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C. Robert Matthews - Publications

Affiliations: 
Biochemistry & Molecular Pharmacology University of Massachusetts Medical School, Worcester, MA, United States 
Area:
Protein Folding
Website:
http://profiles.umassmed.edu/profiles/ProfileDetails.aspx?From=SE&Person=603

102 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
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  0.84
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  0.84
2014 Lee CA, Lee MB, Matthews CR, Tatakis DN. Subpontic osseous hyperplasia: a case series and literature review. General Dentistry. 62: 46-52. PMID 24983170  0.36
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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 Gō model simulation. Journal of Molecular Biology. 374: 528-46. PMID 17942114 DOI: 10.1016/j.jmb.2007.09.024  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
2007 Bilsel O, Wu Y, Kayatekin C, Matthews CR. Merging microsecond mixing and time-correlated single-photon counting: Using time-resolved FRET and time-resolved anisotropy to probe early events in protein folding Proceedings of Spie - the International Society For Optical Engineering. 6771. DOI: 10.1117/12.734486  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.44
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  0.84
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  0.84
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  0.84
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  0.84
1999 Ionescu RM, Matthews CR. Folding under the influence. Nature Structural Biology. 6: 304-7. PMID 10201391 DOI: 10.1038/7534  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
1997 Zitzewitz BJA, Bowers KE, Yang L, Beechem JM, Matthews CR. Elucidating the folding mechanism of AN o/3 barrel protein O Faseb Journal. 11: A1043.  0.84
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  0.84
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  0.76
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  0.84
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  0.84
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  0.84
1995 Li Z, Maki AH, Eftink MR, Mann CJ, Matthews CR. Characterization of the tryptophan binding site of Escherichia coli tryptophan holorepressor by phosphorescence and optical detection of magnetic resonance of a tryptophan-free mutant. Biochemistry. 34: 12866-70. PMID 7548042  0.84
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  0.84
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  0.84
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  0.84
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  0.96
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  0.84
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  0.84
1993 Lecomte JT, Matthews CR. Unraveling the mechanism of protein folding: new tricks for an old problem. Protein Engineering. 6: 1-10. PMID 8433962 DOI: 10.1093/protein/6.1.1  0.84
1993 Eftink MR, Ramsay GD, Burns L, Maki AH, Mann CJ, Matthews CR, Ghiron CA. Luminescence studies with trp repressor and its single-tryptophan mutants. Biochemistry. 32: 9189-98. PMID 8369286  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
1990 Gittelman MS, Matthews CR. Folding and stability of trp aporepressor from Escherichia coli Biochemistry®. 29: 7011-7020. PMID 2223756  0.84
1990 Garvey EP, Matthews CR. Site-directed mutagenesis and its application to protein folding Biotechnology (Reading, Mass.). 14: 37-63. PMID 2183900  0.84
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  0.84
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  0.84
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  0.84
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  0.84
1987 Matthews CR, Hurle MR. Mutant sequences as probes of protein folding mechanisms Bioessays. 6: 254-257. PMID 3619886  0.84
1987 Matthews CR. [26] Effect of point mutations of the folding of globular proteins Methods in Enzymology. 154: 498-511. PMID 3431461 DOI: 10.1016/0076-6879(87)54092-7  0.84
1987 Stackhouse T, Onuffer JJ, Matthews CR, Ahmed SA, Miles EW. The role of protein folding in the evolution of protein sequences Cold Spring Harbor Symposia On Quantitative Biology. 52: 537-544. PMID 3331344  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
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  0.84
1985 Herndon CS, Riggs AD, Matthews CR. Examination of the role of arginine-44 in dihydrofolate reductase by site-directed mutagenesis Federation Proceedings. 44: No. 3737.  0.84
1983 Matthews CR, Crisanti MM, Manz JT, Gepner GL. Effect of a single amino acid substitution on the folding of the alpha subunit of tryptophan synthase. Biochemistry. 22: 1445-52. PMID 6132619  0.84
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  0.84
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  0.84
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  0.84
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