| Year |
Citation |
Score |
| 2020 |
Kim SG, Chen YJ, Falzon L, Baum J, Inouye M. Mimicking cotranslational folding of prosubtilisin E in vitro. Journal of Biochemistry. PMID 31943045 DOI: 10.1093/Jb/Mvaa004 |
0.457 |
|
| 2019 |
Baum J, Chiti F, De Simone A, Knowles TPJ, Kumita JR, Radford SE, Robinson CV, Salvatella X, Valelli K, Vendruscolo M, Pastore A, Tartaglia GG. Homage to Chris Dobson. Frontiers in Molecular Biosciences. 6: 137. PMID 31921887 DOI: 10.3389/Fmolb.2019.00137 |
0.477 |
|
| 2019 |
Hoop CL, Zhu J, Bhattacharya S, Tobita CA, Radford SE, Baum J. Collagen I weakly interacts with the β-sheets of β2-microglobulin and enhances conformational exchange to induce amyloid formation. Journal of the American Chemical Society. PMID 31875390 DOI: 10.1021/Jacs.9B10421 |
0.378 |
|
| 2019 |
Yang X, Williams JK, Yan R, Mouradian MM, Baum J. Increased Dynamics of α-Synuclein Fibrils by β-Synuclein Leads to Reduced Seeding and Cytotoxicity. Scientific Reports. 9: 17579. PMID 31772376 DOI: 10.1038/S41598-019-54063-8 |
0.382 |
|
| 2019 |
Hoop CL, Kemraj AP, Wang B, Gahlawat S, Godesky M, Zhu J, Warren HR, Case DA, Shreiber DI, Baum J. Molecular underpinnings of integrin binding to collagen mimetic peptides containing vascular Ehlers-Danlos syndrome-associated substitutions. The Journal of Biological Chemistry. PMID 31406019 DOI: 10.1074/Jbc.Ra119.009685 |
0.364 |
|
| 2019 |
Benseny-Cases N, Karamanos TK, Hoop CL, Baum J, Radford SE. Extracellular matrix components modulate different stages in β2-microglobulin amyloid formation. The Journal of Biological Chemistry. PMID 30996004 DOI: 10.1074/Jbc.Ra119.008300 |
0.33 |
|
| 2019 |
Hoop CL, Zhu J, Kemraj A, Case DA, Baum J. Understanding the Molecular Underpinnings of Collagen-Protein Interactions in Healthy and Pathological States Biophysical Journal. 116: 16a-17a. DOI: 10.1016/J.Bpj.2018.11.132 |
0.31 |
|
| 2019 |
Baum J. Modulating Alpha-Synuclein Aggregation through IDP-IDP Interactions Biophysical Journal. 116: 4a. DOI: 10.1016/J.Bpj.2018.11.049 |
0.3 |
|
| 2018 |
Zhu J, Hoop CL, Case DA, Baum J. Cryptic binding sites become accessible through surface reconstruction of the type I collagen fibril. Scientific Reports. 8: 16646. PMID 30413772 DOI: 10.1038/S41598-018-34616-Z |
0.319 |
|
| 2018 |
Williams JK, Yang X, Baum J. Interactions between the Intrinsically Disordered Proteins β-Synuclein and α-Synuclein. Proteomics. e1800109. PMID 30142698 DOI: 10.1002/Pmic.201800109 |
0.359 |
|
| 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 |
0.53 |
|
| 2018 |
Nunes AM, Minetti CASA, Remeta DP, Baum J. Magnesium Activates Microsecond Dynamics to Regulate Integrin-Collagen Recognition. Structure (London, England : 1993). PMID 29937357 DOI: 10.1016/J.Str.2018.05.010 |
0.315 |
|
| 2018 |
Williams JK, Yang X, Atieh TB, Olson MP, Khare SD, Baum J. Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein. Journal of Molecular Biology. PMID 29782835 DOI: 10.1016/J.Jmb.2018.05.024 |
0.366 |
|
| 2017 |
Moriarty GM, Olson MP, Atieh TB, Janowska MK, Khare SD, Baum J. A pH Dependent Switch Promotes β-Synuclein Fibril Formation via Glutamate Residues. The Journal of Biological Chemistry. PMID 28710275 DOI: 10.1074/Jbc.M117.780528 |
0.366 |
|
| 2017 |
An B, Chang S, Hoop C, Baum J, Buehler MJ, Kaplan DL. Structural Insights into the Glycine Pair Motifs in Type III Collagen Acs Biomaterials Science & Engineering. 3: 269-278. DOI: 10.1021/Acsbiomaterials.6B00512 |
0.366 |
|
| 2016 |
Bennett NK, Chmielowski R, Abdelhamid DS, Faig JJ, Francis N, Baum J, Pang ZP, Uhrich KE, Moghe PV. Polymer brain-nanotherapeutics for multipronged inhibition of microglial α-synuclein aggregation, activation, and neurotoxicity. Biomaterials. 111: 179-189. PMID 27736702 DOI: 10.1016/J.Biomaterials.2016.10.001 |
0.301 |
|
| 2016 |
Nunes AM, Zhu J, Jezioro J, Minetti CA, Remeta DP, Farndale RW, Hamaia SW, Baum J. Intrinsic local destabilization of the C-terminus predisposes integrin α1 I domain to a conformational switch induced by collagen binding. Protein Science : a Publication of the Protein Society. PMID 27342747 DOI: 10.1002/Pro.2972 |
0.405 |
|
| 2016 |
Janowska MK, Baum J. Intermolecular Paramagnetic Relaxation Enhancement (PRE) Studies of Transient Complexes in Intrinsically Disordered Proteins. Methods in Molecular Biology (Clifton, N.J.). 1345: 45-53. PMID 26453204 DOI: 10.1007/978-1-4939-2978-8_3 |
0.356 |
|
| 2016 |
Janowska MK, Baum J. The loss of inhibitory C-terminal conformations in disease associated P123H β-synuclein. Protein Science : a Publication of the Protein Society. 25: 286-94. PMID 26332674 DOI: 10.1002/Pro.2798 |
0.388 |
|
| 2015 |
Janowska MK, Wu KP, Baum J. Unveiling transient protein-protein interactions that modulate inhibition of alpha-synuclein aggregation by beta-synuclein, a pre-synaptic protein that co-localizes with alpha-synuclein. Scientific Reports. 5: 15164. PMID 26477939 DOI: 10.1038/Srep15164 |
0.585 |
|
| 2015 |
Fu I, Case DA, Baum J. Dynamic Water-Mediated Hydrogen Bonding in a Collagen Model Peptide. Biochemistry. 54: 6029-37. PMID 26339765 DOI: 10.1021/Acs.Biochem.5B00622 |
0.367 |
|
| 2015 |
Xiao J, Sun X, Balaram M, Brodsky B, Baum J. NMR studies demonstrate a unique AAB composition and chain register for a heterotrimeric type IV collagen model peptide containing a natural interruption site. The Journal of Biological Chemistry. PMID 26209635 DOI: 10.1074/Jbc.M115.654871 |
0.609 |
|
| 2015 |
Xiao J, Yang Z, Sun X, Addabbo R, Baum J. Local amino acid sequence patterns dominate the heterogeneous phenotype for the collagen connective tissue disease Osteogenesis Imperfecta resulting from Gly mutations. Journal of Structural Biology. 192: 127-37. PMID 25980613 DOI: 10.1016/J.Jsb.2015.05.002 |
0.567 |
|
| 2014 |
Moriarty GM, Minetti CA, Remeta DP, Baum J. A revised picture of the Cu(II)-α-synuclein complex: the role of N-terminal acetylation. Biochemistry. 53: 2815-7. PMID 24739028 DOI: 10.1021/Bi5003025 |
0.302 |
|
| 2014 |
Baum J. Accessible Conformations of N-Terminal Acetylated Alpha-Synuclein: Implications for Fibril Formation Biophysical Journal. 106: 5a. DOI: 10.1016/J.Bpj.2013.11.058 |
0.393 |
|
| 2013 |
Kang L, Janowska MK, Moriarty GM, Baum J. Mechanistic insight into the relationship between N-terminal acetylation of α-synuclein and fibril formation rates by NMR and fluorescence. Plos One. 8: e75018. PMID 24058647 DOI: 10.1371/Journal.Pone.0075018 |
0.639 |
|
| 2013 |
Moriarty GM, Janowska MK, Kang L, Baum J. Exploring the accessible conformations of N-terminal acetylated α-synuclein. Febs Letters. 587: 1128-38. PMID 23499431 DOI: 10.1016/J.Febslet.2013.02.049 |
0.585 |
|
| 2013 |
Kim S, Wu KP, Baum J. Fast hydrogen exchange affects ¹⁵N relaxation measurements in intrinsically disordered proteins. Journal of Biomolecular Nmr. 55: 249-56. PMID 23314729 DOI: 10.1007/S10858-013-9706-1 |
0.554 |
|
| 2012 |
Narayanan C, Weinstock DS, Wu KP, Baum J, Levy RM. Investigation of the Polymeric Properties of α-Synuclein and Comparison with NMR Experiments: A Replica Exchange Molecular Dynamics Study. Journal of Chemical Theory and Computation. 8: 3929-3942. PMID 23162382 DOI: 10.1021/Ct300241T |
0.601 |
|
| 2012 |
Parmar AS, Nunes AM, Baum J, Brodsky B. A peptide study of the relationship between the collagen triple-helix and amyloid. Biopolymers. 97: 795-806. PMID 22806499 DOI: 10.1002/Bip.22070 |
0.401 |
|
| 2012 |
Kang L, Moriarty GM, Woods LA, Ashcroft AE, Radford SE, Baum J. N-terminal acetylation of α-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer. Protein Science : a Publication of the Protein Society. 21: 911-7. PMID 22573613 DOI: 10.1002/Pro.2088 |
0.652 |
|
| 2012 |
Baum J, Pines A. NMR studies of clustering in solids. Journal of the American Chemical Society. 108: 7447-54. PMID 22283239 DOI: 10.1021/ja00284a001 |
0.363 |
|
| 2011 |
Xiao J, Cheng H, Silva T, Baum J, Brodsky B. Osteogenesis imperfecta missense mutations in collagen: structural consequences of a glycine to alanine replacement at a highly charged site. Biochemistry. 50: 10771-80. PMID 22054507 DOI: 10.1021/Bi201476A |
0.606 |
|
| 2011 |
Xiao J, Madhan B, Li Y, Brodsky B, Baum J. Osteogenesis imperfecta model peptides: incorporation of residues replacing Gly within a triple helix achieved by renucleation and local flexibility. Biophysical Journal. 101: 449-58. PMID 21767498 DOI: 10.1016/J.Bpj.2011.06.017 |
0.634 |
|
| 2011 |
Kang L, Wu KP, Vendruscolo M, Baum J. The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse α-synuclein. Journal of the American Chemical Society. 133: 13465-70. PMID 21721555 DOI: 10.1021/Ja203979J |
0.735 |
|
| 2011 |
Wu KP, Baum J. Backbone assignment and dynamics of human α-synuclein in viscous 2 M glucose solution. Biomolecular Nmr Assignments. 5: 43-6. PMID 20872101 DOI: 10.1007/S12104-010-9263-4 |
0.572 |
|
| 2011 |
Wu K, Baum J. Transient Protein-Protein Interactions in the IDP Alpha-Synuclein Detected by NMR: Implications for Protein Aggregation Biophysical Journal. 100: 519a. DOI: 10.1016/J.Bpj.2010.12.3037 |
0.608 |
|
| 2010 |
Xiao J, Addabbo RM, Lauer JL, Fields GB, Baum J. Local conformation and dynamics of isoleucine in the collagenase cleavage site provide a recognition signal for matrix metalloproteinases. The Journal of Biological Chemistry. 285: 34181-90. PMID 20679339 DOI: 10.1074/Jbc.M110.128355 |
0.58 |
|
| 2010 |
Wu KP, Baum J. Detection of transient interchain interactions in the intrinsically disordered protein alpha-synuclein by NMR paramagnetic relaxation enhancement. Journal of the American Chemical Society. 132: 5546-7. PMID 20359221 DOI: 10.1021/Ja9105495 |
0.605 |
|
| 2010 |
Wu K, Baum J. Backbone assignment of human alpha-synuclein in viscous 2 M glucose solution Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16904 |
0.513 |
|
| 2009 |
Xiao J, Baum J. Structural insights from (15)N relaxation data for an anisotropic collagen peptide. Journal of the American Chemical Society. 131: 18194-5. PMID 19954183 DOI: 10.1021/Ja9056823 |
0.617 |
|
| 2009 |
Wu KP, Weinstock DS, Narayanan C, Levy RM, Baum J. Structural reorganization of alpha-synuclein at low pH observed by NMR and REMD simulations. Journal of Molecular Biology. 391: 784-96. PMID 19576220 DOI: 10.1016/J.Jmb.2009.06.063 |
0.579 |
|
| 2009 |
Li Y, Brodsky B, Baum J. NMR conformational and dynamic consequences of a gly to ser substitution in an osteogenesis imperfecta collagen model peptide. The Journal of Biological Chemistry. 284: 20660-7. PMID 19451653 DOI: 10.1074/Jbc.M109.018077 |
0.468 |
|
| 2008 |
Chen YJ, Wu KP, Kim S, Falzon L, Inouye M, Baum J. Backbone NMR assignments of DFP-inhibited mature subtilisin E. Biomolecular Nmr Assignments. 2: 131-3. PMID 19636887 DOI: 10.1007/S12104-008-9103-Y |
0.54 |
|
| 2008 |
Madhan B, Xiao J, Thiagarajan G, Baum J, Brodsky B. NMR monitoring of chain-specific stability in heterotrimeric collagen peptides. Journal of the American Chemical Society. 130: 13520-1. PMID 18798618 DOI: 10.1021/Ja805496V |
0.58 |
|
| 2008 |
Brodsky B, Baum J. Structural biology: Modelling collagen diseases. Nature. 453: 998-9. PMID 18563144 DOI: 10.1038/453998A |
0.337 |
|
| 2008 |
Weinstock DS, Narayanan C, Baum J, Levy RM. Correlation between 13Calpha chemical shifts and helix content of peptide ensembles. Protein Science : a Publication of the Protein Society. 17: 950-4. PMID 18436960 DOI: 10.1110/Ps.073365408 |
0.404 |
|
| 2008 |
Go A, Kim S, Baum J, Hecht MH. Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles. Protein Science : a Publication of the Protein Society. 17: 821-32. PMID 18436954 DOI: 10.1110/Ps.073377908 |
0.427 |
|
| 2008 |
Wu KP, Kim S, Fela DA, Baum J. Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation. Journal of Molecular Biology. 378: 1104-15. PMID 18423664 DOI: 10.1016/J.Jmb.2008.03.017 |
0.754 |
|
| 2008 |
Thiagarajan G, Li Y, Mohs A, Strafaci C, Popiel M, Baum J, Brodsky B. Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models. Journal of Molecular Biology. 376: 736-48. PMID 18187152 DOI: 10.1016/J.Jmb.2007.11.075 |
0.418 |
|
| 2007 |
Go A, Kim S, Hecht M, Baum J. NMR assignment of S836: A de novo protein from a designed superfamily Biomolecular Nmr Assignments. 1: 213-215. PMID 19636868 DOI: 10.1007/S12104-007-9059-3 |
0.396 |
|
| 2007 |
Li Y, Brodsky B, Baum J. NMR shows hydrophobic interactions replace glycine packing in the triple helix at a natural break in the (Gly-X-Y)n repeat. The Journal of Biological Chemistry. 282: 22699-706. PMID 17550894 DOI: 10.1074/Jbc.M702910200 |
0.465 |
|
| 2007 |
Weinstock DS, Narayanan C, Felts AK, Andrec M, Levy RM, Wu KP, Baum J. Distinguishing among structural ensembles of the GB1 peptide: REMD simulations and NMR experiments. Journal of the American Chemical Society. 129: 4858-9. PMID 17402734 DOI: 10.1021/Ja0677517 |
0.578 |
|
| 2006 |
Hyde TJ, Bryan MA, Brodsky B, Baum J. Sequence dependence of renucleation after a Gly mutation in model collagen peptides. The Journal of Biological Chemistry. 281: 36937-43. PMID 16998200 DOI: 10.1074/Jbc.M605135200 |
0.44 |
|
| 2006 |
Mohs A, Popiel M, Li Y, Baum J, Brodsky B. Conformational features of a natural break in the type IV collagen Gly-X-Y repeat. The Journal of Biological Chemistry. 281: 17197-202. PMID 16613845 DOI: 10.1074/Jbc.M601763200 |
0.441 |
|
| 2006 |
MOHS A, STRAFACI C, LI Y, BAUM J, BRODSKY B. Structural studies of breaks in the type IV collagen triple helix Matrix Biology. 25: S83-S83. DOI: 10.1016/J.Matbio.2006.08.227 |
0.309 |
|
| 2005 |
Li Y, Kim S, Brodsky B, Baum J. Identification of partially disordered peptide intermediates through residue-specific NMR diffusion measurements. Journal of the American Chemical Society. 127: 10490-1. PMID 16045327 DOI: 10.1021/Ja052801D |
0.371 |
|
| 2005 |
Mohs A, Li Y, Doss-Pepe E, Baum J, Brodsky B. Stability junction at a common mutation site in the collagenous domain of the mannose binding lectin. Biochemistry. 44: 1793-9. PMID 15697204 DOI: 10.1021/Bi0482708 |
0.42 |
|
| 2004 |
Buevich AV, Silva T, Brodsky B, Baum J. Transformation of the mechanism of triple-helix peptide folding in the absence of a C-terminal nucleation domain and its implications for mutations in collagen disorders. The Journal of Biological Chemistry. 279: 46890-5. PMID 15299012 DOI: 10.1074/Jbc.M407061200 |
0.446 |
|
| 2003 |
Wei Y, Kim S, Fela D, Baum J, Hecht MH. Solution structure of a de novo protein from a designed combinatorial library. Proceedings of the National Academy of Sciences of the United States of America. 100: 13270-3. PMID 14593201 DOI: 10.1073/Pnas.1835644100 |
0.74 |
|
| 2003 |
Wei Y, Fela D, Kim S, Hecht M, Baum J. 1H, 13C and 15N resonance assignments of S-824, a de novo four-helix bundle from a designed combinatorial library. Journal of Biomolecular Nmr. 27: 395-6. PMID 14512738 DOI: 10.1023/A:1025842221022 |
0.725 |
|
| 2003 |
Xu Y, Hyde T, Wang X, Bhate M, Brodsky B, Baum J. NMR and CD spectroscopy show that imino acid restriction of the unfolded state leads to efficient folding. Biochemistry. 42: 8696-703. PMID 12873129 DOI: 10.1021/Bi034006N |
0.427 |
|
| 2002 |
Buevich AV, Baum J. Residue-specific real-time NMR diffusion experiments define the association states of proteins during folding. Journal of the American Chemical Society. 124: 7156-62. PMID 12059241 DOI: 10.1021/Ja012699U |
0.37 |
|
| 2002 |
Bhate M, Wang X, Baum J, Brodsky B. Folding and conformational consequences of glycine to alanine replacements at different positions in a collagen model peptide. Biochemistry. 41: 6539-47. PMID 12009919 DOI: 10.1021/Bi020070D |
0.453 |
|
| 2002 |
Buevich AV, Shinde UP, Inouye M, Baum J. Backbone dynamics of the natively unfolded pro-peptide of subtilisin by heteronuclear NMR relaxation studies. Journal of Biomolecular Nmr. 20: 233-49. PMID 11519747 DOI: 10.1023/A:1011243116136 |
0.345 |
|
| 2001 |
Buevich A, Baum J, Lindquist S, Kelly JW, Byers PH, Seckler R, Helenius A. Nuclear magnetic resonance characterization of peptide models of collagen-folding diseases Philosophical Transactions of the Royal Society B: Biological Sciences. 356: 159-168. PMID 11260796 DOI: 10.1098/Rstb.2000.0761 |
0.446 |
|
| 2000 |
Buevich AV, Dai QH, Liu X, Brodsky B, Baum J. Site-specific NMR monitoring of cis-trans isomerization in the folding of the proline-rich collagen triple helix. Biochemistry. 39: 4299-308. PMID 10757978 DOI: 10.1021/Bi992584R |
0.612 |
|
| 1999 |
Kim S, Bracken C, Baum J. Characterization of millisecond time-scale dynamics in the molten globule state of α-lactalbumin by NMR Journal of Molecular Biology. 294: 551-560. PMID 10610779 DOI: 10.1006/Jmbi.1999.3250 |
0.362 |
|
| 1999 |
Baum J, Brodsky B. Folding of peptide models of collagen and misfolding in disease Current Opinion in Structural Biology. 9: 122-128. PMID 10047579 DOI: 10.1016/S0959-440X(99)80016-5 |
0.391 |
|
| 1999 |
Murphy LR, Li N, Baum J, Levy RM. Tertiary contacts in alpha-lactalbumin at pH 7 and pH 2: a molecular dynamics study. Journal of Biomolecular Structure & Dynamics. 16: 355-65. PMID 9833674 DOI: 10.1080/07391102.1998.10508253 |
0.336 |
|
| 1999 |
Buevich AV, Baum J. Dynamics of Unfolded Proteins: Incorporation of Distributions of Correlation Times in the Model Free Analysis of NMR Relaxation Data Journal of the American Chemical Society. 121: 8671-8672. DOI: 10.1021/Ja9910412 |
0.318 |
|
| 1998 |
Liu X, Kim S, Dai QH, Brodsky B, Baum J. Nuclear magnetic resonance shows asymmetric loss of triple helix in peptides modeling a collagen mutation in brittle bone disease. Biochemistry. 37: 15528-33. PMID 9799516 DOI: 10.1021/Bi981147U |
0.662 |
|
| 1998 |
Kim S, Baum J. Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR. Protein Science. 7: 1930-1938. PMID 9761473 DOI: 10.1002/Pro.5560070908 |
0.349 |
|
| 1997 |
Baum J, Brodsky B. Real-time NMR investigations of triple-helix folding and collagen folding diseases Folding and Design. 2. PMID 9269560 DOI: 10.1016/S1359-0278(97)00028-X |
0.412 |
|
| 1996 |
Liu X, Siegel DL, Fan P, Brodsky B, Baum J. Direct NMR Measurement of the Folding Kinetics of a Trimeric Peptide Biochemistry. 35: 4306-4313. PMID 8605179 DOI: 10.1021/Bi952270D |
0.448 |
|
| 1996 |
Battineni ML, Yang W, Liu X, Baum J, Brodsky B. Understanding the varying severity of a collagen disease, osteogenesis imperfecta, through a peptide approach Matrix Biology. 15: 175. DOI: 10.1016/S0945-053X(96)90059-1 |
0.302 |
|
| 1995 |
Anachi RB, Siegel DL, Baum J, Brodsky B. Acid Destabilization Of A Triple-Helical Peptide Model Of The Macrophage Scavenger Receptor Febs Letters. 368: 551-555. PMID 7635219 DOI: 10.1016/0014-5793(95)00738-U |
0.404 |
|
| 1994 |
Parkinson GN, Wu Y, Fan P, Kohn J, Baum J, Berman HM. Crystal structure and NMR conformation of a cyclic pseudotetrapeptide containing urethane backbone linkages Biopolymers. 34: 403-414. PMID 8161712 DOI: 10.1002/Bip.360340312 |
0.365 |
|
| 1994 |
Chen Y, Suri AK, Kominos D, Sanyal G, Naylor AM, Pitzenberger SM, Garsky VM, Levy RM, Baum J. Three-dimensional structure of echistatin and dynamics of the active site. Journal of Biomolecular Nmr. 4: 307-24. PMID 8019139 DOI: 10.1007/Bf00179342 |
0.394 |
|
| 1994 |
Bracken C, Gulyas J, Taylor JW, Baum J. Synthesis and Nuclear Magnetic Resonance Structure Determination of an .alpha.-Helical, Bicyclic, Lactam-Bridged Hexapeptide Journal of the American Chemical Society. 116: 6431-6432. DOI: 10.1021/Ja00093A052 |
0.32 |
|
| 1993 |
Chyan CL, Wormald C, Dobson CM, Evans PA, Baum J. Structure and stability of the molten globule state of guinea-pig alpha-lactalbumin: a hydrogen exchange study. Biochemistry. 32: 5681-91. PMID 8504087 DOI: 10.1021/Bi00072A025 |
0.513 |
|
| 1993 |
Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM. Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study. Biochemistry. 32: 1707-18. PMID 8439536 DOI: 10.1021/Bi00058A003 |
0.545 |
|
| 1993 |
Fan P, Bracken C, Baum J. Structural characterization of monellin in the alcohol-denatured state by NMR: evidence for beta-sheet to alpha-helix conversion. Biochemistry. 32: 1573-1582. PMID 8381663 DOI: 10.1021/Bi00057A023 |
0.331 |
|
| 1993 |
Li MH, Fan P, Brodsky B, Baum J. Two-dimensional NMR assignments and conformation of (Pro-Hyp-Gly)10 and a designed collagen triple-helical peptide. Biochemistry. 32: 7377-7387. PMID 8338835 DOI: 10.1021/Bi00080A007 |
0.411 |
|
| 1993 |
Baum J. Backbone dynamics of (pro-hyp-gly)io and a designed collagen-like triple-helical peptide by15N NMR relaxation and hydrogen-exchange measurements Biochemistry®. 32: 13299-13309. PMID 8241186 DOI: 10.1021/Bi00211A043 |
0.4 |
|
| 1992 |
Brodsky B, Li MH, Long CG, Apigo J, Baum J. NMR and CD studies of triple-helical peptides Biopolymers. 32: 447-451. PMID 1623141 DOI: 10.1002/Bip.360320423 |
0.433 |
|
| 1992 |
Long CG, Li MH, Baum J, Brodsky B. Nuclear magnetic resonance and circular dichroism studies of a triple-helical peptide with a glycine substitution Journal of Molecular Biology. 225: 1-4. PMID 1583683 DOI: 10.1016/0022-2836(92)91020-P |
0.436 |
|
| 1992 |
Alexandrescu AT, Broadhurst RW, Wormald C, Chyan CL, Baum J, Dobson CM. 1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin. European Journal of Biochemistry / Febs. 210: 699-709. PMID 1483454 DOI: 10.1111/J.1432-1033.1992.Tb17471.X |
0.536 |
|
| 1991 |
Chen Y, Pitzenberger SM, Garsky VM, Lumma PK, Sanyal G, Baum J. Proton NMR assignments and secondary structure of the snake venom protein echistatin. Biochemistry. 30: 11625-11636. PMID 1661142 DOI: 10.1021/Bi00114A004 |
0.434 |
|
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