no-no. DOI: 10.1002/chin.200106253 |
0.532 |
|
| 2000 |
Hill RB, Raleigh DP, Lombardi A, Degrado WF. De novo design of helical bundles as models for understanding protein folding and function Accounts of Chemical Research. 33: 745-754. PMID 11087311 DOI: 10.1021/Ar970004H |
0.594 |
|
| 2000 |
Sato S, Sayid CJ, Raleigh DP. The failure of simple empirical relationships to predict the viscosity of mixed aqueous solutions of guanidine hydrochloride and glucose has important implications for the study of protein folding. Protein Science : a Publication of the Protein Society. 9: 1601-3. PMID 10975582 DOI: 10.1110/Ps.9.8.1601 |
0.495 |
|
| 2000 |
Luisi DL, Raleigh DP. pH-dependent interactions and the stability and folding kinetics of the N-terminal domain of L9. Electrostatic interactions are only weakly formed in the transition state for folding. Journal of Molecular Biology. 299: 1091-100. PMID 10843860 DOI: 10.1006/Jmbi.2000.3752 |
0.789 |
|
| 2000 |
Sato S, Luisi DL, Raleigh DP. pH jump studies of the folding of the multidomain ribosomal protein L9: the structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain. Biochemistry. 39: 4955-62. PMID 10769155 DOI: 10.1021/Bi992608U |
0.804 |
|
| 2000 |
Demarest SJ, Raleigh DP. Solution structure of a peptide model of a region important for the folding of alpha-lactalbumin provides evidence for the formation of nonnative structure in the denatured state. Proteins. 38: 189-96. PMID 10656265 DOI: 10.1002/(Sici)1097-0134(20000201)38:2<189::Aid-Prot7>3.0.Co;2-F |
0.744 |
|
| 2000 |
Spector S, Wang M, Carp SA, Robblee J, Hendsch ZS, Fairman R, Tidor B, Raleigh DP. Rational modification of protein stability by the mutation of charged surface residues. Biochemistry. 39: 872-9. PMID 10653630 DOI: 10.1021/Bi992091M |
0.665 |
|
| 2000 |
Moriarty DF, Demarest SJ, Robblee J, Fairman R, Raleigh DP. Local interactions and the role of the 6-120 disulfide bond in alpha-lactalbumin: implications for formation of the molten globule state. Biochimica Et Biophysica Acta. 1476: 9-19. PMID 10606762 DOI: 10.1016/S0167-4838(99)00219-8 |
0.823 |
|
| 2000 |
Vugmeyster L, Kroenke CD, Picart F, Palmer AG, Raleigh DP. 15N R(1ρ) measurements allow the determination of ultrafast protein folding rates [1] Journal of the American Chemical Society. 122: 5387-5388. DOI: 10.1021/Ja000225+ |
0.665 |
|
| 1999 |
Nilsson MR, Raleigh DP. Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin. Journal of Molecular Biology. 294: 1375-85. PMID 10600392 DOI: 10.1006/Jmbi.1999.3286 |
0.772 |
|
| 1999 |
Demarest SJ, Boice JA, Fairman R, Raleigh DP. Defining the core structure of the alpha-lactalbumin molten globule state. Journal of Molecular Biology. 294: 213-21. PMID 10556040 DOI: 10.1006/Jmbi.1999.3228 |
0.816 |
|
| 1999 |
Spector S, Raleigh DP. Submillisecond folding of the peripheral subunit-binding domain Journal of Molecular Biology. 293: 763-768. PMID 10543965 DOI: 10.1006/Jmbi.1999.3189 |
0.368 |
|
| 1999 |
Demarest SJ, Hua Y, Raleigh DP. Local interactions drive the formation of nonnative structure in the denatured state of human alpha-lactalbumin: a high resolution structural characterization of a peptide model in aqueous solution. Biochemistry. 38: 7380-7. PMID 10353850 DOI: 10.1021/Bi990320Z |
0.739 |
|
| 1999 |
Luisi DL, Kuhlman B, Sideras K, Evans PA, Raleigh DP. Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9. Journal of Molecular Biology. 289: 167-74. PMID 10339414 DOI: 10.1006/Jmbi.1999.2742 |
0.837 |
|
| 1999 |
Sato S, Kuhlman B, Wu WJ, Raleigh DP. Folding of the multidomain ribosomal protein L9: the two domains fold independently with remarkably different rates. Biochemistry. 38: 5643-50. PMID 10220353 DOI: 10.1021/Bi9830314 |
0.568 |
|
| 1999 |
Kuhlman B, Luisi DL, Young P, Raleigh DP. pKa values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions. Biochemistry. 38: 4896-903. PMID 10200179 DOI: 10.1021/Bi982931H |
0.815 |
|
| 1999 |
Spector S, Young P, Raleigh DP. Nativelike structure and stability in a truncation mutant of a protein minidomain: The peripheral subunit-binding domain Biochemistry. 38: 4128-4136. PMID 10194328 DOI: 10.1021/Bi982915K |
0.441 |
|
| 1999 |
Luisi DL, Wu WJ, Raleigh DP. Conformational analysis of a set of peptides corresponding to the entire primary sequence of the N-terminal domain of the ribosomal protein L9: evidence for stable native-like secondary structure in the unfolded state. Journal of Molecular Biology. 287: 395-407. PMID 10080901 DOI: 10.1006/Jmbi.1999.2595 |
0.835 |
|
| 1999 |
Spector S, Rosconi M, Raleigh DP. Conformational analysis of peptide fragments derived from the peripheral subunit-binding domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: Evidence for nonrandom structure in the unfolded state Biopolymers. 49: 29-40. PMID 10070261 DOI: 10.1002/(Sici)1097-0282(199901)49:1<29::Aid-Bip4>3.0.Co;2-7 |
0.46 |
|
| 1999 |
Moriarty DF, Raleigh DP. Effects of sequential proline substitutions on amyloid formation by human amylin20-29 Biochemistry. 38: 1811-1818. PMID 10026261 DOI: 10.1021/Bi981658G |
0.826 |
|
| 1998 |
Kuhlman B, Luisi DL, Evans PA, Raleigh DP. Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9. Journal of Molecular Biology. 284: 1661-70. PMID 9878377 DOI: 10.1006/Jmbi.1998.2246 |
0.812 |
|
| 1998 |
Kuhlman B, Raleigh DP. Global analysis of the thermal and chemical denaturation of the N-terminal domain of the ribosomal protein L9 in H2O and D2O. Determination of the thermodynamic parameters, deltaH(o), deltaS(o), and deltaC(o)p and evaluation of solvent isotope effects. Protein Science : a Publication of the Protein Society. 7: 2405-12. PMID 9828007 DOI: 10.1002/Pro.5560071118 |
0.319 |
|
| 1998 |
Demarest SJ, Fairman R, Raleigh DP. Peptide models of local and long-range interactions in the molten globule state of human alpha-lactalbumin. Journal of Molecular Biology. 283: 279-91. PMID 9761690 DOI: 10.1006/Jmbi.1998.2099 |
0.801 |
|
| 1998 |
Vugmeyster L, Kuhlman B, Raleigh DP. Amide proton exchange measurements as a probe of the stability and dynamics of the N-terminal domain of the ribosomal protein L9: comparison with the intact protein. Protein Science : a Publication of the Protein Society. 7: 1994-7. PMID 9761480 DOI: 10.1002/Pro.5560070915 |
0.691 |
|
| 1998 |
Hua Y, Raleigh DP. Conformational analysis of the interdomain linker of the central homology region of chloroplast initiation factor IF3 supports a structural model of two compact domains connected by a flexible tether Febs Letters. 433: 153-156. PMID 9738951 DOI: 10.1016/S0014-5793(98)00901-6 |
0.395 |
|
| 1998 |
Hua Y, Raleigh DP. On the global architecture of initiation factor IF3: A comparative study of the linker regions from the Escherichia coli protein and the Bacillus stearothermophilus protein Journal of Molecular Biology. 278: 871-878. PMID 9614948 DOI: 10.1006/Jmbi.1998.1736 |
0.462 |
|
| 1998 |
Moriarty DF, Vagts S, Raleigh DP. A role for the C-terminus of calcitonin in aggregation and gel formation. A comparative study of C-terminal fragments of human and salmon calcitonin Biochemical and Biophysical Research Communications. 245: 344-348. PMID 9571152 DOI: 10.1006/Bbrc.1998.8425 |
0.811 |
|
| 1998 |
Wu WJ, Raleigh DP. Local control of peptide conformation: Stabilization of cis proline peptide bonds by aromatic proline interactions Biopolymers. 45: 381-394. PMID 9530015 DOI: 10.1002/(Sici)1097-0282(19980415)45:5<381::Aid-Bip6>3.0.Co;2-H |
0.398 |
|
| 1998 |
Spector S, Kuhlman B, Fairman R, Wong E, Boice JA, Raleigh DP. Cooperative folding of a protein mini domain: the peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex. Journal of Molecular Biology. 276: 479-89. PMID 9512717 DOI: 10.1006/Jmbi.1997.1522 |
0.699 |
|
| 1998 |
Kuhlman B, Boice JA, Fairman R, Raleigh DP. Structure and stability of the N-terminal domain of the ribosomal protein L9: evidence for rapid two-state folding. Biochemistry. 37: 1025-32. PMID 9454593 DOI: 10.1021/Bi972352X |
0.691 |
|
| 1998 |
Wu WJ, Raleigh DP. Conformational Heterogeneity about Pipecolic Acid Peptide Bonds: Conformational, Thermodynamics, and Kinetic Aspects Journal of Organic Chemistry. 63: 6689-6698. DOI: 10.1021/Jo981340U |
0.371 |
|
| 1998 |
Wu WJ, Tonge PJ, Raleigh DP. Stereospecific 1H and 13C NMR assignments of crotonyl CoA and hexadienoyl CoA: Conformational analysis and comparison with protein-CoA complexes Journal of the American Chemical Society. 120: 9988-9994. DOI: 10.1021/Ja982243L |
0.338 |
|
| 1997 |
Hubbard JAM, Raleigh DP, Bonnerjea JR, Dobson CM. Identification of the epitopes of calcitonin gene-related peptide (CGRP) for two anti-CGRP monoclonal antibodies by 2D NMR Protein Science. 6: 1945-1952. PMID 9300494 DOI: 10.1002/Pro.5560060915 |
0.511 |
|
| 1997 |
Kuhlman B, Yang HY, Boice JA, Fairman R, Raleigh DP. An exceptionally stable helix from the ribosomal protein L9: implications for protein folding and stability. Journal of Molecular Biology. 270: 640-7. PMID 9245593 DOI: 10.1006/Jmbi.1997.1146 |
0.695 |
|
| 1997 |
Kuhlman B, Boice JA, Wu WJ, Fairman R, Raleigh DP. Calcium binding peptides from alpha-lactalbumin: implications for protein folding and stability. Biochemistry. 36: 4607-15. PMID 9109670 DOI: 10.1021/Bi962901J |
0.639 |
|
| 1997 |
Wu WJ, Anderson VE, Raleigh DP, Tonge PJ. Structure of hexadienoyl-coa bound to enoyl-coa hydratase determined by transferred nuclear overhauser effect measurements: Mechanistic predictions based on the x-ray structure of 4-(chlorobenzoyl)-coa dehalogenaset Biochemistry. 36: 2211-2220. PMID 9047322 DOI: 10.1021/Bi962549+ |
0.339 |
|
| 1996 |
Betz SF, Raleigh DP, DeGrado WF, Lovejoy B, Anderson D, Ogihara N, Eisenberg D. Crystallization of a designed peptide from a molten globule ensemble Folding and Design. 1: 57-64. PMID 9079364 DOI: 10.1016/S1359-0278(96)00012-0 |
0.762 |
|
| 1996 |
Miller WT, Raleigh DP. Protein folding: From basic science to biotechnology Genetic Analysis - Biomolecular Engineering. 12: 169-172. PMID 8740832 DOI: 10.1016/S1050-3862(96)80002-7 |
0.345 |
|
| 1995 |
Betz SF, Raleigh DP, DeGrado WF, Lovejoy B, Anderson D, Ogihara N, Eisenberg D. Crystallization of a designed peptide from a molten globule ensemble. Folding & Design. 1: 57-64. PMID 9162140 |
0.335 |
|
| 1995 |
O'Neil KT, Hoess RH, Raleigh DP, DeGrado WF. Thermodynamic genetics of the folding of the B1 immunoglobulin-binding domain from streptococcal protein G Proteins: Structure, Function and Genetics. 21: 11-21. PMID 7716165 DOI: 10.1002/Prot.340210103 |
0.533 |
|
| 1995 |
Raleigh DP, Betz SF, DeGrado WF. A de novo designed protein mimics the native state of natural proteins Journal of the American Chemical Society. 117: 7558-7559. DOI: 10.1021/Ja00133A035 |
0.733 |
|
| 1993 |
O'Connell JP, Kelly SM, Raleigh DP, Hubbard JA, Price NC, Dobson CM, Smith BJ. On the role of the C-terminus of alpha-calcitonin-gene-related peptide (alpha CGRP). The structure of des-phenylalaninamide37-alpha CGRP and its interaction with the CGRP receptor. The Biochemical Journal. 291: 205-10. PMID 8385932 DOI: 10.1042/Bj2910205 |
0.475 |
|
| 1993 |
Betz SF, Raleigh DP, DeGrado WF. De novo protein design: from molten globules to native-like states. Current opinion in structural biology 1993, 3:601-610 Current Opinion in Structural Biology. 3: 601-610. DOI: 10.1016/0959-440X(93)90090-8 |
0.741 |
|
| 1992 |
Raleigh DP, Evans PA, Pitkeathly M, Dobson CM. A peptide model for proline isomerism in the unfolded state of staphylococcal nuclease Journal of Molecular Biology. 228: 338-342. PMID 1453444 DOI: 10.1016/0022-2836(92)90822-2 |
0.522 |
|
| 1992 |
Raleigh DP, DeGrado WF. A de novo designed protein shows a thermally induced transition from a native to a molten globule-like state Journal of the American Chemical Society. 114: 10079-10081. DOI: 10.1021/Ja00051A061 |
0.508 |
|
| 1992 |
Raleigh DP, Grey CP, Soffe N, Dobson CM. Multiple-frequency decoupling in magic-angle-spinning NMR of paramagnetic solids Journal of Magnetic Resonance (1969). 97: 162-170. DOI: 10.1016/0022-2364(92)90244-2 |
0.393 |
|
| 1991 |
Cheetham JC, Redfield C, Griest RE, Raleigh DP, Dobson CM, Rees AR. Use of two-dimensional 1H nuclear magnetic resonance to study high-affinity antibody-peptide interactions Methods in Enzymology. 203: 202-228. PMID 1762556 DOI: 10.1016/0076-6879(91)03011-5 |
0.492 |
|
| 1991 |
Cheetham JC, Raleigh DP, Griest RE, Redfield C, Dobson CM, Rees AR. Antigen mobility in the combining site of an anti-peptide antibody Proceedings of the National Academy of Sciences of the United States of America. 88: 7968-7972. PMID 1716767 DOI: 10.1073/Pnas.88.18.7968 |
0.504 |
|
| 1991 |
DeGrado WF, Raleigh DP, Handel T. De novo protein design: what are we learning? Current Opinion in Structural Biology. 1: 984-993. DOI: 10.1016/0959-440X(91)90095-B |
0.509 |
|
| 1991 |
Raleigh DP, Olejniczak ET, Griffin RG. Theory of combined TOSS-multiple-pulse-scaling experiments Journal of Magnetic Resonance (1969). 93: 472-484. DOI: 10.1016/0022-2364(91)90076-6 |
0.428 |
|
| 1990 |
Herzfeld J, Das Gupta SK, Farrar MR, Harbison GS, McDermott AE, Pelletier SL, Raleigh DP, Smith SO, Winkel C, Lugtenburg J. Solid-state 13C NMR study of tyrosine protonation in dark-adapted bacteriorhodopsin. Biochemistry. 29: 5567-74. PMID 2167129 DOI: 10.1021/Bi00475A022 |
0.588 |
|
| 1990 |
Levitt MH, Raleigh DP, Creuzet F, Griffin RG. Theory and simulations of homonuclear spin pair systems in rotating solids The Journal of Chemical Physics. 92: 6347-6364. DOI: 10.1063/1.458314 |
0.596 |
|
| 1990 |
Kolbert A, Raleigh D, Griffin R, Levitt M. Spinning sideband enhancement using a rotary resonant field Journal of Magnetic Resonance (1969). 89: 133-138. DOI: 10.1016/0022-2364(90)90167-8 |
0.567 |
|
| 1990 |
Raleigh DP, Kolbert AC, Griffin RG. The effect of experimental imperfections on TOSS spectra Journal of Magnetic Resonance (1969). 89: 1-9. DOI: 10.1016/0022-2364(90)90156-4 |
0.423 |
|
| 1989 |
Kolbert AC, Raleigh DP, Levitt MH, Griffin RG. Two‐dimensional spin–echo nuclear magnetic resonance in rotating solids The Journal of Chemical Physics. 90: 679-689. DOI: 10.1063/1.456147 |
0.584 |
|
| 1989 |
Raleigh DP, Creuzet F, Das Gupta SK, Levitt MH, Griffin RG. Measurement of internuclear distances in polycrystalline solids. Rotationally enhanced transfer of nuclear spin magnetization Journal of the American Chemical Society. 111: 4502-4503. DOI: 10.1021/Ja00194A057 |
0.584 |
|
| 1989 |
Kolbert A, Raleigh D, Griffin R. π pulses and echo formation in magic-angle-spinning NMR Journal of Magnetic Resonance (1969). 82: 483-491. DOI: 10.1016/0022-2364(89)90211-4 |
0.422 |
|
| 1989 |
Raleigh D, Olejniczak E, Griffin R. Broadband pulses for excitation and inversion in I = 1 systems Journal of Magnetic Resonance (1969). 81: 455-463. DOI: 10.1016/0022-2364(89)90081-4 |
0.41 |
|
| 1988 |
Raleigh DP, Olejniczak ET, Griffin RG. Multiple‐pulse NMR in inhomogeneously broadened rotating solids: Theory of sideband suppression experiments The Journal of Chemical Physics. 89: 1333-1350. DOI: 10.1063/1.455185 |
0.445 |
|
| 1988 |
Raleigh DP, Kolbert AC, Oas TG, Levitt MH, Griffin RG. Enhancement of the effect of small anisotropies in magic-angle spinning nuclear magnetic resonance Journal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases. 84: 3691-3711. DOI: 10.1039/F19888403691 |
0.719 |
|
| 1988 |
Raleigh D, Levitt M, Griffin R. Rotational resonance in solid state NMR Chemical Physics Letters. 146: 71-76. DOI: 10.1016/0009-2614(88)85051-6 |
0.593 |
|
| 1988 |
Raleigh D, Kolbert A, Levitt M, Griffin R. Techniques for the Measurement of Small Anisotropies in Magic Angle Spinning NMR Spectra Israel Journal of Chemistry. 28: 263-269. DOI: 10.1002/Ijch.198800038 |
0.582 |
|
| 1987 |
Smith SO, Palings I, Copié V, Raleigh DP, Courtin J, Pardoen JA, Lugtenburg J, Mathies RA, Griffin RG. Low-temperature solid-state 13C NMR studies of the retinal chromophore in rhodopsin. Biochemistry. 26: 1606-11. PMID 3593680 DOI: 10.1021/Bi00380A018 |
0.696 |
|
| 1987 |
Raleigh DP, Olejniczak ET, Vega S, Griffin RG. An analysis of sideband suppression techniques in magic-angle sample spinning NMR Journal of Magnetic Resonance (1969). 72: 238-250. DOI: 10.1016/0022-2364(87)90286-1 |
0.442 |
|
| 1987 |
Raleigh DP, Harbison GS, Neiss TG, Roberts JE, Griffin RG. Homonuclear J-couplings and rotationally induced sideband enhancements in NMR spectra of rotating solids Chemical Physics Letters. 138: 285-290. DOI: 10.1016/0009-2614(87)80385-8 |
0.44 |
|
| 1986 |
Schmidt A, Smith SO, Raleigh DP, Roberts JE, Griffin RG, Vega S. Chemical exchange effects in the NMR spectra of rotating solids The Journal of Chemical Physics. 85: 4248-4253. DOI: 10.1063/1.451796 |
0.443 |
|
| 1986 |
Siminovitch DJ, Raleigh DP, Olejniczak ET, Griffin RG. Composite pulse excitation in quadrupole echo spectroscopy The Journal of Chemical Physics. 84: 2556-2565. DOI: 10.1063/1.450325 |
0.416 |
|
| 1985 |
Harbison GS, Raleigh DP, Herzfeld J, Griffin RG. High-field 2D exchange spectroscopy in rotating solids Journal of Magnetic Resonance (1969). 64: 284-295. DOI: 10.1016/0022-2364(85)90352-X |
0.452 |
|
| 1985 |
Menger E, Raleigh D, Griffin R. Off-axis sample spinning in the slow-spinning regime Journal of Magnetic Resonance (1969). 63: 579-582. DOI: 10.1016/0022-2364(85)90247-1 |
0.433 |
|
| 1985 |
RALEIGH DP, OLEJNICZAK ET, VEGA S, GRIFFIN RG. ChemInform Abstract: SPECTRAL SIMPLIFICATION AND IMPROVED SENSITIVITY IN MAGIC ANGLE SAMPLE SPINNING NMR Chemischer Informationsdienst. 16. DOI: 10.1002/Chin.198517046 |
0.422 |
|
| 1984 |
Raleigh DP, Olejniczak ET, Vega S, Griffin RG. Spectral simplification and improved sensitivity in magic angle sample spinning NMR Journal of the American Chemical Society. 106: 8302-8303. DOI: 10.1021/Ja00338A054 |
0.41 |
|
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