| Year |
Citation |
Score |
| 2021 |
Jain R, Muneeruddin K, Anderson J, Harms MJ, Shaffer SA, Matthews CR. A conserved folding nucleus sculpts the free energy landscape of bacterial and archaeal orthologs from a divergent TIM barrel family. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 33875592 DOI: 10.1073/pnas.2019571118 |
0.414 |
|
| 2020 |
Niu B, Mackness BC, Zitzewitz JA, Matthews CR, Gross ML. Trifluoroethanol Partially Unfolds G93A SOD1 Leading to Protein Aggregation: A Study by Native Mass Spectrometry and FPOP Protein Footprinting. Biochemistry. PMID 32924445 DOI: 10.1021/Acs.Biochem.0C00425 |
0.4 |
|
| 2020 |
Chan YH, Zeldovich KB, Matthews CR. An allosteric pathway explains beneficial fitness in yeast for long-range mutations in an essential TIM barrel enzyme. Protein Science : a Publication of the Protein Society. PMID 32643222 DOI: 10.1002/pro.3911 |
0.369 |
|
| 2020 |
Cohen NR, Kayatekin C, Zitzewitz JA, Bilsel O, Matthews CR. Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1. Biophysical Journal. PMID 32191862 DOI: 10.1016/j.bpj.2020.02.028 |
0.456 |
|
| 2019 |
Halloran KT, Wang Y, Arora K, Chakravarthy S, Irving TC, Bilsel O, Brooks CL, Matthews CR. Frustration and folding of a TIM barrel protein. Proceedings of the National Academy of Sciences of the United States of America. PMID 31346089 DOI: 10.1073/Pnas.1900880116 |
0.548 |
|
| 2019 |
Cohen NR, Zitzewitz JA, Bilsel O, Matthews CR. Nonnative structure in a peptide model of the unfolded state of SOD1: Implications for ALS-linked aggregation. The Journal of Biological Chemistry. PMID 31341015 DOI: 10.1074/Jbc.Ra119.008765 |
0.435 |
|
| 2019 |
Basak S, Nobrega RP, Tavella D, Deveau LM, Koga N, Tatsumi-Koga R, Baker D, Massi F, Matthews CR. Networks of electrostatic and hydrophobic interactions modulate the complex folding free energy surface of a designed βα protein. Proceedings of the National Academy of Sciences of the United States of America. PMID 30877249 DOI: 10.1073/Pnas.1818744116 |
0.777 |
|
| 2017 |
Shi J, Nobrega RP, Schwantes C, Kathuria SV, Bilsel O, Matthews CR, Lane TJ, Pande VS. Atomistic structural ensemble refinement reveals non-native structure stabilizes a sub-millisecond folding intermediate of CheY. Scientific Reports. 7: 44116. PMID 28272524 DOI: 10.1038/Srep44116 |
0.464 |
|
| 2017 |
Chan YH, Venev SV, Zeldovich KB, Matthews CR. Correlation of fitness landscapes from three orthologous TIM barrels originates from sequence and structure constraints. Nature Communications. 8: 14614. PMID 28262665 DOI: 10.1038/Ncomms14614 |
0.365 |
|
| 2017 |
Kathuria SV, Bilsel O, Chakravarthy S, Matthews CR. Microfluidic Turbulent Mixers, Time Resolved SAXS and Folding Intermediates of CheY Biophysical Journal. 112: 61a. DOI: 10.1016/J.Bpj.2016.11.367 |
0.443 |
|
| 2017 |
Mackness BC, Cohen NR, Matthews CR, Zitzewitz JA, Bilsel O. Examination of the Oligomerization Mechanism of SOD1 In Vitro and in Live Cells Biophysical Journal. 112: 316a. DOI: 10.1016/J.Bpj.2016.11.1714 |
0.425 |
|
| 2016 |
Niu B, Mackness BC, Rempel DL, Zhang H, Cui W, Matthews CR, Zitzewitz JA, Gross ML. Incorporation of a Reporter Peptide in FPOP Compensates for Adventitious Scavengers and Permits Time-Dependent Measurements. Journal of the American Society For Mass Spectrometry. PMID 27924496 DOI: 10.1007/S13361-016-1552-4 |
0.311 |
|
| 2015 |
Orevi T, Rahamim G, Amir D, Kathuria S, Bilsel O, Matthews CR, Haas E. Sequential Closure of Loop Structures Forms the Folding Nucleus during the Refolding Transition of the Escherichia coli Adenylate Kinase Molecule. Biochemistry. PMID 26666584 DOI: 10.1021/Acs.Biochem.5B00849 |
0.503 |
|
| 2015 |
Kathuria SV, Chan YH, Nobrega RP, Özen A, Matthews CR. Clusters of Isoleucine, Leucine and Valine Side Chains Define Cores of Stability in High-Energy States of Globular Proteins: Sequence Determinants of Structure and Stability. Protein Science : a Publication of the Protein Society. PMID 26660714 DOI: 10.1002/Pro.2860 |
0.513 |
|
| 2015 |
Rosen LE, Kathuria SV, Matthews CR, Bilsel O, Marqusee S. Non-native structure appears in microseconds during the folding of E. coli RNase H. Journal of Molecular Biology. 427: 443-53. PMID 25311861 DOI: 10.1016/J.Jmb.2014.10.003 |
0.515 |
|
| 2014 |
Nobrega RP, Arora K, Kathuria SV, Graceffa R, Barrea RA, Guo L, Chakravarthy S, Bilsel O, Irving TC, Brooks CL, Matthews CR. Modulation of frustration in folding by sequence permutation. Proceedings of the National Academy of Sciences of the United States of America. 111: 10562-7. PMID 25002512 DOI: 10.1073/Pnas.1324230111 |
0.499 |
|
| 2014 |
Kathuria SV, Kayatekin C, Barrea R, Kondrashkina E, Graceffa R, Guo L, Nobrega RP, Chakravarthy S, Matthews CR, Irving TC, Bilsel O. Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS. Journal of Molecular Biology. 426: 1980-94. PMID 24607691 DOI: 10.1016/J.Jmb.2014.02.020 |
0.496 |
|
| 2014 |
Mackness BC, Tran MT, McClain SP, Matthews CR, Zitzewitz JA. Folding of the RNA recognition motif (RRM) domains of the amyotrophic lateral sclerosis (ALS)-linked protein TDP-43 reveals an intermediate state. The Journal of Biological Chemistry. 289: 8264-76. PMID 24497641 DOI: 10.1074/Jbc.M113.542779 |
0.471 |
|
| 2014 |
Rosen LE, Kathuria S, Connell K, Bilsel O, Matthews CR, Marqusee S. Observing and Characterizing Early Folding Intermediates of E.Coli Rnase H using Kinetic and Equilibrium Approaches Biophysical Journal. 106: 246a. DOI: 10.1016/J.Bpj.2013.11.1442 |
0.521 |
|
| 2013 |
Broering TJ, Wang H, Boatright NK, Wang Y, Baptista K, Shayan G, Garrity KA, Kayatekin C, Bosco DA, Matthews CR, Ambrosino DM, Xu Z, Babcock GJ. Identification of human monoclonal antibodies specific for human SOD1 recognizing distinct epitopes and forms of SOD1. Plos One. 8: e61210. PMID 23613814 DOI: 10.1371/Journal.Pone.0061210 |
0.351 |
|
| 2013 |
Gangadhara BN, Laine JM, Kathuria SV, Massi F, Matthews CR. Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein. Journal of Molecular Biology. 425: 1065-81. PMID 23333740 DOI: 10.1016/J.Jmb.2013.01.002 |
0.479 |
|
| 2013 |
Das P, Kapoor D, Halloran KT, Zhou R, Matthews CR. Interplay between drying and stability of a TIM barrel protein: a combined simulation-experimental study. Journal of the American Chemical Society. 135: 1882-90. PMID 23293932 DOI: 10.1021/Ja310544T |
0.408 |
|
| 2012 |
Kayatekin C, Cohen NR, Matthews CR. Enthalpic barriers dominate the folding and unfolding of the human Cu, Zn superoxide dismutase monomer. Journal of Molecular Biology. 424: 192-202. PMID 22999954 DOI: 10.1016/J.Jmb.2012.09.009 |
0.523 |
|
| 2011 |
Arai M, Iwakura M, Matthews CR, Bilsel O. Microsecond subdomain folding in dihydrofolate reductase. Journal of Molecular Biology. 410: 329-42. PMID 21554889 DOI: 10.1016/J.Jmb.2011.04.057 |
0.549 |
|
| 2011 |
Kathuria SV, Guo L, Graceffa R, Barrea R, Nobrega RP, Matthews CR, Irving TC, Bilsel O. Minireview: structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scattering. Biopolymers. 95: 550-8. PMID 21442608 DOI: 10.1002/Bip.21628 |
0.374 |
|
| 2011 |
Arai M, Iwakura M, Matthews CR, Bilsel O. 2H1536 Microsecond Subdomain Folding in Dihydrofolate Reductase(Protein: Property 3,The 48th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 51: S88. DOI: 10.2142/Biophys.51.S88_2 |
0.328 |
|
| 2010 |
Svensson AK, Bilsel O, Kayatekin C, Adefusika JA, Zitzewitz JA, Matthews CR. Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species. Plos One. 5: e10064. PMID 20404910 DOI: 10.1371/Journal.Pone.0010064 |
0.446 |
|
| 2010 |
Hills RD, Kathuria SV, Wallace LA, Day IJ, Brooks CL, Matthews CR. Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins. Journal of Molecular Biology. 398: 332-50. PMID 20226790 DOI: 10.1016/J.Jmb.2010.03.001 |
0.461 |
|
| 2010 |
Kayatekin C, Zitzewitz JA, Matthews CR. Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species. Journal of Molecular Biology. 398: 320-31. PMID 20184893 DOI: 10.1016/J.Jmb.2010.02.034 |
0.438 |
|
| 2009 |
Yang X, Kathuria SV, Vadrevu R, Matthews CR. Betaalpha-hairpin clamps brace betaalphabeta modules and can make substantive contributions to the stability of TIM barrel proteins. Plos One. 4: e7179. PMID 19787060 DOI: 10.1371/Journal.Pone.0007179 |
0.472 |
|
| 2009 |
Tiwari A, Liba A, Sohn SH, Seetharaman SV, Bilsel O, Matthews CR, Hart PJ, Valentine JS, Hayward LJ. Metal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral sclerosis. The Journal of Biological Chemistry. 284: 27746-58. PMID 19651777 DOI: 10.1074/Jbc.M109.043729 |
0.356 |
|
| 2009 |
Noel AF, Bilsel O, Kundu A, Wu Y, Zitzewitz JA, Matthews CR. The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors. Journal of Molecular Biology. 387: 1002-16. PMID 19150359 DOI: 10.1016/J.Jmb.2008.12.061 |
0.552 |
|
| 2008 |
Kayatekin C, Zitzewitz JA, Matthews CR. Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase. Journal of Molecular Biology. 384: 540-55. PMID 18840448 DOI: 10.1016/J.Jmb.2008.09.045 |
0.541 |
|
| 2008 |
Wu Y, Kondrashkina E, Kayatekin C, Matthews CR, Bilsel O. Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein. Proceedings of the National Academy of Sciences of the United States of America. 105: 13367-72. PMID 18757725 DOI: 10.1073/Pnas.0802788105 |
0.544 |
|
| 2008 |
Kathuria SV, Day IJ, Wallace LA, Matthews CR. Kinetic traps in the folding of beta alpha-repeat proteins: CheY initially misfolds before accessing the native conformation. Journal of Molecular Biology. 382: 467-84. PMID 18619461 DOI: 10.1016/J.Jmb.2008.06.054 |
0.542 |
|
| 2008 |
Vadrevu R, Wu Y, Matthews CR. NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein. Journal of Molecular Biology. 377: 294-306. PMID 18234216 DOI: 10.1016/J.Jmb.2007.11.010 |
0.513 |
|
| 2007 |
Gu Z, Rao MK, Forsyth WR, Finke JM, Matthews CR. Structural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and GÅ model simulation. Journal of Molecular Biology. 374: 528-46. PMID 17942114 DOI: 10.1016/J.Jmb.2007.09.024 |
0.783 |
|
| 2007 |
Forsyth WR, Bilsel O, Gu Z, Matthews CR. Topology and sequence in the folding of a TIM barrel protein: global analysis highlights partitioning between transient off-pathway and stable on-pathway folding intermediates in the complex folding mechanism of a (betaalpha)8 barrel of unknown function from B. subtilis. Journal of Molecular Biology. 372: 236-53. PMID 17619021 DOI: 10.1016/J.Jmb.2007.06.018 |
0.574 |
|
| 2007 |
Yang X, Vadrevu R, Wu Y, Matthews CR. Long-range side-chain-main-chain interactions play crucial roles in stabilizing the (betaalpha)8 barrel motif of the alpha subunit of tryptophan synthase. Protein Science : a Publication of the Protein Society. 16: 1398-409. PMID 17586773 DOI: 10.1110/Ps.062704507 |
0.422 |
|
| 2007 |
Gu Z, Zitzewitz JA, Matthews CR. Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus. Journal of Molecular Biology. 368: 582-94. PMID 17359995 DOI: 10.1016/J.Jmb.2007.02.027 |
0.559 |
|
| 2007 |
Arai M, Kondrashkina E, Kayatekin C, Matthews CR, Iwakura M, Bilsel O. Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate reductase, an alpha/beta-type protein. Journal of Molecular Biology. 368: 219-29. PMID 17331539 DOI: 10.1016/J.Jmb.2007.01.085 |
0.44 |
|
| 2007 |
Wu Y, Vadrevu R, Kathuria S, Yang X, Matthews CR. A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein. Journal of Molecular Biology. 366: 1624-38. PMID 17222865 DOI: 10.1016/J.Jmb.2006.12.005 |
0.356 |
|
| 2006 |
Svensson AK, Bilsel O, Kondrashkina E, Zitzewitz JA, Matthews CR. Mapping the folding free energy surface for metal-free human Cu,Zn superoxide dismutase. Journal of Molecular Biology. 364: 1084-102. PMID 17046019 DOI: 10.1016/J.Jmb.2006.09.005 |
0.548 |
|
| 2006 |
Simler BR, Levy Y, Onuchic JN, Matthews CR. The folding energy landscape of the dimerization domain of Escherichia coli Trp repressor: a joint experimental and theoretical investigation. Journal of Molecular Biology. 363: 262-78. PMID 16956620 DOI: 10.1016/J.Jmb.2006.07.080 |
0.789 |
|
| 2006 |
Svensson AK, Zitzewitz JA, Matthews CR, Smith VF. The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli. Protein Engineering, Design & Selection : Peds. 19: 175-85. PMID 16452118 DOI: 10.1093/Protein/Gzj017 |
0.77 |
|
| 2006 |
Bilsel O, Matthews CR. Molecular dimensions and their distributions in early folding intermediates. Current Opinion in Structural Biology. 16: 86-93. PMID 16442277 DOI: 10.1016/J.Sbi.2006.01.007 |
0.442 |
|
| 2006 |
Arai M, Iwakura M, Matthews CR, Bilsel O. 1P106 Submillisecond Folding of Escherichia coli Dihydrofolate Reductase Monitored by Time-Resolved Fluorescence Spectroscopy(3. Protein folding and misfolding (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) Seibutsu Butsuri. 46: S173. DOI: 10.2142/Biophys.46.S173_2 |
0.401 |
|
| 2005 |
Wu Y, Vadrevu R, Yang X, Matthews CR. Specific structure appears at the N terminus in the sub-millisecond folding intermediate of the alpha subunit of tryptophan synthase, a TIM barrel protein. Journal of Molecular Biology. 351: 445-52. PMID 16023136 DOI: 10.1016/J.Jmb.2005.06.006 |
0.434 |
|
| 2005 |
Wintrode PL, Rojsajjakul T, Vadrevu R, Matthews CR, Smith DL. An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein. Journal of Molecular Biology. 347: 911-9. PMID 15784252 DOI: 10.1016/J.Jmb.2005.01.064 |
0.5 |
|
| 2005 |
Bilsel O, Kayatekin C, Wallace LA, Matthews CR. A microchannel solution mixer for studying microsecond protein folding reactions Review of Scientific Instruments. 76: 014302. DOI: 10.1063/1.1834698 |
0.438 |
|
| 2004 |
Simler BR, Doyle BL, Matthews CR. Zinc binding drives the folding and association of the homo-trimeric gamma-carbonic anhydrase from Methanosarcina thermophila. Protein Engineering, Design & Selection : Peds. 17: 285-91. PMID 15051865 DOI: 10.1093/Protein/Gzh027 |
0.756 |
|
| 2004 |
Ibarra-Molero B, Zitzewitz JA, Matthews CR. Salt-bridges can stabilize but do not accelerate the folding of the homodimeric coiled-coil peptide GCN4-p1. Journal of Molecular Biology. 336: 989-96. PMID 15037063 DOI: 10.1016/J.Jmb.2003.12.069 |
0.506 |
|
| 2003 |
Wu Y, Matthews CR. Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein. Journal of Molecular Biology. 330: 1131-44. PMID 12860133 DOI: 10.1016/S0022-2836(03)00723-X |
0.494 |
|
| 2003 |
Arai M, Kataoka M, Kuwajima K, Matthews CR, Iwakura M. Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase. Journal of Molecular Biology. 329: 779-91. PMID 12787677 DOI: 10.1016/S0022-2836(03)00511-4 |
0.574 |
|
| 2003 |
Svensson AK, O'Neill JC, Matthews CR. The coordination of the isomerization of a conserved non-prolyl cis peptide bond with the rate-limiting steps in the folding of dihydrofolate reductase. Journal of Molecular Biology. 326: 569-83. PMID 12559923 DOI: 10.1016/S0022-2836(02)01444-4 |
0.504 |
|
| 2003 |
Vadrevu R, Falzone CJ, Matthews CR. Partial NMR assignments and secondary structure mapping of the isolated alpha subunit of Escherichia coli tryptophan synthase, a 29-kD TIM barrel protein. Protein Science : a Publication of the Protein Society. 12: 185-91. PMID 12493842 DOI: 10.1110/Ps.0221103 |
0.476 |
|
| 2002 |
Wallace LA, Matthews CR. Sequential vs. parallel protein-folding mechanisms: experimental tests for complex folding reactions. Biophysical Chemistry. 101: 113-31. PMID 12487994 DOI: 10.1016/S0301-4622(02)00155-2 |
0.506 |
|
| 2002 |
Wu Y, Matthews CR. Parallel channels and rate-limiting steps in complex protein folding reactions: prolyl isomerization and the alpha subunit of Trp synthase, a TIM barrel protein. Journal of Molecular Biology. 323: 309-25. PMID 12381323 DOI: 10.1016/S0022-2836(02)00922-1 |
0.498 |
|
| 2002 |
Wu Y, Matthews CR. A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein. Journal of Molecular Biology. 322: 7-13. PMID 12215410 DOI: 10.1016/S0022-2836(02)00737-4 |
0.496 |
|
| 2002 |
Knappenberger JA, Smith JE, Thorpe SH, Zitzewitz JA, Matthews CR. A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding. Journal of Molecular Biology. 321: 1-6. PMID 12139928 DOI: 10.1016/S0022-2836(02)00592-2 |
0.447 |
|
| 2002 |
Forsyth WR, Matthews CR. Folding mechanism of indole-3-glycerol phosphate synthase from Sulfolobus solfataricus: a test of the conservation of folding mechanisms hypothesis in (beta(alpha))(8) barrels. Journal of Molecular Biology. 320: 1119-33. PMID 12126630 DOI: 10.1016/S0022-2836(02)00557-0 |
0.548 |
|
| 2002 |
Steinbach PJ, Ionescu R, Matthews CR. Analysis of kinetics using a hybrid maximum-entropy/nonlinear-least-squares method: application to protein folding. Biophysical Journal. 82: 2244-55. PMID 11916879 DOI: 10.1016/S0006-3495(02)75570-7 |
0.353 |
|
| 2002 |
Wallace LA, Matthews CR. Highly divergent dihydrofolate reductases conserve complex folding mechanisms. Journal of Molecular Biology. 315: 193-211. PMID 11779239 DOI: 10.1006/Jmbi.2001.5230 |
0.551 |
|
| 2001 |
Gloss LM, Simler BR, Matthews CR. Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channels. Journal of Molecular Biology. 312: 1121-34. PMID 11580254 DOI: 10.1006/Jmbi.2001.4974 |
0.779 |
|
| 2001 |
Smith VF, Matthews CR. Testing the role of chain connectivity on the stability and structure of dihydrofolate reductase from E. coli: fragment complementation and circular permutation reveal stable, alternatively folded forms. Protein Science : a Publication of the Protein Society. 10: 116-28. PMID 11266600 DOI: 10.1110/Ps.26601 |
0.519 |
|
| 2001 |
Ibarra-Molero B, Makhatadze GI, Matthews CR. Mapping the energy surface for the folding reaction of the coiled-coil peptide GCN4-p1. Biochemistry. 40: 719-31. PMID 11170389 DOI: 10.1021/Bi001438E |
0.493 |
|
| 2000 |
Ionescu RM, Smith VF, O'Neill JC, Matthews CR. Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles. Biochemistry. 39: 9540-50. PMID 10924151 DOI: 10.1021/Bi000511Y |
0.517 |
|
| 2000 |
Bilsel O, Matthews CR. Barriers in protein folding reactions. Advances in Protein Chemistry. 53: 153-207. PMID 10751945 DOI: 10.1016/S0065-3233(00)53004-6 |
0.521 |
|
| 2000 |
Zitzewitz JA, Ibarra-Molero B, Fishel DR, Terry KL, Matthews CR. Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system. Journal of Molecular Biology. 296: 1105-16. PMID 10686107 DOI: 10.1006/Jmbi.2000.3507 |
0.696 |
|
| 2000 |
O’Neill JC, Matthews CR. Localized, stereochemically sensitive hydrophobic packing in an early folding intermediate of dihydrofolate reductase from Escherichia coli. Journal of Molecular Biology. 295: 737-744. PMID 10656786 DOI: 10.1006/Jmbi.1999.3403 |
0.502 |
|
| 1999 |
Gualfetti PJ, Iwakura M, Lee JC, Kihara H, Bilsel O, Zitzewitz JA, Matthews CR. Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. Biochemistry. 38: 13367-78. PMID 10529212 DOI: 10.1021/Bi991296S |
0.4 |
|
| 1999 |
Gualfetti PJ, Bilsel O, Matthews CR. The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. Protein Science : a Publication of the Protein Society. 8: 1623-35. PMID 10452606 DOI: 10.1110/Ps.8.8.1623 |
0.439 |
|
| 1999 |
Zitzewitz JA, Matthews CR. Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein. Biochemistry. 38: 10205-14. PMID 10433729 DOI: 10.1021/bi9909041 |
0.472 |
|
| 1999 |
Zitzewitz JA, Gualfetti PJ, Perkons IA, Wasta SA, Matthews CR. Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. Protein Science : a Publication of the Protein Society. 8: 1200-9. PMID 10386870 DOI: 10.1110/Ps.8.6.1200 |
0.486 |
|
| 1999 |
Ionescu RM, Matthews CR. Folding under the influence. Nature Structural Biology. 6: 304-7. PMID 10201391 DOI: 10.1038/7534 |
0.327 |
|
| 1999 |
Bilsel O, Yang L, Zitzewitz JA, Beechem JM, Matthews CR. Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time. Biochemistry. 38: 4177-87. PMID 10194334 DOI: 10.1021/bi9829433 |
0.424 |
|
| 1999 |
Bilsel O, Zitzewitz JA, Bowers KE, Matthews CR. Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry. 38: 1018-29. PMID 9893998 DOI: 10.1021/bi982365q |
0.443 |
|
| 1998 |
Gloss LM, Matthews CR. The barriers in the bimolecular and unimolecular folding reactions of the dimeric core domain of Escherichia coli Trp repressor are dominated by enthalpic contributions. Biochemistry. 37: 16000-10. PMID 9843407 DOI: 10.1021/bi981694f |
0.426 |
|
| 1998 |
Gloss LM, Matthews CR. Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: a nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate. Biochemistry. 37: 15990-9. PMID 9843406 DOI: 10.1021/bi981511p |
0.441 |
|
| 1998 |
Zhang J, Matthews CR. The role of ligand binding in the kinetic folding mechanism of human p21(H-ras) protein. Biochemistry. 37: 14891-9. PMID 9778365 DOI: 10.1021/bi981116z |
0.317 |
|
| 1998 |
Zhang J, Matthews CR. Ligand binding is the principal determinant of stability for the p21(H)-ras protein. Biochemistry. 37: 14881-90. PMID 9778364 DOI: 10.1021/bi9811157 |
0.303 |
|
| 1998 |
Shao X, Matthews CR. Single-tryptophan mutants of monomeric tryptophan repressor: optical spectroscopy reveals nonnative structure in a model for an early folding intermediate. Biochemistry. 37: 7850-8. PMID 9601046 DOI: 10.1021/bi973171y |
0.448 |
|
| 1997 |
Gegg CV, Bowers KE, Matthews CR. Probing minimal independent folding units in dihydrofolate reductase by molecular dissection. Protein Science : a Publication of the Protein Society. 6: 1885-92. PMID 9300488 DOI: 10.1002/pro.5560060909 |
0.427 |
|
| 1997 |
Shao X, Hensley P, Matthews CR. Construction and characterization of monomeric tryptophan repressor: a model for an early intermediate in the folding of a dimeric protein. Biochemistry. 36: 9941-9. PMID 9245428 DOI: 10.1021/bi9707786 |
0.471 |
|
| 1997 |
Gloss LM, Matthews CR. Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor. Biochemistry. 36: 5612-23. PMID 9153401 DOI: 10.1021/bi970056e |
0.489 |
|
| 1997 |
Goldberg MS, Zhang J, Sondek S, Matthews CR, Fox RO, Horwich AL. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proceedings of the National Academy of Sciences of the United States of America. 94: 1080-5. PMID 9037009 DOI: 10.1073/pnas.94.4.1080 |
0.45 |
|
| 1996 |
Saab-Rincón G, Gualfetti PJ, Matthews CR. Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. Biochemistry. 35: 1988-94. PMID 8639683 DOI: 10.1021/bi951726o |
0.388 |
|
| 1995 |
Jones BE, Beechem JM, Matthews CR. Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy. Biochemistry. 34: 1867-77. PMID 7849046 |
0.721 |
|
| 1995 |
Jones BE, Matthews CR. Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR. Protein Science : a Publication of the Protein Society. 4: 167-77. PMID 7757007 DOI: 10.1002/Pro.5560040204 |
0.704 |
|
| 1995 |
Luo J, Iwakura M, Matthews CR. Detection of a stable intermediate in the thermal unfolding of a cysteine-free form of dihydrofolate reductase from Escherichia coli. Biochemistry. 34: 10669-75. PMID 7654721 |
0.389 |
|
| 1995 |
Iwakura M, Jones BE, Luo J, Matthews CR. A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli. Journal of Biochemistry. 117: 480-8. PMID 7629011 |
0.685 |
|
| 1995 |
Mann CJ, Shao X, Matthews CR. Characterization of the slow folding reactions of trp aporepressor from Escherichia coli by mutational analysis of prolines and catalysis by a peptidyl-prolyl isomerase. Biochemistry. 34: 14573-80. PMID 7578063 DOI: 10.1021/bi00044a036 |
0.46 |
|
| 1995 |
Zitzewitz JA, Bilsel O, Luo J, Jones BE, Matthews CR. Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy. Biochemistry. 34: 12812-9. PMID 7548036 |
0.709 |
|
| 1994 |
Chen X, Matthews CR. Thermodynamic properties of the transition state for the rate-limiting step in the folding of the alpha subunit of tryptophan synthase. Biochemistry. 33: 6356-62. PMID 8193152 |
0.362 |
|
| 1994 |
Falzone CJ, Cavanagh J, Cowart M, Palmer AG, Matthews CR, Benkovic SJ, Wright PE. 1H, 15N and 13C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductase. Journal of Biomolecular Nmr. 4: 349-66. PMID 8019142 DOI: 10.1007/Bf00179346 |
0.507 |
|
| 1994 |
Jones BE, Jennings PA, Pierre RA, Matthews CR. Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding. Biochemistry. 33: 15250-8. PMID 7803387 |
0.763 |
|
| 1993 |
Tsuji T, Chrunyk BA, Chen X, Matthews CR. Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. Biochemistry. 32: 5566-75. PMID 8504078 |
0.438 |
|
| 1993 |
Mann CJ, Matthews CR. Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding. Biochemistry. 32: 5282-90. PMID 8499433 |
0.33 |
|
| 1993 |
Jennings PA, Finn BE, Jones BE, Matthews CR. A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model. Biochemistry. 32: 3783-9. PMID 8466916 |
0.778 |
|
| 1993 |
Mann CJ, Royer CA, Matthews CR. Tryptophan replacements in the trp aporepressor from Escherichia coli: probing the equilibrium and kinetic folding models. Protein Science : a Publication of the Protein Society. 2: 1853-61. PMID 8268796 DOI: 10.1002/Pro.5560021107 |
0.505 |
|
| 1993 |
Royer CA, Mann CJ, Matthews CR. Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants. Protein Science : a Publication of the Protein Society. 2: 1844-52. PMID 8268795 DOI: 10.1002/Pro.5560021106 |
0.332 |
|
| 1993 |
Saab-Rincón G, Froebe CL, Matthews CR. Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration. Biochemistry. 32: 13981-90. PMID 8268176 DOI: 10.1021/bi00213a031 |
0.384 |
|
| 1993 |
Iwakura M, Jones BE, Falzone CJ, Matthews CR. Collapse of parallel folding channels in dihydrofolate reductase from Escherichia coli by site-directed mutagenesis. Biochemistry. 32: 13566-74. PMID 8257692 |
0.724 |
|
| 1993 |
Zitzewitz JA, Matthews CR. Protein engineering strategies in examining protein folding intermediates. Current opinion in Structural Biology 1993, 3:594-600 Current Opinion in Structural Biology. 3: 594-600. DOI: 10.1016/0959-440X(93)90089-4 |
0.504 |
|
| 1992 |
Texter FL, Spencer DB, Rosenstein R, Matthews CR. Intramolecular catalysis of a proline isomerization reaction in the folding of dihydrofolate reductase. Biochemistry. 31: 5687-91. PMID 1610817 DOI: 10.1021/Bi00140A001 |
0.513 |
|
| 1992 |
Chen X, Rambo R, Matthews CR. Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. Biochemistry. 31: 2219-23. PMID 1540577 DOI: 10.1021/Bi00123A002 |
0.485 |
|
| 1992 |
Iwakura M, Matthews CR. Construction and characterization of a single polypeptide chain containing two enzymatically active dihydrofolate reductase domains. Protein Engineering. 5: 791-6. PMID 1287660 DOI: 10.1093/protein/5.8.791 |
0.394 |
|
| 1991 |
Kuwajima K, Garvey EP, Finn BE, Matthews CR, Sugai S. Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry. 30: 7693-703. PMID 1868049 DOI: 10.1021/BI00245A005 |
0.383 |
|
| 1991 |
Jennings PA, Saalau-Bethell SM, Finn BE, Chen XW, Matthews CR. Mutational analysis of protein folding mechanisms. Methods in Enzymology. 202: 113-26. PMID 1784172 DOI: 10.1016/0076-6879(91)02009-X |
0.658 |
|
| 1990 |
Gittelman MS, Matthews CR. Folding and stability of trp aporepressor from Escherichia coli Biochemistry®. 29: 7011-7020. PMID 2223756 |
0.46 |
|
| 1990 |
Chrunyk BA, Matthews CR. Role of diffusion in the folding of the α subunit of tryptophan synthase from Escherichia coli Biochemistry®. 2149-2154. PMID 2183877 |
0.341 |
|
| 1989 |
Garvey EP, Matthews CR. Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli Biochemistry. 28: 2083-2093. PMID 2655702 |
0.447 |
|
| 1989 |
Garvey EP, Swank J, Matthews CR. A hydrophobic cluster forms early in the folding of dihydrofolate reductase Proteins: Structure, Function and Genetics. 6: 259-266. PMID 2622906 DOI: 10.1002/prot.340060308 |
0.361 |
|
| 1988 |
Stackhouse TM, Onuffer JJ, Matthews CR, Ahmed SA, Miles EW. Folding of homologous proteins: Conservation of the folding mechanism of the α subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids Biochemistry. 27: 824-832. PMID 3280027 |
0.358 |
|
| 1987 |
Matthews CR, Hurle MR. Mutant sequences as probes of protein folding mechanisms Bioessays. 6: 254-257. PMID 3619886 DOI: 10.1002/Bies.950060603 |
0.486 |
|
| 1987 |
Hurle MR, Matthews CR, Cohen FE, Kuntz ID, Toumadje A, Johnson WC. Prediction of the tertiary structure of the α-subunit of tryptophan synthase Proteins: Structure, Function and Genetics. 2: 210-224. PMID 3328862 DOI: 10.1002/Prot.340020306 |
0.372 |
|
| 1987 |
Hurle MR, Michelotti GA, Crisanti MM, Matthews CR. Characterization of a slow folding reaction for the alpha subunit of tryptophan synthase Proteins. 2: 54-63. PMID 3328859 DOI: 10.1002/Prot.340020107 |
0.52 |
|
| 1987 |
Hurle MR, Matthews CR. Proline isomerization and the slow folding reactions of the α subunit of tryptophan synthase from Escherichia coli Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 913: 179-184. PMID 3297161 DOI: 10.1016/0167-4838(87)90328-1 |
0.463 |
|
| 1986 |
Hurle MR, Tweedy NB, Matthews CR. Synergism in folding of a double mutant of the α subunit of tryptophan synthase Biochemistry. 25: 6356-6360. PMID 3539187 |
0.398 |
|
| 1986 |
Beasty AM, Hurle MR, Manz JT, Stackhouse T, Onuffer JJ, Matthews CR. Effects of the phenylalanine-22----leucine, glutamic acid-49----methionine, glycine-234----aspartic acid, and glycine-234----lysine mutations on the folding and stability of the alpha subunit of tryptophan synthase from Escherichia coli. Biochemistry. 25: 2965-74. PMID 2872918 |
0.412 |
|
| 1985 |
Beasty AM, Matthews CR. Characterization of an early intermediate in the folding of the α subunit of tryptophan synthase by hydrogen exchange measurement Biochemistry. 24: 3547-3553. PMID 3899169 |
0.393 |
|
| 1982 |
Recchia J, Matthews CR, Rhee Mj, Horrocks WD. Interresidue distance measurements in proteins Fluorescent energy transfer between tryptophans and a Ru(III)(NH3)5-histidine complex in α-lytic protease and lysozyme Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 702: 105-111. PMID 6802183 DOI: 10.1016/0167-4838(82)90032-2 |
0.416 |
|
| 1981 |
Crisanti MM, Matthews CR. Characterization of the slow steps in the folding of the a subunit of tryptophan synthase Biochemistry. 20: 2700-2706. PMID 7016182 |
0.345 |
|
| 1981 |
Matthews CR, Crisanti MM. Urea-induced unfolding of the α subunit of tryptophan synthase: Evidence for a multistate process Biochemistry. 20: 784-792. PMID 7011372 |
0.334 |
|
| 1981 |
Matthews CR, Recchia J, Froebe CL. The pentaammineruthenium(III)histidine complex in ribonuclease A: Application to the assignment of histidine proton resonances Analytical Biochemistry. 112: 329-337. PMID 6266280 DOI: 10.1016/0003-2697(81)90301-8 |
0.355 |
|
| 1973 |
Westmoreland DG, Matthews CR. Nuclear magnetic resonance study of the thermal denaturation of ribonuclease A: implications for multistate behavior at low pH Proceedings of the National Academy of Sciences of the United States of America. 70: 914-918. PMID 4515001 DOI: 10.1073/Pnas.70.3.914 |
0.338 |
|
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