Year |
Citation |
Score |
2020 |
Wetzel R. Exploding the Repeat Length Paradigm while Exploring Amyloid Toxicity in Huntington's Disease. Accounts of Chemical Research. 53: 2347-2357. PMID 32975927 DOI: 10.1021/acs.accounts.0c00450 |
0.401 |
|
2018 |
Drombosky KW, Rode S, Kodali R, Jacob TC, Palladino MJ, Wetzel R. Mutational analysis implicates the amyloid fibril as the toxic entity in Huntington's disease. Neurobiology of Disease. PMID 30171891 DOI: 10.1016/J.Nbd.2018.08.019 |
0.487 |
|
2018 |
Wetzel R, Chemuru S, Misra P, Kodali R, Mukherjee S, Kar K. An Aggregate Weight-Normalized Thioflavin-T Measurement Scale for Characterizing Polymorphic Amyloids and Assembly Intermediates. Methods in Molecular Biology (Clifton, N.J.). 1777: 121-144. PMID 29744831 DOI: 10.1007/978-1-4939-7811-3_6 |
0.461 |
|
2017 |
Lin HK, Boatz JC, Krabbendam IE, Kodali R, Hou Z, Wetzel R, Dolga AM, Poirier MA, van der Wel PCA. Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core. Nature Communications. 8: 15462. PMID 28537272 DOI: 10.1038/Ncomms15462 |
0.467 |
|
2016 |
Kar K, Baker MA, Lengyel GA, Hoop CL, Kodali R, Byeon IJ, Horne WS, van der Wel PC, Wetzel R. Backbone engineering within a latent β-hairpin structure to design inhibitors of polyglutamine amyloid formation. Journal of Molecular Biology. PMID 27986569 DOI: 10.1016/J.Jmb.2016.12.010 |
0.474 |
|
2016 |
Misra P, Kodali R, Chemuru S, Kar K, Wetzel R. Rapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway. Nature Communications. 7: 12419. PMID 27546208 DOI: 10.1038/Ncomms12419 |
0.501 |
|
2016 |
Sahoo B, Arduini I, Drombosky KW, Kodali R, Sanders LH, Greenamyre JT, Wetzel R. Folding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer. Plos One. 11: e0155747. PMID 27271685 DOI: 10.1371/Journal.Pone.0155747 |
0.437 |
|
2016 |
Hoop CL, Lin HK, Kar K, Magyarfalvi G, Lamley JM, Boatz JC, Mandal A, Lewandowski JR, Wetzel R, van der Wel PC. Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core. Proceedings of the National Academy of Sciences of the United States of America. PMID 26831073 DOI: 10.1073/Pnas.1521933113 |
0.479 |
|
2016 |
Sahoo B, Drombosky KW, Wetzel R. Fluorescence Correlation Spectroscopy: A Tool to Study Protein Oligomerization and Aggregation In Vitro and In Vivo. Methods in Molecular Biology (Clifton, N.J.). 1345: 67-87. PMID 26453206 DOI: 10.1007/978-1-4939-2978-8_5 |
0.407 |
|
2016 |
Chemuru S, Kodali R, Wetzel R. C-Terminal Threonine Reduces Aβ43 Amyloidogenicity Compared with Aβ42. Journal of Molecular Biology. 428: 274-291. PMID 26122432 DOI: 10.1016/J.Jmb.2015.06.008 |
0.486 |
|
2015 |
Roland BP, Amrich CG, Kammerer CJ, Stuchul KA, Larsen SB, Rode S, Aslam AA, Heroux A, Wetzel R, VanDemark AP, Palladino MJ. Triosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency. Biochimica Et Biophysica Acta. 1852: 61-9. PMID 25463631 DOI: 10.1016/J.Bbadis.2014.10.010 |
0.313 |
|
2015 |
Hoop CL, Lin H, Kar K, Wetzel R, Wel PCAvd. Huntingtin N-Terminal Fragment Fibrils have a Rigid Amyloid Core Flanked by Non-Amyloid Domains with Increased Dynamics Biophysical Journal. 108: 385-386. DOI: 10.1016/J.Bpj.2014.11.2114 |
0.516 |
|
2014 |
Hoop CL, Lin HK, Kar K, Hou Z, Poirier MA, Wetzel R, van der Wel PC. Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance. Biochemistry. 53: 6653-66. PMID 25280367 DOI: 10.1021/Bi501010Q |
0.448 |
|
2014 |
Sahoo B, Singer D, Kodali R, Zuchner T, Wetzel R. Aggregation behavior of chemically synthesized, full-length huntingtin exon1. Biochemistry. 53: 3897-907. PMID 24921664 DOI: 10.1021/Bi500300C |
0.493 |
|
2014 |
Usmani SM, Zirafi O, Müller JA, Sandi-Monroy NL, Yadav JK, Meier C, Weil T, Roan NR, Greene WC, Walther P, Nilsson KP, Hammarström P, Wetzel R, Pilcher CD, Gagsteiger F, et al. Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen. Nature Communications. 5: 3508. PMID 24691351 DOI: 10.1038/Ncomms4508 |
0.379 |
|
2014 |
Landrum E, Wetzel R. Biophysical underpinnings of the repeat length dependence of polyglutamine amyloid formation. Journal of Biological Chemistry. 289: 10254-10260. PMID 24596088 DOI: 10.1074/Jbc.C114.552943 |
0.456 |
|
2014 |
Chemuru S, Kodali R, Wetzel R. Improved chemical synthesis of hydrophobic Aβ peptides using addition of C-terminal lysines later removed by carboxypeptidase B. Biopolymers. 102: 206-221. PMID 24488729 DOI: 10.1002/Bip.22470 |
0.434 |
|
2014 |
Kar K, Arduini I, Drombosky KW, van der Wel PC, Wetzel R. D-polyglutamine amyloid recruits L-polyglutamine monomers and kills cells. Journal of Molecular Biology. 426: 816-29. PMID 24291210 DOI: 10.1016/J.Jmb.2013.11.019 |
0.445 |
|
2014 |
Hoop C, Kar K, Wetzel R, Wel Pvd, Lin H, Poirier M, Boatz J. Solid-state NMR chemical shifts of amyloid-like fibrils formed by huntingtin exon 1 with a 44-residue polyQ domain. Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27045 |
0.389 |
|
2014 |
Hoop C, Kar K, Wetzel R, Wel Pvd. Solid-state NMR chemical shifts of amyloid-like fibrils formed by huntingtin N-terminal fragments (httNTQ30P10K2) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25146 |
0.392 |
|
2014 |
Rode S, Drombosky K, Wetzel R. Towards a Test of the Aggregation Hypothesis in Huntington's Disease using β-Hairpin Enhancing Motifs Biophysical Journal. 106: 672. DOI: 10.1016/J.Bpj.2013.11.3721 |
0.503 |
|
2013 |
Roland BP, Kodali R, Mishra R, Wetzel R. A serendipitous survey of prediction algorithms for amyloidogenicity. Biopolymers. 100: 780-9. PMID 23893755 DOI: 10.1002/Bip.22305 |
0.462 |
|
2013 |
Kurouski D, Kar K, Wetzel R, Dukor RK, Lednev IK, Nafie LA. Levels of supramolecular chirality of polyglutamine aggregates revealed by vibrational circular dichroism. Febs Letters. 587: 1638-43. PMID 23583713 DOI: 10.1016/J.Febslet.2013.03.038 |
0.44 |
|
2013 |
Kar K, Hoop CL, Drombosky KW, Baker MA, Kodali R, Arduini I, van der Wel PC, Horne WS, Wetzel R. β-hairpin-mediated nucleation of polyglutamine amyloid formation. Journal of Molecular Biology. 425: 1183-97. PMID 23353826 DOI: 10.1016/J.Jmb.2013.01.016 |
0.463 |
|
2013 |
Hoop CL, Mishra R, Kar K, Kodali R, Wetzel R, Wel PCAvd. Structural and Motional Investigations of Polyglutamine-Containing Amyloid Fibrils by Magic-Angle-Spinning Solid-State NMR Biophysical Journal. 104: 181. DOI: 10.1016/J.Bpj.2012.11.1017 |
0.502 |
|
2012 |
Mishra R, Hoop CL, Kodali R, Sahoo B, van der Wel PC, Wetzel R. Serine phosphorylation suppresses huntingtin amyloid accumulation by altering protein aggregation properties. Journal of Molecular Biology. 424: 1-14. PMID 22999956 DOI: 10.1016/J.Jmb.2012.09.011 |
0.524 |
|
2012 |
Jayaraman M, Mishra R, Kodali R, Thakur AK, Koharudin LMI, Gronenborn AM, Wetzel R. Kinetically competing huntingtin aggregation pathways control amyloid polymorphism and properties Biochemistry. 51: 2706-2716. PMID 22432740 DOI: 10.1021/Bi3000929 |
0.476 |
|
2012 |
Wetzel R. Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence. Journal of Molecular Biology. 421: 466-490. PMID 22306404 DOI: 10.1016/J.Jmb.2012.01.030 |
0.39 |
|
2012 |
Mishra R, Jayaraman M, Roland BP, Landrum E, Fullam T, Kodali R, Thakur AK, Arduini I, Wetzel R. Inhibiting the nucleation of amyloid structure in a huntingtin fragment by targeting α-helix-rich oligomeric intermediates. Journal of Molecular Biology. 415: 900-17. PMID 22178478 DOI: 10.1016/J.Jmb.2011.12.011 |
0.468 |
|
2012 |
Jayaraman M, Kodali R, Sahoo B, Thakur AK, Mayasundari A, Mishra R, Peterson CB, Wetzel R. Slow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments. Journal of Molecular Biology. 415: 881-99. PMID 22178474 DOI: 10.1016/J.Jmb.2011.12.010 |
0.503 |
|
2012 |
Mishra R, Kodali R, Roland B, Wetzel RB. Role of (httNT) α-Helix Formation in Huntingtin N-Terminal Fragment Aggregation Biophysical Journal. 102: 254a-255a. DOI: 10.1016/J.Bpj.2011.11.1403 |
0.473 |
|
2011 |
Sivanandam VN, Jayaraman M, Hoop CL, Kodali R, Wetzel R, van der Wel PC. The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils. Journal of the American Chemical Society. 133: 4558-66. PMID 21381744 DOI: 10.1021/Ja110715F |
0.521 |
|
2011 |
Kar K, Jayaraman M, Sahoo B, Kodali R, Wetzel R. Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent. Nature Structural & Molecular Biology. 18: 328-36. PMID 21317897 DOI: 10.1038/Nsmb.1992 |
0.382 |
|
2011 |
Jayaraman M, Thakur AK, Kar K, Kodali R, Wetzel R. Assays for studying nucleated aggregation of polyglutamine proteins. Methods (San Diego, Calif.). 53: 246-54. PMID 21232603 DOI: 10.1016/J.Ymeth.2011.01.001 |
0.464 |
|
2011 |
Fitz N, Chronican A, Kodali R, Wetzel R, Lefterov I, Koldamova R. ABCA1 deficiency decreases Amyloid clearance and increases Amyloid aggregation in Alzheimer's disease mouse model Alzheimers & Dementia. 7. DOI: 10.1016/J.Jalz.2011.05.2032 |
0.448 |
|
2010 |
Lefterov I, Fitz NF, Cronican AA, Fogg A, Lefterov P, Kodali R, Wetzel R, Koldamova R. Apolipoprotein A-I deficiency increases cerebral amyloid angiopathy and cognitive deficits in APP/PS1DeltaE9 mice. The Journal of Biological Chemistry. 285: 36945-57. PMID 20739292 DOI: 10.1074/Jbc.M110.127738 |
0.387 |
|
2010 |
Kodali R, Williams AD, Chemuru S, Wetzel R. Abeta(1-40) forms five distinct amyloid structures whose beta-sheet contents and fibril stabilities are correlated. Journal of Molecular Biology. 401: 503-17. PMID 20600131 DOI: 10.1016/J.Jmb.2010.06.023 |
0.498 |
|
2010 |
Popova LA, Kodali R, Wetzel R, Lednev IK. Structural variations in the cross-beta core of amyloid beta fibrils revealed by deep UV resonance Raman spectroscopy. Journal of the American Chemical Society. 132: 6324-8. PMID 20405832 DOI: 10.1021/Ja909074J |
0.441 |
|
2010 |
Isas JM, Luibl V, Johnson LV, Kayed R, Wetzel R, Glabe CG, Langen R, Chen J. Soluble and mature amyloid fibrils in drusen deposits. Investigative Ophthalmology & Visual Science. 51: 1304-10. PMID 19892876 DOI: 10.1167/Iovs.09-4207 |
0.408 |
|
2010 |
Mishra R, Kodali R, Wetzel R. Amino Acid Modifications in the N terminal Sequence of htt Exon-1 Modulate In Vitro Aggregation Biophysical Journal. 98. DOI: 10.1016/J.Bpj.2009.12.1382 |
0.454 |
|
2009 |
Gu X, Greiner ER, Mishra R, Kodali R, Osmand A, Finkbeiner S, Steffan JS, Thompson LM, Wetzel R, Yang XW. Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice. Neuron. 64: 828-40. PMID 20064390 DOI: 10.1016/J.Neuron.2009.11.020 |
0.406 |
|
2009 |
Jayaraman M, Kodali R, Wetzel R. The impact of ataxin-1-like histidine insertions on polyglutamine aggregation. Protein Engineering Design & Selection. 22: 469-478. PMID 19541676 DOI: 10.1093/Protein/Gzp023 |
0.486 |
|
2009 |
Gardberg A, Dice L, Pridgen K, Ko J, Patterson P, Ou S, Wetzel R, Dealwis C. Structures of Aβ-related peptide-monoclonal antibody complexes Biochemistry. 48: 5210-5217. PMID 19385664 DOI: 10.1021/Bi9001216 |
0.429 |
|
2009 |
Thakur AK, Jayaraman M, Mishra R, Thakur M, Chellgren VM, Byeon IJ, Anjum DH, Kodali R, Creamer TP, Conway JF, Gronenborn AM, Wetzel R. Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. Nature Structural & Molecular Biology. 16: 380-9. PMID 19270701 DOI: 10.1038/Nsmb.1570 |
0.498 |
|
2009 |
Wood SJ, Wetzel R. Novel cyclization chemistry especially suited for biologically derived, unprotected peptides. International Journal of Peptide and Protein Research. 39: 533-539. PMID 1399273 DOI: 10.1111/J.1399-3011.1992.Tb00285.X |
0.346 |
|
2007 |
Larsen P, Nielsen JL, Dueholm MS, Wetzel R, Otzen D, Nielsen PH. Amyloid adhesins are abundant in natural biofilms Environmental Microbiology. 9: 3077-3090. PMID 17991035 DOI: 10.1111/J.1462-2920.2007.01418.X |
0.417 |
|
2007 |
Ignatova Z, Thakur AK, Wetzel R, Gierasch LM. In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence. The Journal of Biological Chemistry. 282: 36736-43. PMID 17942400 DOI: 10.1074/Jbc.M703682200 |
0.475 |
|
2007 |
Gardberg AS, Dice LT, Ou S, Rich RL, Helmbrecht E, Ko J, Wetzel R, Myszka DG, Patterson PH, Dealwis C. Molecular basis for passive immunotherapy of Alzheimer's disease. Proceedings of the National Academy of Sciences of the United States of America. 104: 15659-64. PMID 17895381 DOI: 10.1073/Pnas.0705888104 |
0.46 |
|
2007 |
Kodali R, Wetzel R. Polymorphism in the intermediates and products of amyloid assembly. Current Opinion in Structural Biology. 17: 48-57. PMID 17251001 DOI: 10.1016/J.Sbi.2007.01.007 |
0.444 |
|
2007 |
Wetzel R, Shivaprasad S, Williams AD. Plasticity of amyloid fibrils. Biochemistry. 46: 1-10. PMID 17198370 DOI: 10.1021/Bi0620959 |
0.457 |
|
2007 |
Chen M, Cook KD, Kheterpal I, Wetzel R. A triaxial probe for on-line proteolysis coupled with hydrogen/deuterium exchange-electrospray mass spectrometry. Journal of the American Society For Mass Spectrometry. 18: 208-17. PMID 17074502 DOI: 10.1016/J.Jasms.2006.09.011 |
0.336 |
|
2006 |
Beal MF, Bossy-Wetzel E, Finkbeiner S, Fiskum G, Giasson B, Johnson C, Khachaturian ZS, Lee VM, Nicholls D, Reddy H, Reynolds I, Teplow DB, Thal LJ, Trojanowski JQ, Walsh DM, ... Wetzel R, et al. Common threads in neurodegenerative disorders of aging. Alzheimer's & Dementia : the Journal of the Alzheimer's Association. 2: 322-6. PMID 19595906 DOI: 10.1016/J.Jalz.2006.08.008 |
0.346 |
|
2006 |
Crick SL, Jayaraman M, Frieden C, Wetzel R, Pappu RV. Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions Proceedings of the National Academy of Sciences of the United States of America. 103: 16764-16769. PMID 17075061 DOI: 10.1073/Pnas.0608175103 |
0.379 |
|
2006 |
Osmand AP, Berthelier V, Wetzel R. Imaging polyglutamine deposits in brain tissue. Methods in Enzymology. 412: 106-122. PMID 17046655 DOI: 10.1016/S0076-6879(06)12008-X |
0.445 |
|
2006 |
Berthelier V, Wetzel R. Screening for modulators of aggregation with a microplate elongation assay. Methods in Enzymology. 413: 313-325. PMID 17046403 DOI: 10.1016/S0076-6879(06)13016-5 |
0.462 |
|
2006 |
Shivaprasad S, Wetzel R. Analysis of Amyloid Fibril Structure by Scanning Cysteine Mutagenesis Methods in Enzymology. 413: 182-198. PMID 17046397 DOI: 10.1016/S0076-6879(06)13010-4 |
0.473 |
|
2006 |
Kheterpal I, Cook KD, Wetzel R. Hydrogen/deuterium exchange mass spectrometry analysis of protein aggregates. Methods in Enzymology. 413: 140-66. PMID 17046395 DOI: 10.1016/S0076-6879(06)13008-6 |
0.49 |
|
2006 |
O'Nuallain B, Thakur AK, Williams AD, Bhattacharyya AM, Chen S, Thiagarajan G, Wetzel R. Kinetics and thermodynamics of amyloid assembly using a high-performance liquid chromatography-based sedimentation assay. Methods in Enzymology. 413: 34-74. PMID 17046390 DOI: 10.1016/S0076-6879(06)13003-7 |
0.498 |
|
2006 |
Nguyen HP, Kobbe P, Rahne H, Wörpel T, Jäger B, Stephan M, Pabst R, Holzmann C, Riess O, Korr H, Kántor O, Petrasch-Parwez E, Wetzel R, Osmand A, von Hörsten S. Behavioral abnormalities precede neuropathological markers in rats transgenic for Huntington's disease. Human Molecular Genetics. 15: 3177-94. PMID 16984963 DOI: 10.1093/Hmg/Ddl394 |
0.357 |
|
2006 |
Wetzel R. Kinetics and thermodynamics of amyloid fibril assembly. Accounts of Chemical Research. 39: 671-679. PMID 16981684 DOI: 10.1021/Ar050069H |
0.511 |
|
2006 |
Kheterpal I, Wetzel R. Hydrogen/deuterium exchange mass spectrometry--a window into amyloid structure. Accounts of Chemical Research. 39: 584-593. PMID 16981674 DOI: 10.1021/Ar050057W |
0.415 |
|
2006 |
Wetzel R. Amyloid FibrilsCommon Threads in the Natural History of Proteins Accounts of Chemical Research. 39: 567-567. PMID 16981671 DOI: 10.1021/Ar0681934 |
0.411 |
|
2006 |
Slepko N, Bhattacharyya AM, Jackson GR, Steffan JS, Marsh JL, Thompson LM, Wetzel R. Normal-repeat-length polyglutamine peptides accelerate aggregation nucleation and cytotoxicity of expanded polyglutamine proteins. Proceedings of the National Academy of Sciences of the United States of America. 103: 14367-72. PMID 16980414 DOI: 10.1073/Pnas.0602348103 |
0.452 |
|
2006 |
Kheterpal I, Chen M, Cook KD, Wetzel R. Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange--mass spectrometry with on-line proteolytic fragmentation. Journal of Molecular Biology. 361: 785-95. PMID 16875699 DOI: 10.1016/J.Jmb.2006.06.066 |
0.492 |
|
2006 |
Wetzel R. Nucleation of huntingtin aggregation in cells. Nature Chemical Biology. 2: 297-298. PMID 16710335 DOI: 10.1038/Nchembio0606-297 |
0.444 |
|
2006 |
Williams AD, Shivaprasad S, Wetzel R. Alanine scanning mutagenesis of Abeta(1-40) amyloid fibril stability. Journal of Molecular Biology. 357: 1283-94. PMID 16476445 DOI: 10.1016/J.Jmb.2006.01.041 |
0.491 |
|
2006 |
Bhattacharyya A, Thakur AK, Chellgren VM, Thiagarajan G, Williams AD, Chellgren BW, Creamer TP, Wetzel R. Oligoproline effects on polyglutamine conformation and aggregation. Journal of Molecular Biology. 355: 524-35. PMID 16321399 DOI: 10.1016/J.Jmb.2005.10.053 |
0.423 |
|
2006 |
Shivaprasad S, Wetzel R. Scanning Cysteine Mutagenesis Analysis of Aβ-(1-40) Amyloid Fibrils Journal of Biological Chemistry. 281: 993-1000. PMID 16263715 DOI: 10.1074/Jbc.M505091200 |
0.512 |
|
2006 |
Kheterpal I, Chen M, Cook KD, Wetzel R. WITHDRAWN: Erratum to “Structural Differences in Aβ Amyloid Protofibrils and Fibrils Mapped by Hydrogen Exchange-Mass Spectrometry with On-line Proteolytic Fragmentation” [J. Mol. Biol. 361 (2006) 785–795] Journal of Molecular Biology. DOI: 10.1016/J.Jmb.2006.06.087 |
0.375 |
|
2005 |
Bhattacharyya AM, Thakur AK, Wetzel R. polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction. Proceedings of the National Academy of Sciences of the United States of America. 102: 15400-5. PMID 16230628 DOI: 10.1073/Pnas.0501651102 |
0.479 |
|
2005 |
O'Nuallain B, Shivaprasad S, Kheterpal I, Wetzel R. Thermodynamics of Aβ(1−40) Amyloid Fibril Elongation† Biochemistry. 44: 12709-12718. PMID 16171385 DOI: 10.1021/Bi050927H |
0.424 |
|
2005 |
Sharma D, Shinchuk LM, Inouye H, Wetzel R, Kirschner DA. Polyglutamine homopolymers having 8-45 residues form slablike beta-crystallite assemblies. Proteins. 61: 398-411. PMID 16114051 DOI: 10.1002/Prot.20602 |
0.425 |
|
2005 |
Williams AD, Sega M, Chen M, Kheterpal I, Geva M, Berthelier V, Kaleta DT, Cook KD, Wetzel R. Structural properties of Abeta protofibrils stabilized by a small molecule. Proceedings of the National Academy of Sciences of the United States of America. 102: 7115-20. PMID 15883377 DOI: 10.1073/Pnas.0408582102 |
0.482 |
|
2005 |
Whittemore NA, Mishra R, Kheterpal I, Williams AD, Wetzel R, Serpersu EH. Hydrogen-deuterium (H/D) exchange mapping of Abeta 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy. Biochemistry. 44: 4434-41. PMID 15766273 DOI: 10.1021/Bi048292U |
0.409 |
|
2004 |
Shivaprasad S, Wetzel R. An Intersheet Packing Interaction in Aβ Fibrils Mapped by Disulfide Cross-Linking† Biochemistry. 43: 15310-15317. PMID 15581343 DOI: 10.1021/Bi048019S |
0.469 |
|
2004 |
Guo JT, Wetzel R, Xu Y. Molecular modeling of the core of Abeta amyloid fibrils. Proteins. 57: 357-64. PMID 15340923 DOI: 10.1002/Prot.20222 |
0.458 |
|
2004 |
Cannon MJ, Williams AD, Wetzel R, Myszka DG. Kinetic analysis of beta-amyloid fibril elongation. Analytical Biochemistry. 328: 67-75. PMID 15081909 DOI: 10.1016/J.Ab.2004.01.014 |
0.45 |
|
2004 |
Venkatraman P, Wetzel R, Tanaka M, Nukina N, Goldberg AL. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Molecular Cell. 14: 95-104. PMID 15068806 DOI: 10.1016/S1097-2765(04)00151-0 |
0.368 |
|
2004 |
Thakur AK, Yang W, Wetzel R. Inhibition of polyglutamine aggregate cytotoxicity by a structure-based elongation inhibitor. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 18: 923-5. PMID 15001566 DOI: 10.1096/Fj.03-1238Fje |
0.577 |
|
2004 |
O'Nuallain B, Williams AD, Westermark P, Wetzel R. Seeding specificity in amyloid growth induced by heterologous fibrils. The Journal of Biological Chemistry. 279: 17490-9. PMID 14752113 DOI: 10.1074/Jbc.M311300200 |
0.502 |
|
2004 |
Williams AD, Portelius E, Kheterpal I, Guo JT, Cook KD, Xu Y, Wetzel R. Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis. Journal of Molecular Biology. 335: 833-42. PMID 14687578 DOI: 10.1016/J.Jmb.2003.11.008 |
0.502 |
|
2004 |
Shivaprasad S, Wetzel R. P1-226 Mapping Abeta amyloid topology using cysteine mutants Neurobiology of Aging. 25. DOI: 10.1016/S0197-4580(04)80539-6 |
0.354 |
|
2004 |
Kirschner DA, Shinchuk LM, Reixach N, Blondelle SE, Wetzel R, Inouye H. O2-06-01 Protein folding and amyloid formation: studies on poly(L-alanine) and poly(L-glutamine) Neurobiology of Aging. 25: S43. DOI: 10.1016/S0197-4580(04)80143-X |
0.31 |
|
2003 |
Kheterpal I, Lashuel HA, Hartley DM, Walz T, Lansbury PT, Wetzel R. Abeta protofibrils possess a stable core structure resistant to hydrogen exchange. Biochemistry. 42: 14092-8. PMID 14640676 DOI: 10.1021/Bi0357816 |
0.486 |
|
2003 |
Kheterpal I, Wetzel R, Cook KD. Enhanced correction methods for hydrogen exchange-mass spectrometric studies of amyloid fibrils. Protein Science : a Publication of the Protein Society. 12: 635-43. PMID 12592034 DOI: 10.1110/Ps.0225703 |
0.453 |
|
2003 |
Berthelier V, Wetzel R. An Assay for Characterizing In Vitro the Kinetics of Polyglutamine Aggregation Methods of Molecular Biology. 217: 295-304. PMID 12491942 DOI: 10.1385/1-59259-330-5:295 |
0.414 |
|
2002 |
Thakur AK, Wetzel R. Mutational analysis of the structural organization of polyglutamine aggregates. Proceedings of the National Academy of Sciences of the United States of America. 99: 17014-9. PMID 12444250 DOI: 10.1073/Pnas.252523899 |
0.49 |
|
2002 |
Chen S, Ferrone FA, Wetzel R. Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proceedings of the National Academy of Sciences of the United States of America. 99: 11884-9. PMID 12186976 DOI: 10.1073/Pnas.182276099 |
0.477 |
|
2002 |
Wetzel R. Ideas of Order for Amyloid Fibril Structure Structure. 10: 1031-1036. PMID 12176381 DOI: 10.1016/S0969-2126(02)00809-2 |
0.465 |
|
2002 |
Chen S, Berthelier V, Hamilton JB, O'Nuallain B, Wetzel R. Amyloid-like features of polyglutamine aggregates and their assembly kinetics. Biochemistry. 41: 7391-9. PMID 12044172 DOI: 10.1021/Bi011772Q |
0.458 |
|
2002 |
O'Nuallain B, Wetzel R. Conformational Abs recognizing a generic amyloid fibril epitope. Proceedings of the National Academy of Sciences of the United States of America. 99: 1485-1490. PMID 11818542 DOI: 10.1073/Pnas.022662599 |
0.516 |
|
2001 |
Kheterpal I, Williams A, Murphy C, Bledsoe B, Wetzel R. Structural features of the Abeta amyloid fibril elucidated by limited proteolysis. Biochemistry. 40: 11757-67. PMID 11570876 DOI: 10.1021/Bi010805Z |
0.479 |
|
2001 |
Berthelier V, Hamilton JB, Chen S, Wetzel R. A microtiter plate assay for polyglutamine aggregate extension. Analytical Biochemistry. 295: 227-36. PMID 11488626 DOI: 10.1006/Abio.2001.5217 |
0.467 |
|
2001 |
Chen S, Berthelier V, Yang W, Wetzel R. Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity. Journal of Molecular Biology. 311: 173-182. PMID 11469866 DOI: 10.1006/Jmbi.2001.4850 |
0.591 |
|
2001 |
Chen S, Wetzel R. Solubilization and disaggregation of polyglutamine peptides Protein Science. 10: 887-891. PMID 11274480 DOI: 10.1110/Ps.42301 |
0.487 |
|
2000 |
Kheterpal I, Zhou S, Cook KD, Wetzel R. Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange. Proceedings of the National Academy of Sciences of the United States of America. 97: 13597-601. PMID 11087832 DOI: 10.1073/Pnas.250288897 |
0.48 |
|
2000 |
O'Nuallain B, Wetzel R. Denaturation improves the abilities of some globular proteins to inhibit Aβ fibrillogenesis Neurobiology of Aging. 21: 77. DOI: 10.1016/S0197-4580(00)82570-1 |
0.373 |
|
1997 |
Wetzel R. Domain Stability in Immunoglobulin Light Chain Deposition Disorders Advances in Protein Chemistry. 50: 183-242. PMID 9338082 DOI: 10.1016/S0065-3233(08)60322-8 |
0.346 |
|
1996 |
Chan W, Helms LR, Brooks I, Lee G, Ngola S, McNulty D, Maleeff B, Hensley P, Wetzel R. Mutational effects on inclusion body formation in the periplasmic expression of the immunoglobulin VL domain REI. Folding & Design. 1: 77-89. PMID 9079368 DOI: 10.1016/S1359-0278(96)00017-X |
0.378 |
|
1996 |
Wood SJ, Chan W, Wetzel R. An ApoE-Aβ inhibition complex in Aβ fibril extension Chemistry & Biology. 3: 949-956. PMID 8939715 DOI: 10.1016/S1074-5521(96)90183-0 |
0.473 |
|
1996 |
Wood SJ, Chan W, Wetzel R. Seeding of A beta fibril formation is inhibited by all three isotypes of apolipoprotein E. Biochemistry. 35: 12623-12628. PMID 8823200 DOI: 10.1021/Bi961074J |
0.429 |
|
1996 |
Wetzel R. For Protein Misassembly, It's the “I” Decade Cell. 86: 699-702. PMID 8797816 DOI: 10.1016/S0092-8674(00)80143-9 |
0.367 |
|
1996 |
Chan W, Fornwald J, Brawner M, Wetzel R. Native complex formation between apolipoprotein E isoforms and the Alzheimer's disease peptide A beta. Biochemistry. 35: 7123-7130. PMID 8679539 DOI: 10.1021/Bi952852V |
0.448 |
|
1996 |
Helms LR, Wetzel R. Specificity of abnormal assembly in immunoglobulin light chain deposition disease and amyloidosis. Journal of Molecular Biology. 257: 77-86. PMID 8632461 DOI: 10.1006/Jmbi.1996.0148 |
0.456 |
|
1996 |
Wood SJ, MacKenzie L, Maleeff B, Hurle MR, Wetzel R. Selective inhibition of Abeta fibril formation. Journal of Biological Chemistry. 271: 4086-4092. PMID 8626745 DOI: 10.1074/Jbc.271.8.4086 |
0.47 |
|
1996 |
Wood SJ, Maleeff B, Hart T, Wetzel R. Physical, Morphological and Functional Differences between pH 5.8 and 7.4 Aggregates of the Alzheimer's Amyloid Peptide A β Journal of Molecular Biology. 256: 870-877. PMID 8601838 DOI: 10.1006/Jmbi.1996.0133 |
0.401 |
|
1995 |
Helms LR, Wetzel R. Destabilizing loop swaps in the CDRs of an immunoglobulin VL domain. Protein Science. 4: 2073-2081. PMID 8535243 DOI: 10.1002/Pro.5560041012 |
0.31 |
|
1995 |
Wood SJ, Wetzel R, Martin JD, Hurle MR. Prolines and amyloidogenicity in fragments of the Alzheimer's peptide beta/A4. Biochemistry. 34: 724-730. PMID 7827029 DOI: 10.1021/Bi00003A003 |
0.449 |
|
1995 |
Howlett DR, Jennings KH, Lee DC, Clark MS, Brown F, Wetzel R, Wood SJ, Camilleri P, Roberts GW. Aggregation state and neurotoxic properties of Alzheimer beta-amyloid peptide. Neurodegeneration : a Journal For Neurodegenerative Disorders, Neuroprotection, and Neuroregeneration. 4: 23-32. PMID 7600183 DOI: 10.1006/Neur.1995.0003 |
0.445 |
|
1994 |
Hurle MR, Helms LR, Li L, Chan W, Wetzel R. A role for destabilizing amino acid replacements in light-chain amyloidosis Proceedings of the National Academy of Sciences of the United States of America. 91: 5446-5450. PMID 8202506 DOI: 10.1073/Pnas.91.12.5446 |
0.375 |
|
1994 |
Oberg K, Chrunyk BA, Wetzel R, Fink AL. Native-like Secondary Structure in Interleukin-1.beta. Inclusion Bodies by Attenuated Total Reflectance FTIR Biochemistry. 33: 2628-2634. PMID 8117725 DOI: 10.1021/Bi00175A035 |
0.341 |
|
1994 |
Wetzel R, Chrunyk BA. Inclusion body formation by interleukin‐1β depends on the thermal sensitivity of a folding intermediate Febs Letters. 350: 245-248. PMID 8070572 DOI: 10.1016/0014-5793(94)00775-6 |
0.338 |
|
1994 |
Helms LR, Wetzel R. Proteolytic excision and in situ cyclization of a bioactive loop from an REI-VL presentation scaffold Protein Science. 3: 1108-1113. PMID 7920257 DOI: 10.1002/Pro.5560030714 |
0.369 |
|
1994 |
Stevens PW, Raffen R, Hanson DK, Deng Y, Berrios-Hammond M, Westholm FA, Schiffer M, Stevens FJ, Murphy C, Solomon A, Eulitz M, Wetzel R. Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light-chain amyloid proteins. Protein Science. 4: 421-432. PMID 7795526 DOI: 10.1002/Pro.5560040309 |
0.384 |
|
1994 |
Wetzel R. Mutations and off-pathway aggregation of proteins Trends in Biotechnology. 12: 193-198. PMID 7764903 DOI: 10.1016/0167-7799(94)90082-5 |
0.458 |
|
1993 |
Stults JT, Lai J, McCune S, Wetzel R. Simplification of high-energy collision spectra of peptides by amino-terminal derivatization. Analytical Chemistry. 65: 1703-8. PMID 8368523 DOI: 10.1021/Ac00061A012 |
0.318 |
|
1993 |
Lee G, Chan W, Hurle MR, DesJarlais RL, Watson F, Sathe GM, Wetzel R. Strong inhibition of fibrinogen binding to platelet receptor αIIbβ3 by RGD sequences installed into a presentation scaffold Protein Engineering. 6: 745-754. PMID 8248098 DOI: 10.1093/Protein/6.7.745 |
0.358 |
|
1993 |
Chrunyk BA, Wetzel R. Breakdown in the relationship between thermal and thermodynamic stability in an interleukin-1β point mutant modified in a surface loop Protein Engineering. 6: 733-738. PMID 8248096 DOI: 10.1093/Protein/6.7.733 |
0.37 |
|
1992 |
Wood SJ, Wetzel R. A novel method for the incorporation of glycoprotein-derived oligosaccharides into neoglycopeptides. Bioconjugate Chemistry. 3: 391-396. PMID 1420438 DOI: 10.1021/Bc00017A006 |
0.332 |
|
1990 |
Wetzel R, Halualani R, Stults JT, Quan C. A general method for highly selective cross-linking of unprotected polypeptides via pH-controlled modification of N-terminal α-amino groups Bioconjugate Chemistry. 1: 114-122. PMID 2095209 DOI: 10.1021/Bc00002A005 |
0.375 |
|
1989 |
Mulkerrin MG, Wetzel R. pH dependence of the reversible and irreversible thermal denaturation of gamma interferons. Biochemistry. 28: 6556-6561. PMID 2506928 DOI: 10.1021/Bi00442A005 |
0.316 |
|
1988 |
Wetzel R, Perry LJ, Baase WA, Becktel WJ. Disulfide bonds and thermal stability in T4 lysozyme Proceedings of the National Academy of Sciences of the United States of America. 85: 401-405. PMID 3277175 DOI: 10.1073/Pnas.85.2.401 |
0.308 |
|
1984 |
Perry LJ, Wetzel R. Disulfide bond engineered into T4 lysozyme: Stabilization of the protein toward thermal inactivation Science. 226: 555-557. PMID 6387910 DOI: 10.1126/Science.6387910 |
0.302 |
|
1982 |
Wetzel R, Kleid DG, Crea R, Heyneker HL, Yansura DG, Hirose T, Kraszewski A, Riggs AD, Itakura K, Goeddel DV. Expression in Escherichia coli of a chemically synthesized gene for a "mini-C" analog of human proinsulin. Gene. 16: 63-71. PMID 7044895 DOI: 10.1016/0378-1119(81)90061-5 |
0.342 |
|
1982 |
Morehead H, McKay P, Wetzel R. High-performance liquid chromatography analysis in the synthesis, characterization, and reactions of neoglycopeptides Analytical Biochemistry. 126: 29-36. PMID 6817665 DOI: 10.1016/0003-2697(82)90104-X |
0.316 |
|
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