| Year |
Citation |
Score |
| 2017 |
Matthews B. David Davies: Structural Biologist and Mentor. Protein Science : a Publication of the Protein Society. PMID 28168800 DOI: 10.1002/Pro.3130 |
0.349 |
|
| 2015 |
Matthews BW. Which of the 100,000 structures in the protein data bank are reliable? Protein Science : a Publication of the Protein Society. 24: 589-91. PMID 25676441 DOI: 10.1002/Pro.2662 |
0.38 |
|
| 2014 |
Matthews BW. Protein science "best paper" awards to Mark Landau and Brian Ziemba. Protein Science : a Publication of the Protein Society. 23: 515-6. PMID 24692246 DOI: 10.1002/Pro.2447 |
0.37 |
|
| 2014 |
Matthews B. Protein Crystallography: Getting in on the Ground Floor Acta Crystallographica Section a Foundations and Advances. 70: C931-C931. DOI: 10.1107/S2053273314090688 |
0.42 |
|
| 2012 |
Juers DH, Matthews BW, Huber RE. LacZ β-galactosidase: structure and function of an enzyme of historical and molecular biological importance. Protein Science : a Publication of the Protein Society. 21: 1792-807. PMID 23011886 DOI: 10.1002/Pro.2165 |
0.762 |
|
| 2011 |
Matthews BW. Stoichiometry versus hydrophobicity in protein folding. Journal of Biomolecular Structure & Dynamics. 28: 589-91; discussion 6. PMID 21142227 DOI: 10.1080/073911011010524956 |
0.36 |
|
| 2010 |
Matthews BW. Peripatetic proteins. Protein Science : a Publication of the Protein Society. 19: 1279-80. PMID 20499369 DOI: 10.1002/Pro.422 |
0.327 |
|
| 2010 |
Baase WA, Liu L, Tronrud DE, Matthews BW. Lessons from the lysozyme of phage T4. Protein Science : a Publication of the Protein Society. 19: 631-41. PMID 20095051 DOI: 10.1002/Pro.344 |
0.545 |
|
| 2009 |
Liu L, Marwitz AJ, Matthews BW, Liu SY. Boron mimetics: 1,2-dihydro-1,2-azaborines bind inside a nonpolar cavity of T4 lysozyme. Angewandte Chemie (International Ed. in English). 48: 6817-9. PMID 19688806 DOI: 10.1002/Anie.200903390 |
0.465 |
|
| 2009 |
Liu L, Baase WA, Michael MM, Matthews BW. Use of stabilizing mutations to engineer a charged group within a ligand-binding hydrophobic cavity in T4 lysozyme. Biochemistry. 48: 8842-51. PMID 19663503 DOI: 10.1021/Bi900685J |
0.53 |
|
| 2009 |
Juers DH, Rob B, Dugdale ML, Rahimzadeh N, Giang C, Lee M, Matthews BW, Huber RE. Direct and indirect roles of His-418 in metal binding and in the activity of beta-galactosidase (E. coli). Protein Science : a Publication of the Protein Society. 18: 1281-92. PMID 19472413 DOI: 10.1002/Pro.140 |
0.744 |
|
| 2009 |
Matthews BW. Racemic crystallography--easy crystals and easy structures: what's not to like? Protein Science : a Publication of the Protein Society. 18: 1135-8. PMID 19472321 DOI: 10.1002/Pro.125 |
0.394 |
|
| 2009 |
Mooers BH, Baase WA, Wray JW, Matthews BW. Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. Protein Science : a Publication of the Protein Society. 18: 871-80. PMID 19384988 DOI: 10.1002/Pro.94 |
0.778 |
|
| 2009 |
Mooers BH, Tronrud DE, Matthews BW. Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His. Protein Science : a Publication of the Protein Society. 18: 863-70. PMID 19384984 DOI: 10.1002/Pro.93 |
0.77 |
|
| 2009 |
Matthews BW, Liu L. A review about nothing: are apolar cavities in proteins really empty? Protein Science : a Publication of the Protein Society. 18: 494-502. PMID 19241368 DOI: 10.1002/Pro.61 |
0.45 |
|
| 2009 |
Tronrud DE, Matthews BW. Sorting the chaff from the wheat at the PDB. Protein Science : a Publication of the Protein Society. 18: 2-5. PMID 19177345 DOI: 10.1002/Pro.13 |
0.339 |
|
| 2009 |
Liu L, Baase WA, Matthews BW. Halogenated benzenes bound within a non-polar cavity in T4 lysozyme provide examples of I...S and I...Se halogen-bonding. Journal of Molecular Biology. 385: 595-605. PMID 19014950 DOI: 10.1016/J.Jmb.2008.10.086 |
0.49 |
|
| 2009 |
Palmer AG, Matthews BW. Interactive graphics return to protein science Protein Science. 18: 677. DOI: 10.1002/Pro.103 |
0.32 |
|
| 2008 |
Ando N, Barstow B, Baase WA, Fields A, Matthews BW, Gruner SM. Structural and thermodynamic characterization of T4 lysozyme mutants and the contribution of internal cavities to pressure denaturation. Biochemistry. 47: 11097-109. PMID 18816066 DOI: 10.1021/Bi801287M |
0.309 |
|
| 2008 |
Liu L, Quillin ML, Matthews BW. Use of experimental crystallographic phases to examine the hydration of polar and nonpolar cavities in T4 lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 105: 14406-11. PMID 18780783 DOI: 10.1073/Pnas.0806307105 |
0.463 |
|
| 2008 |
Kingston RL, Gay LS, Baase WS, Matthews BW. Structure of the nucleocapsid-binding domain from the mumps virus polymerase; an example of protein folding induced by crystallization. Journal of Molecular Biology. 379: 719-31. PMID 18468621 DOI: 10.1016/J.Jmb.2007.12.080 |
0.73 |
|
| 2008 |
Addlagatta A, Gay L, Matthews BW. Structural basis for the unusual specificity of Escherichia coli aminopeptidase N. Biochemistry. 47: 5303-11. PMID 18416562 DOI: 10.1021/Bi7022333 |
0.683 |
|
| 2008 |
Bradshaw RA, Eisenberg DS, Hermodson MA, Villafranca JJ, Matthews BW, Sauer RT. Thank you, Hans! Protein Science. 7: 231-232. DOI: 10.1002/Pro.5560070201 |
0.428 |
|
| 2007 |
Juers DH, Lovelace J, Bellamy HD, Snell EH, Matthews BW, Borgstahl GE. Changes to crystals of Escherichia coli beta-galactosidase during room-temperature/low-temperature cycling and their relation to cryo-annealing. Acta Crystallographica. Section D, Biological Crystallography. 63: 1139-53. PMID 18007029 DOI: 10.1107/S0907444907045040 |
0.703 |
|
| 2007 |
Matthews BW. Protein Structure Initiative: getting into gear. Nature Structural & Molecular Biology. 14: 459-60. PMID 17549078 DOI: 10.1038/Nsmb0607-459 |
0.359 |
|
| 2007 |
Matthews BW. Five retracted structure reports: inverted or incorrect? Protein Science : a Publication of the Protein Society. 16: 1013-6. PMID 17473006 DOI: 10.1110/Ps.072888607 |
0.304 |
|
| 2007 |
Collins MD, Quillin ML, Hummer G, Matthews BW, Gruner SM. Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography. Journal of Molecular Biology. 367: 752-63. PMID 17292912 DOI: 10.1016/J.Jmb.2006.12.021 |
0.4 |
|
| 2006 |
Quillin ML, Wingfield PT, Matthews BW. Determination of solvent content in cavities in IL-1beta using experimentally phased electron density. Proceedings of the National Academy of Sciences of the United States of America. 103: 19749-53. PMID 17179045 DOI: 10.1073/Pnas.0609442104 |
0.304 |
|
| 2006 |
Hu X, Addlagatta A, Lu J, Matthews BW, Liu JO. Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression. Proceedings of the National Academy of Sciences of the United States of America. 103: 18148-53. PMID 17114291 DOI: 10.1073/Pnas.0608389103 |
0.609 |
|
| 2006 |
Addlagatta A, Gay L, Matthews BW. Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site. Proceedings of the National Academy of Sciences of the United States of America. 103: 13339-44. PMID 16938892 DOI: 10.1073/Pnas.0606167103 |
0.692 |
|
| 2006 |
Addlagatta A, Matthews BW. Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human Type 1 methionine aminopeptidase. Protein Science : a Publication of the Protein Society. 15: 1842-8. PMID 16823043 DOI: 10.1110/Ps.062278006 |
0.676 |
|
| 2006 |
Hu X, Addlagatta A, Matthews BW, Liu JO. Identification of pyridinylpyrimidines as inhibitors of human methionine aminopeptidases. Angewandte Chemie (International Ed. in English). 45: 3772-5. PMID 16724298 DOI: 10.1002/Anie.200600757 |
0.575 |
|
| 2006 |
Yousef MS, Bischoff N, Dyer CM, Baase WA, Matthews BW. Guanidinium derivatives bind preferentially and trigger long-distance conformational changes in an engineered T4 lysozyme. Protein Science : a Publication of the Protein Society. 15: 853-61. PMID 16600969 DOI: 10.1110/Ps.052020606 |
0.379 |
|
| 2006 |
Sagermann M, Baase WA, Matthews BW. Sequential reorganization of beta-sheet topology by insertion of a single strand. Protein Science : a Publication of the Protein Society. 15: 1085-92. PMID 16597830 DOI: 10.1110/Ps.052018006 |
0.777 |
|
| 2006 |
Wood ZA, Weaver LH, Brown PH, Beckett D, Matthews BW. Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution. Journal of Molecular Biology. 357: 509-23. PMID 16438984 DOI: 10.1016/J.Jmb.2005.12.066 |
0.815 |
|
| 2006 |
Mooers BH, Matthews BW. Extension to 2268 atoms of direct methods in the ab initio determination of the unknown structure of bacteriophage P22 lysozyme. Acta Crystallographica. Section D, Biological Crystallography. 62: 165-76. PMID 16421448 DOI: 10.1107/S0907444905037212 |
0.743 |
|
| 2006 |
Hu X, Addlagatta A, Matthews BW, Liu JO. Cover Picture: Identification of Pyridinylpyrimidines as Inhibitors of Human Methionine Aminopeptidases (Angew. Chem. Int. Ed. 23/2006) Angewandte Chemie International Edition. 45: 3717-3717. DOI: 10.1002/Anie.200690079 |
0.577 |
|
| 2006 |
Hu X, Addlagatta A, Matthews BW, Liu JO. Titelbild: Identification of Pyridinylpyrimidines as Inhibitors of Human Methionine Aminopeptidases (Angew. Chem. 23/2006) Angewandte Chemie. 118: 3801-3801. DOI: 10.1002/Ange.200690079 |
0.577 |
|
| 2005 |
Juers DH, Kim J, Matthews BW, Sieburth SM. Structural analysis of silanediols as transition-state-analogue inhibitors of the benchmark metalloprotease thermolysin. Biochemistry. 44: 16524-8. PMID 16342943 DOI: 10.1021/Bi051346V |
0.737 |
|
| 2005 |
Addlagatta A, Hu X, Liu JO, Matthews BW. Structural basis for the functional differences between type I and type II human methionine aminopeptidases. Biochemistry. 44: 14741-9. PMID 16274222 DOI: 10.1021/Bi051691K |
0.681 |
|
| 2005 |
Collins MD, Hummer G, Quillin ML, Matthews BW, Gruner SM. Cooperative water filling of a nonpolar protein cavity observed by high-pressure crystallography and simulation. Proceedings of the National Academy of Sciences of the United States of America. 102: 16668-71. PMID 16269539 DOI: 10.1073/Pnas.0508224102 |
0.348 |
|
| 2005 |
Desvaux H, Dubois L, Huber G, Quillin ML, Berthault P, Matthews BW. Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy. Journal of the American Chemical Society. 127: 11676-83. PMID 16104744 DOI: 10.1021/Ja053074P |
0.399 |
|
| 2005 |
Matthews BW. The structure of E. coli beta-galactosidase. Comptes Rendus Biologies. 328: 549-56. PMID 15950161 DOI: 10.1016/J.Crvi.2005.03.006 |
0.394 |
|
| 2005 |
Addlagatta A, Quillin ML, Omotoso O, Liu JO, Matthews BW. Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome. Biochemistry. 44: 7166-74. PMID 15882055 DOI: 10.1021/Bi0501176 |
0.71 |
|
| 2005 |
Yousef MS, Matthews BW. Structural basis of Prospero-DNA interaction: implications for transcription regulation in developing cells. Structure (London, England : 1993). 13: 601-7. PMID 15837198 DOI: 10.1016/J.Str.2005.01.023 |
0.393 |
|
| 2005 |
Ostheimer GJ, Hadjivassiliou H, Hadjivasiliou H, Kloer DP, Barkan A, Matthews BW. Structural analysis of the group II intron splicing factor CRS2 yields insights into its protein and RNA interaction surfaces. Journal of Molecular Biology. 345: 51-68. PMID 15567410 DOI: 10.1016/J.Jmb.2004.10.032 |
0.81 |
|
| 2005 |
Zhang XJ, Matthews BW. Enhancement of the method of molecular replacement by incorporation of known structural information. Acta Crystallographica. Section D, Biological Crystallography. 50: 675-86. PMID 15299365 DOI: 10.1107/S0907444994002295 |
0.386 |
|
| 2005 |
Kingston R, Hamel D, Dahlquist F, Matthews B. Measles virus P protein (amino acids 457-407) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr6568 |
0.662 |
|
| 2005 |
Ostheimer GJ, Hadjivassiliou H, Kloer DP, Barkan A, Matthews BW. Corrigendum to “Structural Analysis of the Group II Intron Splicing Factor CRS2 Yields Insights into its Protein and RNA Interaction Surfaces” [J. Mol. Biol. (2005) 345, 51–68] Journal of Molecular Biology. 350: 185. DOI: 10.1016/J.Jmb.2005.05.007 |
0.769 |
|
| 2004 |
Juers DH, Matthews BW. Cryo-cooling in macromolecular crystallography: advantages, disadvantages and optimization. Quarterly Reviews of Biophysics. 37: 105-19. PMID 15999418 DOI: 10.1017/S0033583504004007 |
0.703 |
|
| 2004 |
Mooers BH, Matthews BW. Use of an ion-binding site to bypass the 1000-atom limit to structure determination by direct methods. Acta Crystallographica. Section D, Biological Crystallography. 60: 1726-37. PMID 15388918 DOI: 10.1107/S0907444904017020 |
0.761 |
|
| 2004 |
Dyer CM, Quillin ML, Campos A, Lu J, McEvoy MM, Hausrath AC, Westbrook EM, Matsumura P, Matthews BW, Dahlquist FW. Structure of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide. Journal of Molecular Biology. 342: 1325-35. PMID 15351654 DOI: 10.1016/J.Jmb.2004.07.084 |
0.767 |
|
| 2004 |
He MM, Wood ZA, Baase WA, Xiao H, Matthews BW. Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation. Protein Science : a Publication of the Protein Society. 13: 2716-24. PMID 15340171 DOI: 10.1110/Ps.04875504 |
0.788 |
|
| 2004 |
Yousef MS, Baase WA, Matthews BW. Use of sequence duplication to engineer a ligand-triggered, long-distance molecular switch in T4 lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 101: 11583-6. PMID 15286283 DOI: 10.1073/Pnas.0404482101 |
0.466 |
|
| 2004 |
Kingston RL, Hamel DJ, Gay LS, Dahlquist FW, Matthews BW. Structural basis for the attachment of a paramyxoviral polymerase to its template. Proceedings of the National Academy of Sciences of the United States of America. 101: 8301-6. PMID 15159535 DOI: 10.1073/Pnas.0402690101 |
0.723 |
|
| 2004 |
Wei BQ, Weaver LH, Ferrari AM, Matthews BW, Shoichet BK. Testing a flexible-receptor docking algorithm in a model binding site. Journal of Molecular Biology. 337: 1161-82. PMID 15046985 DOI: 10.1016/J.Jmb.2004.02.015 |
0.685 |
|
| 2004 |
Juers DH, Matthews BW. The role of solvent transport in cryo-annealing of macromolecular crystals. Acta Crystallographica. Section D, Biological Crystallography. 60: 412-21. PMID 14993664 DOI: 10.1107/S0907444903027938 |
0.697 |
|
| 2004 |
Sagermann M, Baase WA, Mooers BH, Gay L, Matthews BW. Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding. Biochemistry. 43: 1296-301. PMID 14756565 DOI: 10.1021/Bi035702Q |
0.821 |
|
| 2004 |
Carmel AB, Matthews BW. Crystal structure of the BstDEAD N-terminal domain: a novel DEAD protein from Bacillus stearothermophilus. Rna (New York, N.Y.). 10: 66-74. PMID 14681586 DOI: 10.1261/Rna.5134304 |
0.83 |
|
| 2003 |
Matthews BW. Transformations in structural biology: a personal view. Methods in Enzymology. 368: 3-11. PMID 14674265 DOI: 10.1016/S0076-6879(03)68001-8 |
0.334 |
|
| 2003 |
Juers DH, Hakda S, Matthews BW, Huber RE. Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase. Biochemistry. 42: 13505-11. PMID 14621996 DOI: 10.1021/Bi035506J |
0.735 |
|
| 2003 |
Quillin ML, Matthews BW. Selling candles in a post-Edison world: phasing with noble gases bound within engineered sites. Acta Crystallographica. Section D, Biological Crystallography. 59: 1930-4. PMID 14573947 DOI: 10.1107/S0907444903018018 |
0.394 |
|
| 2003 |
Carmel AB, Matthews BW. Purification, crystallization and preliminary X-ray analysis of the novel DEAD protein BstDEAD from Bacillus stearothermophilus. Acta Crystallographica. Section D, Biological Crystallography. 59: 1869-70. PMID 14501141 DOI: 10.1107/S0907444903018389 |
0.808 |
|
| 2003 |
Mooers BH, Datta D, Baase WA, Zollars ES, Mayo SL, Matthews BW. Repacking the Core of T4 lysozyme by automated design. Journal of Molecular Biology. 332: 741-56. PMID 12963380 DOI: 10.1016/S0022-2836(03)00856-8 |
0.784 |
|
| 2003 |
Sagermann M, Gay L, Matthews BW. Long-distance conformational changes in a protein engineered by modulated sequence duplication. Proceedings of the National Academy of Sciences of the United States of America. 100: 9191-5. PMID 12869697 DOI: 10.1073/Pnas.1633549100 |
0.78 |
|
| 2003 |
Copik AJ, Swierczek SI, Lowther WT, D'souza VM, Matthews BW, Holz RC. Kinetic and spectroscopic characterization of the H178A methionyl aminopeptidase from Escherichia coli. Biochemistry. 42: 6283-92. PMID 12755633 DOI: 10.1021/Bi027327S |
0.634 |
|
| 2003 |
Gassner NC, Baase WA, Mooers BH, Busam RD, Weaver LH, Lindstrom JD, Quillin ML, Matthews BW. Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability. Biophysical Chemistry. 100: 325-40. PMID 12646375 DOI: 10.1016/S0301-4622(02)00290-9 |
0.82 |
|
| 2003 |
Peters RJ, Carter OA, Zhang Y, Matthews BW, Croteau RB. Bifunctional abietadiene synthase: mutual structural dependence of the active sites for protonation-initiated and ionization-initiated cyclizations. Biochemistry. 42: 2700-7. PMID 12614165 DOI: 10.1021/Bi020492N |
0.407 |
|
| 2003 |
Shoemaker GK, Juers DH, Coombs JM, Matthews BW, Craig DB. Crystallization of beta-galactosidase does not reduce the range of activity of individual molecules. Biochemistry. 42: 1707-10. PMID 12578385 DOI: 10.1021/Bi0204138 |
0.711 |
|
| 2002 |
Zhang XJ, Baase WA, Matthews BW. A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. Biophysical Chemistry. 101: 43-56. PMID 12487988 DOI: 10.1016/S0301-4622(02)00193-X |
0.477 |
|
| 2002 |
Lowther WT, Matthews BW. Metalloaminopeptidases: common functional themes in disparate structural surroundings. Chemical Reviews. 102: 4581-608. PMID 12475202 DOI: 10.1021/Cr0101757 |
0.644 |
|
| 2002 |
Ostheimer GJ, Barkan A, Matthews BW. Crystal structure of E. coli YhbY: a representative of a novel class of RNA binding proteins. Structure (London, England : 1993). 10: 1593-601. PMID 12429100 DOI: 10.1016/S0969-2126(02)00886-9 |
0.807 |
|
| 2002 |
Ryter JM, Doe CQ, Matthews BW. Structure of the DNA binding region of prospero reveals a novel homeo-prospero domain. Structure (London, England : 1993). 10: 1541-9. PMID 12429095 DOI: 10.1016/S0969-2126(02)00883-3 |
0.785 |
|
| 2002 |
Wei BQ, Baase WA, Weaver LH, Matthews BW, Shoichet BK. A model binding site for testing scoring functions in molecular docking. Journal of Molecular Biology. 322: 339-55. PMID 12217695 DOI: 10.1016/S0022-2836(02)00777-5 |
0.688 |
|
| 2002 |
Hausrath AC, Matthews BW. Thermolysin in the absence of substrate has an open conformation. Acta Crystallographica. Section D, Biological Crystallography. 58: 1002-7. PMID 12037302 DOI: 10.1107/S090744490200584X |
0.774 |
|
| 2002 |
Lowther WT, Weissbach H, Etienne F, Brot N, Matthews BW. The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB. Nature Structural Biology. 9: 348-52. PMID 11938352 DOI: 10.1038/Nsb783 |
0.706 |
|
| 2002 |
Sagermann M, Matthews BW. Crystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity. Journal of Molecular Biology. 316: 931-40. PMID 11884133 DOI: 10.1006/Jmbi.2001.5376 |
0.802 |
|
| 2002 |
Sagermann M, Mårtensson LG, Baase WA, Matthews BW. A test of proposed rules for helix capping: implications for protein design. Protein Science : a Publication of the Protein Society. 11: 516-21. PMID 11847274 DOI: 10.1110/Ps.39802 |
0.798 |
|
| 2002 |
Weissbach H, Etienne F, Hoshi T, Heinemann SH, Lowther WT, Matthews B, St John G, Nathan C, Brot N. Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function. Archives of Biochemistry and Biophysics. 397: 172-8. PMID 11795868 DOI: 10.1006/Abbi.2001.2664 |
0.646 |
|
| 2002 |
Quillin ML, Matthews BW. Generation of noble-gas binding sites for crystallographic phasing using site-directed mutagenesis. Acta Crystallographica. Section D, Biological Crystallography. 58: 97-103. PMID 11752783 DOI: 10.1107/S0907444901018145 |
0.417 |
|
| 2001 |
Juers DH, Heightman TD, Vasella A, McCarter JD, Mackenzie L, Withers SG, Matthews BW. A structural view of the action of Escherichia coli (lacZ) beta-galactosidase. Biochemistry. 40: 14781-94. PMID 11732897 DOI: 10.1021/Bi011727I |
0.742 |
|
| 2001 |
Weaver LH, Kwon K, Beckett D, Matthews BW. Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor. Protein Science : a Publication of the Protein Society. 10: 2618-22. PMID 11714930 DOI: 10.1110/Ps.32701 |
0.418 |
|
| 2001 |
Hausrath AC, Capaldi RA, Matthews BW. The conformation of the epsilon- and gamma-subunits within the Escherichia coli F(1) ATPase. The Journal of Biological Chemistry. 276: 47227-32. PMID 11585832 DOI: 10.1074/Jbc.M107536200 |
0.718 |
|
| 2001 |
Juers DH, Matthews BW. Reversible lattice repacking illustrates the temperature dependence of macromolecular interactions. Journal of Molecular Biology. 311: 851-62. PMID 11518535 DOI: 10.1006/Jmbi.2001.4891 |
0.738 |
|
| 2001 |
Breyer WA, Matthews BW. A structural basis for processivity. Protein Science : a Publication of the Protein Society. 10: 1699-711. PMID 11514661 DOI: 10.1110/Ps.10301 |
0.821 |
|
| 2001 |
Sagermann M, Stevens TH, Matthews BW. Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences of the United States of America. 98: 7134-9. PMID 11416198 DOI: 10.1073/Pnas.131192798 |
0.781 |
|
| 2001 |
Weaver LH, Kwon K, Beckett D, Matthews BW. Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator. Proceedings of the National Academy of Sciences of the United States of America. 98: 6045-50. PMID 11353844 DOI: 10.1073/Pnas.111128198 |
0.391 |
|
| 2001 |
Xu J, Baase WA, Quillin ML, Baldwin EP, Matthews BW. Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. Protein Science : a Publication of the Protein Society. 10: 1067-78. PMID 11316887 DOI: 10.1110/Ps.02101 |
0.74 |
|
| 2001 |
Su AI, Lorber DM, Weston GS, Baase WA, Matthews BW, Shoichet BK. Docking molecules by families to increase the diversity of hits in database screens: computational strategy and experimental evaluation. Proteins. 42: 279-93. PMID 11119652 DOI: 10.1002/1097-0134(20010201)42:2<279::Aid-Prot150>3.0.Co;2-U |
0.779 |
|
| 2000 |
Breyer WA, Matthews BW. Structure of Escherichia coli exonuclease I suggests how processivity is achieved. Nature Structural Biology. 7: 1125-8. PMID 11101894 DOI: 10.1038/81978 |
0.793 |
|
| 2000 |
Lowther WT, Brot N, Weissbach H, Matthews BW. Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme. Biochemistry. 39: 13307-12. PMID 11063566 DOI: 10.1021/Bi0020269 |
0.698 |
|
| 2000 |
Juers DH, Jacobson RH, Wigley D, Zhang XJ, Huber RE, Tronrud DE, Matthews BW. High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation. Protein Science : a Publication of the Protein Society. 9: 1685-99. PMID 11045615 DOI: 10.1110/Ps.9.9.1685 |
0.781 |
|
| 2000 |
Quillin ML, Breyer WA, Griswold IJ, Matthews BW. Size versus polarizability in protein-ligand interactions: binding of noble gases within engineered cavities in phage T4 lysozyme. Journal of Molecular Biology. 302: 955-77. PMID 10993735 DOI: 10.1006/Jmbi.2000.4063 |
0.812 |
|
| 2000 |
He MM, Clugston SL, Honek JF, Matthews BW. Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation. Biochemistry. 39: 8719-27. PMID 10913283 DOI: 10.1021/Bi000856G |
0.359 |
|
| 2000 |
Korndörfer IP, Fessner WD, Matthews BW. The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution. Journal of Molecular Biology. 300: 917-33. PMID 10891278 DOI: 10.1006/Jmbi.2000.3896 |
0.467 |
|
| 2000 |
Lowther WT, Brot N, Weissbach H, Honek JF, Matthews BW. Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase. Proceedings of the National Academy of Sciences of the United States of America. 97: 6463-8. PMID 10841552 DOI: 10.1073/Pnas.97.12.6463 |
0.674 |
|
| 2000 |
Wray JW, Baase WA, Ostheimer GJ, Zhang XJ, Matthews BW. Use of a non-rigid region in T4 lysozyme to design an adaptable metal-binding site. Protein Engineering. 13: 313-21. PMID 10835104 DOI: 10.1093/Protein/13.5.313 |
0.802 |
|
| 2000 |
Sagermann M, Matthews BW. Cloning, expression and crystallization of VMA13p, an essential subunit of the vacuolar H+-ATPase of Saccharomyces cerevisiae. Acta Crystallographica. Section D, Biological Crystallography. 56: 475-7. PMID 10739925 DOI: 10.1107/S0907444900000950 |
0.755 |
|
| 2000 |
Lowther WT, Matthews BW. Structure and function of the methionine aminopeptidases. Biochimica Et Biophysica Acta. 1477: 157-67. PMID 10708856 DOI: 10.1016/S0167-4838(99)00271-X |
0.689 |
|
| 2000 |
Rupert PB, Mollah AK, Mossing MC, Matthews BW. The structural basis for enhanced stability and reduced DNA binding seen in engineered second-generation Cro monomers and dimers. Journal of Molecular Biology. 296: 1079-90. PMID 10686105 DOI: 10.1006/Jmbi.1999.3498 |
0.355 |
|
| 2000 |
Korndörfer IP, Salerno J, Jing D, Matthews BW. Crystallization and preliminary X-ray analysis of a bacteriophage T4 primase fragment. Acta Crystallographica. Section D, Biological Crystallography. 56: 95-7. PMID 10666640 DOI: 10.1107/S0907444999014225 |
0.38 |
|
| 2000 |
Liu R, Baase WA, Matthews BW. The introduction of strain and its effects on the structure and stability of T4 lysozyme. Journal of Molecular Biology. 295: 127-45. PMID 10623513 DOI: 10.1006/Jmbi.1999.3300 |
0.449 |
|
| 2000 |
Yang G, Cecconi C, Baase WA, Vetter IR, Breyer WA, Haack JA, Matthews BW, Dahlquist FW, Bustamante C. Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 97: 139-44. PMID 10618384 DOI: 10.1073/Pnas.97.1.139 |
0.796 |
|
| 1999 |
Gassner NC, Matthews BW. Use of differentially substituted selenomethionine proteins in X-ray structure determination. Acta Crystallographica. Section D, Biological Crystallography. 55: 1967-70. PMID 10666571 DOI: 10.1107/S0907444999013347 |
0.391 |
|
| 1999 |
Hausrath AC, Grüber G, Matthews BW, Capaldi RA. Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography. Proceedings of the National Academy of Sciences of the United States of America. 96: 13697-702. PMID 10570135 DOI: 10.1073/Pnas.96.24.13697 |
0.722 |
|
| 1999 |
Gassner NC, Baase WA, Hausrath AC, Matthews BW. Substitution with selenomethionine can enhance the stability of methionine-rich proteins. Journal of Molecular Biology. 294: 17-20. PMID 10556025 DOI: 10.1006/Jmbi.1999.3220 |
0.767 |
|
| 1999 |
Lowther WT, Zhang Y, Sampson PB, Honek JF, Matthews BW. Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues. Biochemistry. 38: 14810-9. PMID 10555963 DOI: 10.1021/Bi991711G |
0.664 |
|
| 1999 |
Gassner NC, Baase WA, Lindstrom JD, Lu J, Dahlquist FW, Matthews BW. Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry. 38: 14451-60. PMID 10545167 DOI: 10.1021/Bi9915519 |
0.432 |
|
| 1999 |
Wray JW, Baase WA, Lindstrom JD, Weaver LH, Poteete AR, Matthews BW. Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. Journal of Molecular Biology. 292: 1111-20. PMID 10512706 DOI: 10.1006/Jmbi.1999.3102 |
0.444 |
|
| 1999 |
Kovall RA, Matthews BW. Type II restriction endonucleases: structural, functional and evolutionary relationships. Current Opinion in Chemical Biology. 3: 578-83. PMID 10508668 DOI: 10.1016/S1367-5931(99)00012-5 |
0.716 |
|
| 1999 |
Kuroki R, Weaver LH, Matthews BW. Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site. Proceedings of the National Academy of Sciences of the United States of America. 96: 8949-54. PMID 10430876 DOI: 10.1073/Pnas.96.16.8949 |
0.404 |
|
| 1999 |
Lowther WT, Orville AM, Madden DT, Lim S, Rich DH, Matthews BW. Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis. Biochemistry. 38: 7678-88. PMID 10387007 DOI: 10.1021/Bi990684R |
0.667 |
|
| 1999 |
Sagermann M, Baase WA, Matthews BW. Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding. Proceedings of the National Academy of Sciences of the United States of America. 96: 6078-83. PMID 10339544 DOI: 10.1073/Pnas.96.11.6078 |
0.81 |
|
| 1999 |
Juers DH, Huber RE, Matthews BW. Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between beta-galactosidase and other glycohydrolases. Protein Science : a Publication of the Protein Society. 8: 122-36. PMID 10210191 DOI: 10.1110/Ps.8.1.122 |
0.732 |
|
| 1998 |
Lowther WT, McMillen DA, Orville AM, Matthews BW. The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase. Proceedings of the National Academy of Sciences of the United States of America. 95: 12153-7. PMID 9770455 DOI: 10.1073/pnas.95.21.12153 |
0.651 |
|
| 1998 |
Albright RA, Mossing MC, Matthews BW. Crystal structure of an engineered Cro monomer bound nonspecifically to DNA: possible implications for nonspecific binding by the wild-type protein. Protein Science : a Publication of the Protein Society. 7: 1485-94. PMID 9684880 DOI: 10.1002/Pro.5560070701 |
0.403 |
|
| 1998 |
Kovall RA, Matthews BW. Structural, functional, and evolutionary relationships between lambda-exonuclease and the type II restriction endonucleases. Proceedings of the National Academy of Sciences of the United States of America. 95: 7893-7. PMID 9653111 DOI: 10.1073/Pnas.95.14.7893 |
0.722 |
|
| 1998 |
Albright RA, Matthews BW. Crystal structure of lambda-Cro bound to a consensus operator at 3.0 A resolution. Journal of Molecular Biology. 280: 137-51. PMID 9653037 DOI: 10.1006/Jmbi.1998.1848 |
0.436 |
|
| 1998 |
Ohlendorf DH, Tronrud DE, Matthews BW. Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity. Journal of Molecular Biology. 280: 129-36. PMID 9653036 DOI: 10.1006/jmbi.1998.1849 |
0.37 |
|
| 1998 |
Rupert PB, Daughdrill GW, Bowerman B, Matthews BW. A new DNA-binding motif in the Skn-1 binding domain-DNA complex. Nature Structural Biology. 5: 484-91. PMID 9628487 DOI: 10.1038/Nsb0698-484 |
0.333 |
|
| 1998 |
Lipscomb LA, Gassner NC, Snow SD, Eldridge AM, Baase WA, Drew DL, Matthews BW. Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme. Protein Science : a Publication of the Protein Society. 7: 765-73. PMID 9541409 DOI: 10.1002/pro.5560070326 |
0.302 |
|
| 1998 |
Albright RA, Matthews BW. How Cro and lambda-repressor distinguish between operators: the structural basis underlying a genetic switch. Proceedings of the National Academy of Sciences of the United States of America. 95: 3431-6. PMID 9520383 DOI: 10.1073/Pnas.95.7.3431 |
0.407 |
|
| 1998 |
Baldwin E, Baase WA, Zhang Xj, Feher V, Matthews BW. Generation of ligand binding sites in T4 lysozyme by deficiency-creating substitutions. Journal of Molecular Biology. 277: 467-85. PMID 9514755 DOI: 10.1006/Jmbi.1997.1606 |
0.743 |
|
| 1998 |
Xu J, Baase WA, Baldwin E, Matthews BW. The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. Protein Science : a Publication of the Protein Society. 7: 158-77. PMID 9514271 DOI: 10.1002/Pro.5560070117 |
0.747 |
|
| 1997 |
Matthews BW. [1] Recent transformations in structural biology. Methods in Enzymology. 276: 3-10. PMID 27799102 DOI: 10.1016/S0076-6879(97)76047-6 |
0.392 |
|
| 1997 |
Kovall R, Matthews BW. Toroidal structure of lambda-exonuclease. Science (New York, N.Y.). 277: 1824-7. PMID 9295273 DOI: 10.1126/Science.277.5333.1824 |
0.718 |
|
| 1997 |
Beckett D, Matthews BW. Escherichia coli repressor of biotin biosynthesis. Methods in Enzymology. 279: 362-76. PMID 9211289 DOI: 10.1016/S0076-6879(97)79041-4 |
0.459 |
|
| 1997 |
Gassner NC, Baase WA, Lindstrom JD, Shoichet BK, Matthews BW. Isolation and characterization of multiple-methionine mutants of T4 lysozyme with simplified cores Techniques in Protein Chemistry. 8: 851-863. DOI: 10.1016/S1080-8914(97)80082-8 |
0.629 |
|
| 1996 |
Weaver L, Stagsted J, Behnke O, Matthews BW, Olsson L. Beta-sheet models for the ordered filamentous structure formed by a peptide that enhances the action of insulin. Journal of Structural Biology. 117: 165-72. PMID 8986646 DOI: 10.1006/Jsbi.1996.0080 |
0.322 |
|
| 1996 |
Vetter IR, Baase WA, Heinz DW, Xiong JP, Snow S, Matthews BW. Protein structural plasticity exemplified by insertion and deletion mutants in T4 lysozyme. Protein Science : a Publication of the Protein Society. 5: 2399-415. PMID 8976549 DOI: 10.1002/Pro.5560051203 |
0.462 |
|
| 1996 |
Morimoto K, Kuroki R, Matthews BW. Control of the catalytic mechanism of an enzyme by amino acid substitution. Annals of the New York Academy of Sciences. 799: 56-60. PMID 8958073 DOI: 10.1111/J.1749-6632.1996.Tb33177.X |
0.304 |
|
| 1996 |
Gassner NC, Baase WA, Matthews BW. A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 93: 12155-8. PMID 8901549 DOI: 10.1073/Pnas.93.22.12155 |
0.446 |
|
| 1996 |
Baldwin E, Xu J, Hajiseyedjavadi O, Baase WA, Matthews BW. Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. Journal of Molecular Biology. 259: 542-59. PMID 8676387 DOI: 10.1006/Jmbi.1996.0338 |
0.73 |
|
| 1996 |
Matthews BW. Structural and genetic analysis of the folding and function of T4 lysozyme. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 10: 35-41. PMID 8566545 DOI: 10.1096/Fasebj.10.1.8566545 |
0.498 |
|
| 1996 |
Albright RA, Mossing MC, Matthews BW. High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer. Biochemistry. 35: 735-42. PMID 8547253 DOI: 10.1021/Bi951958N |
0.469 |
|
| 1996 |
Quillin ML, Baase WA, Matthews BW. Binding of small electron-dense ligands in large protein cavities Acta Crystallographica Section a Foundations of Crystallography. 52: C215-C215. DOI: 10.1107/S0108767396090757 |
0.323 |
|
| 1995 |
Zhang XJ, Baase WA, Shoichet BK, Wilson KP, Matthews BW. Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. Protein Engineering. 8: 1017-22. PMID 8771182 DOI: 10.1093/Protein/8.10.1017 |
0.574 |
|
| 1995 |
Holland DR, Hausrath AC, Juers D, Matthews BW. Structural analysis of zinc substitutions in the active site of thermolysin. Protein Science : a Publication of the Protein Society. 4: 1955-65. PMID 8535232 DOI: 10.1002/Pro.5560041001 |
0.814 |
|
| 1995 |
Blaber M, Baase WA, Gassner N, Matthews BW. Alanine Scanning Mutagenesis of the α-Helix 115-123 of Phage T4 Lysozyme: Effects on Structure, Stability and the Binding of Solvent Journal of Molecular Biology. 246: 317-330. PMID 7869383 DOI: 10.1006/Jmbi.1994.0087 |
0.659 |
|
| 1995 |
Shoichet BK, Baase WA, Kuroki R, Matthews BW. A relationship between protein stability and protein function. Proceedings of the National Academy of Sciences of the United States of America. 92: 452-6. PMID 7831309 DOI: 10.1073/Pnas.92.2.452 |
0.628 |
|
| 1995 |
Weaver LH, Grütter MG, Matthews BW. The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "Goose-type" ly'sozymes lack a catalytic aspartate residue Journal of Molecular Biology. 245: 54-68. PMID 7823320 DOI: 10.1016/S0022-2836(95)80038-7 |
0.47 |
|
| 1995 |
Matthews BW. Studies on protein stability with T4 lysozyme Advances in Protein Chemistry. 46: 249-278. PMID 7771320 DOI: 10.1016/S0065-3233(08)60337-X |
0.455 |
|
| 1995 |
Matthews BW. Can proteins be turned inside-out? Nature Structural Biology. 2: 85-86. PMID 7749923 DOI: 10.1038/Nsb0295-85 |
0.337 |
|
| 1995 |
Arfin SM, Kendall RL, Hall L, Weaver LH, Stewart AE, Matthews BW, Bradshaw RA. Eukaryotic methionyl aminopeptidases: Two classes of cobalt-dependent enzymes Proceedings of the National Academy of Sciences of the United States of America. 92: 7714-7718. PMID 7644482 DOI: 10.1073/Pnas.92.17.7714 |
0.575 |
|
| 1995 |
Zhang XJ, Wozniak JA, Matthews BW. Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme. Journal of Molecular Biology. 250: 527-52. PMID 7616572 DOI: 10.1006/Jmbi.1995.0396 |
0.487 |
|
| 1995 |
Morton A, Matthews BW. Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: linkage of dynamics and structural plasticity. Biochemistry. 34: 8576-88. PMID 7612599 DOI: 10.1021/Bi00027A007 |
0.395 |
|
| 1995 |
Morton A, Baase WA, Matthews BW. Energetic origins of specificity of ligand binding in an interior nonpolar cavity of T4 lysozyme. Biochemistry. 34: 8564-75. PMID 7612598 DOI: 10.1021/Bi00027A006 |
0.371 |
|
| 1995 |
Kuroki R, Weaver LH, Matthews BW. Structure-based design of a lysozyme with altered catalytic activity. Nature Structural Biology. 2: 1007-11. PMID 7583653 DOI: 10.1038/Nsb1195-1007 |
0.39 |
|
| 1994 |
Blaber M, Zhang XJ, Lindstrom JD, Pepiot SD, Baase WA, Matthews BW. Determination of α-helix propensity within the context of a folded protein: Sites 44 and 131 in bacteriophage T4 lysozyme Journal of Molecular Biology. 235: 600-624. PMID 8289284 DOI: 10.1006/Jmbi.1994.1016 |
0.671 |
|
| 1994 |
Holland DR, Cousens LS, Meng W, Matthews BW. Nerve growth factor in different crystal forms displays structural flexibility and reveals zinc binding sites Journal of Molecular Biology. 239: 385-400. PMID 8201620 DOI: 10.1006/Jmbi.1994.1380 |
0.457 |
|
| 1994 |
Heinz DW, Matthews BW. Rapid crystallization of T4 lysozyme by intermolecular disulphide cross-linking Protein Engineering. 7: 301-307. PMID 8177878 DOI: 10.1093/Protein/7.3.301 |
0.382 |
|
| 1994 |
Bazan JF, Weaver LH, Roderick SL, Huber R, Matthews BW. Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold Proceedings of the National Academy of Sciences of the United States of America. 91: 2473-2477. PMID 8146141 DOI: 10.1073/Pnas.91.7.2473 |
0.562 |
|
| 1994 |
Heinz DW, Baase WA, Zhang XJ, Blaber M, Dahlquist FW, Matthews BW. Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis. Journal of Molecular Biology. 236: 869-86. PMID 8114100 DOI: 10.1006/Jmbi.1994.1195 |
0.676 |
|
| 1994 |
Hausrath AC, Matthews BW. Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A. The Journal of Biological Chemistry. 269: 18839-42. PMID 8034637 DOI: 10.2210/Pdb1Hyt/Pdb |
0.731 |
|
| 1994 |
Jacobson RH, Zhang XJ, DuBose RF, Matthews BW. Three-dimensional structure of β-galactosidase from E. coli Nature. 369: 761-766. PMID 8008071 DOI: 10.1038/369761A0 |
0.472 |
|
| 1994 |
Zhang NJ, Matthews BW. Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme Protein Science. 3: 1031-1039. PMID 7920248 DOI: 10.1002/Pro.5560030705 |
0.388 |
|
| 1994 |
Baldwin EP, Matthews BW. Core-packing constraints, hydrophobicity and protein design. Current Opinion in Biotechnology. 5: 396-402. PMID 7765172 DOI: 10.1016/0958-1669(94)90048-5 |
0.729 |
|
| 1993 |
Blaber M, Zhang XJ, Matthews BW. Structural basis of amino acid α helix propensity Science. 260: 1637-1640. PMID 8503008 DOI: 10.1126/Science.8503008 |
0.631 |
|
| 1993 |
Pjura P, McIntosh LP, Wozniak JA, Matthews BW. Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties Proteins: Structure, Function and Genetics. 15: 401-412. PMID 8460110 DOI: 10.1002/Prot.340150407 |
0.446 |
|
| 1993 |
Eriksson AE, Baase WA, Matthews BW. Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences Journal of Molecular Biology. 229: 747-769. PMID 8433369 DOI: 10.1006/Jmbi.1993.1077 |
0.45 |
|
| 1993 |
Heinz DW, Baase WA, Dahlquist FW, Matthews BW. How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme. Nature. 361: 561-4. PMID 8429913 DOI: 10.1038/361561A0 |
0.441 |
|
| 1993 |
Anderson DE, Hurley JH, Nicholson H, Baase WA, Matthews BW. Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117 → Phe Protein Science. 2: 1285-1290. PMID 8401213 DOI: 10.1002/Pro.5560020811 |
0.63 |
|
| 1993 |
Stagsted J, Mapelli C, Meyers C, Matthews BW, Anfinsen CB, Goldstein A, Olsson L. Amino acid residues essential for biological activity of a peptide derived from a major histocompatibility complex class I antigen. Proceedings of the National Academy of Sciences of the United States of America. 90: 7686-90. PMID 8356070 DOI: 10.1073/Pnas.90.16.7686 |
0.301 |
|
| 1993 |
Matthews BW. Structural and genetic analysis of protein stability Annual Review of Biochemistry. 62: 139-160. PMID 8352587 DOI: 10.1146/Annurev.Bi.62.070193.001035 |
0.43 |
|
| 1993 |
Kuroki R, Weaver LH, Matthews BW. A covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme Science. 262: 2030-2033. PMID 8266098 DOI: 10.1126/Science.8266098 |
0.391 |
|
| 1993 |
Baldwin EP, Hajiseyedjavadi O, Baase WA, Matthews BW. The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. Science (New York, N.Y.). 262: 1715-8. PMID 8259514 DOI: 10.1126/Science.8259514 |
0.75 |
|
| 1993 |
Shortle D, Clarke N, Blaber M, Zhang XJ, Matthews BW. Alpha helix propensity of amino acids Science. 262: 917-918. PMID 8235616 DOI: 10.1126/Science.8235616 |
0.513 |
|
| 1993 |
Blaber M, Lindstrom JD, Gassner N, Xu J, Heinz DW, Matthews BW. Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala → Ser and Val → Thr substitutions in T4 lysozyme Biochemistry. 32: 11363-11373. PMID 8218201 DOI: 10.1021/Bi00093A013 |
0.65 |
|
| 1993 |
Eriksson AE, Cousens LS, Matthews BW. Refinement of the structure of human basic fibroblast growth factor at 1.6 Å resolution and analysis of presumed heparin binding sites by selenate substitution Protein Science. 2: 1274-1284. PMID 7691311 DOI: 10.1002/Pro.5560020810 |
0.411 |
|
| 1993 |
Pjura P, Matsumura M, Baase WA, Matthews BW. Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability Protein Science. 2: 2217-2225. PMID 7507755 DOI: 10.1002/Pro.5560021221 |
0.302 |
|
| 1993 |
Nicholson H, Tronrud DE, Becktel WJ, Matthews BW. Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. Biopolymers. 32: 1431-41. PMID 1457724 DOI: 10.1002/Bip.360321103 |
0.426 |
|
| 1993 |
Wilson KP, Malcolm BA, Matthews BW. Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme. Journal of Biological Chemistry. 267: 10842-10849. DOI: 10.2210/Pdb1Hel/Pdb |
0.489 |
|
| 1993 |
Matthews BW. Structural and Genetic Analysis of Protein Folding Protein Engineering Design & Selection. 6: 6-6. DOI: 10.1093/Protein/6.Supplement.6-B |
0.369 |
|
| 1993 |
Matthews BW. Structural and genetic analysis of protein folding and stability. Current Opinion in Sturctural Biology 1993, 3:589-593 Current Opinion in Structural Biology. 3: 589-593. DOI: 10.1016/0959-440X(93)90088-3 |
0.428 |
|
| 1993 |
Pjura P, Matthews BW. Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent Protein Science. 2: 226-232. DOI: 10.1002/Pro.5560021222 |
0.476 |
|
| 1992 |
Matsumura M, Matthews BW. Stabilization of functional proteins by introduction of multiple disulfide bonds. Methods in Enzymology. 202: 336-56. PMID 1784181 DOI: 10.1016/0076-6879(91)02018-5 |
0.396 |
|
| 1992 |
Eriksson AE, Baase WA, Wozniak JA, Matthews BW. A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene. Nature. 355: 371-3. PMID 1731252 DOI: 10.1038/355371A0 |
0.466 |
|
| 1992 |
Heinz DW, Baase WA, Matthews BW. Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. Proceedings of the National Academy of Sciences of the United States of America. 89: 3751-5. PMID 1570293 DOI: 10.1073/Pnas.89.9.3751 |
0.467 |
|
| 1992 |
Hurley JH, Baase WA, Matthews BW. Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. Journal of Molecular Biology. 224: 1143-59. PMID 1569571 DOI: 10.1016/0022-2836(92)90475-Y |
0.609 |
|
| 1992 |
Bell JA, Becktel WJ, Sauer U, Baase WA, Matthews BW. Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59 Biochemistry®. 31: 3590-3596. PMID 1567817 DOI: 10.1021/bi00129a006 |
0.466 |
|
| 1992 |
Eriksson AE, Baase WA, Zhang XJ, Heinz DW, Blaber M, Baldwin EP, Matthews BW. Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science (New York, N.Y.). 255: 178-83. PMID 1553543 DOI: 10.1126/Science.1553543 |
0.782 |
|
| 1992 |
Jacobson RH, Matthews BW. Crystallization of beta-galactosidase from Escherichia coli. Journal of Molecular Biology. 223: 1177-82. PMID 1538395 DOI: 10.1016/0022-2836(92)90269-P |
0.326 |
|
| 1992 |
Hurley JH, Mason DA, Matthews BW. Flexible-geometry conformational energy maps for the amino acid residue preceding a proline. Biopolymers. 32: 1443-6. PMID 1457725 DOI: 10.1002/Bip.360321104 |
0.573 |
|
| 1992 |
Holland DR, Tronrud DE, Pley HW, Flaherty KM, Stark W, Jansonius JN, McKay DB, Matthews BW. Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis. Biochemistry. 31: 11310-6. PMID 1445869 DOI: 10.1021/Bi00161A008 |
0.43 |
|
| 1992 |
Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proceedings of the National Academy of Sciences of the United States of America. 89: 9257-61. PMID 1409631 DOI: 10.1073/Pnas.89.19.9257 |
0.658 |
|
| 1992 |
Dixon MM, Nicholson H, Shewchuk L, Baase WA, Matthews BW. Structure of a hinge-bending bacteriophage T4 lysozyme mutant, Ile3-->Pro. Journal of Molecular Biology. 227: 917-33. PMID 1404394 DOI: 10.1016/0022-2836(92)90231-8 |
0.47 |
|
| 1992 |
Zhang XJ, Baase WA, Matthews BW. Multiple alanine replacements within α-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability Protein Science. 1: 761-776. PMID 1304917 DOI: 10.1002/Pro.5560010608 |
0.488 |
|
| 1992 |
Jacobson RH, Matsumura M, Faber HR, Matthews BW. Structure of a stabilizing disulfide bridge mutant that closes the active- site cleft of T4 lysozyme Protein Science. 1: 46-57. PMID 1304882 DOI: 10.1002/Pro.5560010106 |
0.462 |
|
| 1992 |
Baase WA, Eriksson AE, Zhang XJ, Heinz DW, Sauer U, Blaber M, Baldwin EP, Wozniak JA, Matthews BW. Dissection of protein structure and folding by directed mutagenesis. Faraday Discussions. 173-81. PMID 1290931 DOI: 10.1039/Fd9929300173 |
0.815 |
|
| 1991 |
Bell JA, Wilson KP, Zhang XJ, Faber HR, Nicholson H, Matthews BW. Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths. Proteins. 10: 10-21. PMID 2062826 DOI: 10.1002/Prot.340100103 |
0.379 |
|
| 1991 |
Poteete AR, Sun DP, Nicholson H, Matthews BW. Second-site revertants of an inactive T4 lysozyme mutant restore activity by restructuring the active site cleft. Biochemistry. 30: 1425-32. PMID 1991123 DOI: 10.1021/Bi00219A037 |
0.44 |
|
| 1991 |
Dao-pin S, Söderlind E, Baase WA, Wozniak JA, Sauer U, Matthews BW. Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. Journal of Molecular Biology. 221: 873-87. PMID 1942034 DOI: 10.1016/0022-2836(91)80181-S |
0.416 |
|
| 1991 |
Daopin S, Alber T, Baase WA, Wozniak JA, Matthews BW. Structural and thermodynamic analysis of the packing of two α-helices in bacteriophage T4 lysozyme Journal of Molecular Biology. 221: 647-667. PMID 1920439 DOI: 10.1016/0022-2836(91)80079-A |
0.67 |
|
| 1991 |
Nicholson H, Anderson DE, Dao-pin S, Matthews BW. Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. Biochemistry. 30: 9816-28. PMID 1911773 DOI: 10.1021/Bi00105A002 |
0.395 |
|
| 1991 |
Dixon MM, Brennan RG, Matthews BW. Structure of γ-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that γ-chymotrypsin is a covalent acyl-enzyme adduct at low pH International Journal of Biological Macromolecules. 13: 89-96. PMID 1888717 DOI: 10.1016/0141-8130(91)90054-X |
0.546 |
|
| 1991 |
Sun DP, Sauer U, Nicholson H, Matthews BW. Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry. 30: 7142-53. PMID 1854726 DOI: 10.1021/Bi00243A015 |
0.449 |
|
| 1991 |
Dao-pin S, Anderson DE, Baase WA, Dahlquist FW, Matthews BW. Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. Biochemistry. 30: 11521-9. PMID 1747370 DOI: 10.1021/Bi00113A006 |
0.433 |
|
| 1991 |
Eriksson AE, Cousens LS, Weaver LH, Matthews BW. Three-dimensional structure of human basic fibroblast growth factor. Proceedings of the National Academy of Sciences of the United States of America. 88: 3441-5. PMID 1707542 DOI: 10.1073/Pnas.88.8.3441 |
0.463 |
|
| 1991 |
Matthews BW. Mutational analysis of protein stability Current Opinion in Structural Biology. 1: 17-21. DOI: 10.1016/0959-440X(91)90005-E |
0.393 |
|
| 1990 |
Ohlendorf DH, Anderson WF, Takeda Y, Matthews BW. High resolution structural studies of Cro repressor protein and implications for DNA recognition. Journal of Biomolecular Structure & Dynamics. 1: 553-63. PMID 6400887 DOI: 10.1080/07391102.1983.10507461 |
0.426 |
|
| 1990 |
Dixon MM, Matthews BW. Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin? Biochemistry. 28: 7033-8. PMID 2819046 DOI: 10.1021/Bi00443A038 |
0.36 |
|
| 1990 |
Nicholson H, Söderlind E, Tronrud DE, Matthews BW. Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. Journal of Molecular Biology. 210: 181-93. PMID 2511328 DOI: 10.1016/0022-2836(89)90299-4 |
0.442 |
|
| 1990 |
Pjura PE, Matsumura M, Wozniak JA, Matthews BW. Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein. Biochemistry. 29: 2592-8. PMID 2334683 DOI: 10.1021/Bi00462A023 |
0.464 |
|
| 1990 |
Malcolm BA, Wilson KP, Matthews BW, Kirsch JF, Wilson AC. Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing. Nature. 345: 86-9. PMID 2330057 DOI: 10.1038/345086A0 |
0.412 |
|
| 1990 |
Dao-Pin S, Baase WA, Matthews BW. A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. Proteins. 7: 198-204. PMID 2326253 DOI: 10.1002/Prot.340070208 |
0.439 |
|
| 1990 |
Faber HR, Matthews BW. A mutant T4 lysozyme displays five different crystal conformations. Nature. 348: 263-6. PMID 2234094 DOI: 10.1038/348263A0 |
0.484 |
|
| 1990 |
Brennan RG, Roderick SL, Takeda Y, Matthews BW. Protein-DNA conformational changes in the crystal structure of a λ Cro-operator complex Proceedings of the National Academy of Sciences of the United States of America. 87: 8165-8169. PMID 2146682 DOI: 10.1073/Pnas.87.20.8165 |
0.622 |
|
| 1990 |
Matsumura M, Wozniak JA, Sun DP, Matthews BW. Structural studies of mutants of T4 lysozyme that alter hydrophobic stabilization. Journal of Biological Chemistry. 264: 16059-16066. DOI: 10.2210/Pdb3Lzm/Pdb |
0.487 |
|
| 1990 |
Wozniak JA, Faber HR, Dao-pin S, Zhang XJ, Matthews BW. Crystallization of designed protein variants Methods. 1: 100-104. DOI: 10.1016/S1046-2023(05)80152-5 |
0.386 |
|
| 1989 |
Nicholson H, Becktel WJ, Matthews BW. Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles. Nature. 336: 651-6. PMID 3200317 DOI: 10.1038/336651A0 |
0.387 |
|
| 1989 |
Matsumura M, Matthews BW. Control of enzyme activity by an engineered disulfide bond. Science (New York, N.Y.). 243: 792-4. PMID 2916125 DOI: 10.1126/Science.2916125 |
0.318 |
|
| 1989 |
Matsumura M, Signor G, Matthews BW. Substantial increase of protein stability by multiple disulphide bonds. Nature. 342: 291-3. PMID 2812028 DOI: 10.1038/342291A0 |
0.402 |
|
| 1989 |
Karpusas M, Baase WA, Matsumura M, Matthews BW. Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. Proceedings of the National Academy of Sciences of the United States of America. 86: 8237-41. PMID 2682639 DOI: 10.1073/Pnas.86.21.8237 |
0.475 |
|
| 1989 |
Brennan RG, Matthews BW. Structural basis of DNA-protein recognition Trends in Biochemical Sciences. 14: 286-290. PMID 2672451 DOI: 10.1016/0968-0004(89)90066-2 |
0.573 |
|
| 1989 |
Matsumura M, Becktel WJ, Levitt M, Matthews BW. Stabilization of phage T4 lysozyme by engineered disulfide bonds. Proceedings of the National Academy of Sciences of the United States of America. 86: 6562-6. PMID 2671995 DOI: 10.1073/Pnas.86.17.6562 |
0.411 |
|
| 1989 |
Weaver LH, Gray TM, Grütter MG, Anderson DE, Wozniak JA, Dahlquist FW, Matthews BW. High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96----His. Biochemistry. 28: 3793-7. PMID 2665808 DOI: 10.1021/Bi00435A025 |
0.439 |
|
| 1988 |
Gray TM, Matthews BW. Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid. The Journal of Biological Chemistry. 262: 16858-64. PMID 3680274 DOI: 10.2210/Pdb1L16/Pdb |
0.417 |
|
| 1988 |
Matthews BW. Genetic and structural analysis of the protein stability problem. Biochemistry. 26: 6885-8. PMID 3427049 DOI: 10.1021/Bi00396A001 |
0.334 |
|
| 1988 |
Matsumura M, Becktel WJ, Matthews BW. Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature. 334: 406-10. PMID 3405287 DOI: 10.1038/334406A0 |
0.398 |
|
| 1988 |
Holden HM, Matthews BW. The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis Journal of Biological Chemistry. 263: 3256-3260. PMID 3343246 DOI: 10.2210/Pdb3Tmn/Pdb |
0.319 |
|
| 1988 |
Alber T, Bell JA, Dao-Pin S, Nicholson H, Wozniak JA, Cook S, Matthews BW. Replacements of Pro86 in phage T4 lysozyme extend an α-helix but do not alter protein stability Science. 239: 631-635. PMID 3277275 DOI: 10.1126/Science.3277275 |
0.675 |
|
| 1988 |
Remington SJ, Woodbury RG, Reynolds RA, Matthews BW, Neurath H. The structure of rat mast cell protease II at 1.9-A resolution. Biochemistry. 27: 8097-105. PMID 3233198 DOI: 10.1021/Bi00421A019 |
0.649 |
|
| 1988 |
Matthews BW. Structural basis of the action of thermolysin and related zinc peptidases Accounts of Chemical Research. 21: 333-340. DOI: 10.1021/Ar00153A003 |
0.325 |
|
| 1988 |
Brennan RG, Wozniak J, Faber R, Matthews BW. Crystallization of mutant lysozymes from bacteriophage T4 Journal of Crystal Growth. 90: 160-167. DOI: 10.1016/0022-0248(88)90311-9 |
0.629 |
|
| 1987 |
Tronrud DE, Holden HM, Matthews BW. Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond Science. 235: 571-574. PMID 3810156 DOI: 10.1126/Science.3810156 |
0.35 |
|
| 1987 |
Grütter MG, Gray TM, Weaver LH, Alber T, Wilson K, Matthews BW. Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157 → Ile Journal of Molecular Biology. 197: 315-329. PMID 3681997 DOI: 10.1016/0022-2836(87)90126-4 |
0.432 |
|
| 1987 |
Alber T, Sun DP, Nye JA, Muchmore DC, Matthews BW. Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein. Biochemistry. 26: 3754-8. PMID 3651410 DOI: 10.1021/Bi00387A002 |
0.659 |
|
| 1987 |
Weaver LH, Matthews BW. Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution. Journal of Molecular Biology. 193: 189-99. PMID 3586019 DOI: 10.1016/0022-2836(87)90636-X |
0.385 |
|
| 1987 |
Dao-Pin S, Alber T, Bell JA, Weaver LH, Matthews BW. Use of site-directed mutagenesis to obtain isomorphous heavy-atom derivatives for protein crystallography: Cysteine-containing mutants of phage t4 lysozyme Protein Engineering, Design and Selection. 1: 115-123. PMID 3507694 DOI: 10.1093/Protein/1.2.115 |
0.621 |
|
| 1987 |
Matthews BW, Nicholson H, Becktel WJ. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proceedings of the National Academy of Sciences of the United States of America. 84: 6663-7. PMID 3477797 DOI: 10.1073/Pnas.84.19.6663 |
0.486 |
|
| 1987 |
Holden HM, Tronrud DE, Monzingo AF, Weaver LH, Matthews BW. Slow- and fast-binding inhibitors of thermolysin display different modes of binding: Crystallographic analysis of extended phosphonamidate transition-state analogues Biochemistry. 26: 8542-8553. PMID 3442675 DOI: 10.1021/Bi00400A008 |
0.381 |
|
| 1987 |
Alber T, Matthews BW. [27] Structure and thermal stability of phage T4 lysozyme Methods in Enzymology. 154: 511-533. PMID 3323816 DOI: 10.1016/0076-6879(87)54093-9 |
0.649 |
|
| 1987 |
Alber T, Sun DP, Wilson K, Wozniak JA, Cook SP, Matthews BW. Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature. 330: 41-6. PMID 3118211 DOI: 10.1038/330041A0 |
0.644 |
|
| 1987 |
Tronrud DE, Ten Eyck LF, Matthews BW. An efficient general-purpose least-squares refinement program for macromolecular structures Acta Crystallographica Section a Foundations of Crystallography. 43: 489-501. DOI: 10.1107/S0108767387099124 |
0.35 |
|
| 1987 |
Alber T, Bell J, Cook S, Nye JA, Daopin S, Wilson K, Wozniak J, Matthews BW. Correlations between structure and thermodynamic stability of phage T4 lysozyme Acta Crystallographica Section a Foundations of Crystallography. 43: C15-C15. DOI: 10.1107/S0108767387085131 |
0.605 |
|
| 1987 |
Holden HM, Tronrud DE, Monzingo AF, Weaver LH, Matthews BW. Structural basis of the action of thermolysin and the zinc proteases Acta Crystallographica Section a Foundations of Crystallography. 43: C17-C17. DOI: 10.1107/S010876738708509X |
0.348 |
|
| 1987 |
Matthews BW. Crystallography in the life sciences Acta Crystallographica Section a Foundations of Crystallography. 43: C1-C1. DOI: 10.1080/08893119008032953 |
0.367 |
|
| 1986 |
Ohlendorf DH, Anderson WF, Matthews BW. Many gene-regulatory proteins appear to have a similar alpha-helical fold that binds DNA and evolved from a common precursor. Journal of Molecular Evolution. 19: 109-14. PMID 6571216 DOI: 10.1007/Bf02300748 |
0.384 |
|
| 1986 |
Matthews BW, Rossmann MG. Comparison of protein structures. Methods in Enzymology. 115: 397-420. PMID 4079794 DOI: 10.1016/0076-6879(85)15029-9 |
0.558 |
|
| 1986 |
Tronrud DE, Schmid MF, Matthews BW. Structure and X-ray amino acid sequence of a bacteriochlorophyll A protein from Prosthecochloris aestuarii refined at 1.9 A resolution. Journal of Molecular Biology. 188: 443-54. PMID 3735428 DOI: 10.1016/0022-2836(86)90167-1 |
0.42 |
|
| 1986 |
Tronrud DE, Monzingo AF, Matthews BW. Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin. European Journal of Biochemistry. 157: 261-8. PMID 3709536 DOI: 10.1111/J.1432-1033.1986.Tb09664.X |
0.346 |
|
| 1986 |
Brennan RG, Takeda Y, Kim J, Anderson WF, Matthews BW. Crystallization of a complex of cro repressor with a 17 base-pair operator Journal of Molecular Biology. 188: 115-118. PMID 2940371 DOI: 10.1016/0022-2836(86)90488-2 |
0.515 |
|
| 1986 |
Brennan RG, Kim J, Takeda Y, Anderson WF, Matthews BW. Studies on the crystallization of the cro protein-pseudo OR3 complex Journal of Crystal Growth. 76: 715-718. DOI: 10.1016/0022-0248(86)90189-2 |
0.56 |
|
| 1985 |
Monzingo AF, Matthews BW. Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases. Biochemistry. 23: 5724-9. PMID 6395881 DOI: 10.1021/Bi00319A010 |
0.36 |
|
| 1985 |
Weaver LH, Rennell D, Poteete AR, Matthews BW. Structure of phage P22 gene 19 lysozyme inferred from its homology with phage T4 lysozyme. Implications for lysozyme evolution. Journal of Molecular Biology. 184: 739-741. PMID 4046032 DOI: 10.1016/0022-2836(85)90318-3 |
0.372 |
|
| 1985 |
Swanson R, Weaver LH, Remington SJ, Matthews BW, Baldwin TO. Crystals of luciferase from Vibrio harveyi. A preliminary characterization. The Journal of Biological Chemistry. 260: 1287-9. PMID 3968061 |
0.54 |
|
| 1985 |
Reynolds RA, Remington SJ, Weaver LH, Fisher RG, Anderson WF, Ammon HL, Matthews BW. Structure of a serine protease from rat mast cells determined from twinned crystals by isomorphous and molecular replacement Acta Crystallographica Section B Structural Science. 41: 139-147. DOI: 10.1107/S010876818500177X |
0.604 |
|
| 1984 |
Weaver LH, Grütter MG, Remington SJ, Gray TM, Isaacs NW, Matthews BW. Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution. Journal of Molecular Evolution. 21: 97-111. PMID 6442995 DOI: 10.1007/Bf02100084 |
0.678 |
|
| 1984 |
Gray TM, Matthews BW. Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins. Journal of Molecular Biology. 175: 75-81. PMID 6427470 DOI: 10.1016/0022-2836(84)90446-7 |
0.346 |
|
| 1983 |
Holmes MA, Matthews BW. Structure of thermolysin refined at 1.6 A resolution. Journal of Molecular Biology. 160: 623-39. PMID 7175940 DOI: 10.1016/0022-2836(82)90319-9 |
0.43 |
|
| 1983 |
Anderson WF, Cygler M, Vandonselaar M, Ohlendorf DH, Matthews BW, Kim J, Takeda Y. Crystallographic data for complexes of the Cro repressor with DNA. Journal of Molecular Biology. 168: 903-6. PMID 6887256 DOI: 10.1016/S0022-2836(83)80082-5 |
0.333 |
|
| 1983 |
Grütter MG, Weaver LH, Matthews BW. Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes? Nature. 303: 828-831. PMID 6866082 DOI: 10.1038/303828A0 |
0.426 |
|
| 1983 |
Holmes MA, Tronrud DE, Matthews BW. Structural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitor. Biochemistry. 22: 236-40. PMID 6830761 DOI: 10.1021/Bi00270A034 |
0.418 |
|
| 1983 |
Ohlendorf DH, Anderson WF, Lewis M, Pabo CO, Matthews BW. Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda. Journal of Molecular Biology. 169: 757-69. PMID 6226802 DOI: 10.1016/S0022-2836(83)80169-7 |
0.412 |
|
| 1983 |
Matthews B, Ohlendorf D, Anderson W, Fisher R, Takeda Y. How does cro repressor recognize its DNA target sites? Trends in Biochemical Sciences. 8: 25-29. DOI: 10.1016/0968-0004(83)90065-8 |
0.368 |
|
| 1982 |
Grütter MG, Matthews BW. Amino acid substitutions far from the active site of bacteriophage T4 lysozyme reduce catalytic activity and suggest that the C-terminal lobe of the enzyme participates in substrate binding. Journal of Molecular Biology. 154: 525-35. PMID 7077670 DOI: 10.1016/S0022-2836(82)80011-9 |
0.483 |
|
| 1982 |
Monzingo AF, Matthews BW. Structure of a mercaptan-thermolysin complex illustrates mode of inhibition of zinc proteases by substrate-analogue mercaptans. Biochemistry. 21: 3390-4. PMID 7052122 DOI: 10.1021/Bi00257A022 |
0.36 |
|
| 1982 |
Matthews BW, Ohlendorf DH, Anderson WF, Takeda Y. Structure of the DNA-binding region of lac repressor inferred from its homology with cro repressor. Proceedings of the National Academy of Sciences of the United States of America. 79: 1428-32. PMID 6951187 DOI: 10.1073/Pnas.79.5.1428 |
0.411 |
|
| 1982 |
Ohlendorf DH, Anderson WF, Fisher RG, Takeda Y, Matthews BW. The molecular basis of DNA-protein recognition inferred from the structure of cro repressor. Nature. 298: 718-23. PMID 6213863 DOI: 10.1038/298718A0 |
0.402 |
|
| 1982 |
Steitz TA, Ohlendorf DH, McKay DB, Anderson WF, Matthews BW. Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteins. Proceedings of the National Academy of Sciences of the United States of America. 79: 3097-100. PMID 6212926 DOI: 10.1073/Pnas.79.10.3097 |
0.606 |
|
| 1981 |
Matthews BW, Remington SJ, Grütter MG, Anderson WF. Relation between hen egg white lysozyme and bacteriophage T4 lysozyme: evolutionary implications. Journal of Molecular Biology. 147: 545-58. PMID 7277500 DOI: 10.1016/0022-2836(81)90399-5 |
0.673 |
|
| 1981 |
Anderson WF, Grütter MG, Remington SJ, Weaver LH, Matthews BW. Crystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme: implications for the mechanism of catalysis. Journal of Molecular Biology. 147: 523-43. PMID 7277499 DOI: 10.1016/0022-2836(81)90398-3 |
0.663 |
|
| 1981 |
Matthews BW, Grütter MG, Anderson WF, Remington SJ. Common precursor of lysozymes of hen egg-white and bacteriophage T4. Nature. 290: 334-5. PMID 7207627 DOI: 10.1038/290334A0 |
0.649 |
|
| 1981 |
Anderson WF, Ohlendorf DH, Takeda Y, Matthews BW. Structure of the cro repressor from bacteriophage lambda and its interaction with DNA. Nature. 290: 754-8. PMID 6452580 DOI: 10.1038/290754A0 |
0.397 |
|
| 1981 |
Matthews BW, Anderson WF, Ohlendorf DH, Takeda Y. Structural studies of the Cro repressor protein from bacteriophage λ Acta Crystallographica Section a Foundations of Crystallography. 37: C21-C21. DOI: 10.1107/S0108767381098954 |
0.305 |
|
| 1981 |
Anderson WF, Ohlendorf DH, Takeda Y, Matthews BW. Structure of the bacteriophage lambda Cro repressor: model for protein–DNA interactions Acta Crystallographica Section a Foundations of Crystallography. 37: C46-C46. DOI: 10.1107/S010876738109819X |
0.324 |
|
| 1980 |
Remington SJ, Matthews BW. A systematic approach to the comparison of protein structures. Journal of Molecular Biology. 140: 77-99. PMID 6774102 DOI: 10.1016/0022-2836(80)90357-5 |
0.66 |
|
| 1980 |
Matthews BW, Fenna RE. Structure of a green bacteriochlorophyll protein Accounts of Chemical Research. 13: 309-317. DOI: 10.1021/Ar50153A003 |
0.402 |
|
| 1979 |
Matthews BW, Fenna RE, Bolognesi MC, Schmid MF, Olson JM. Structure of a bacteriochlorophyll a-protein from the green photosynthetic bacterium Prosthecochloris aestuarii. Journal of Molecular Biology. 131: 259-85. PMID 490647 DOI: 10.1016/0022-2836(79)90076-7 |
0.424 |
|
| 1979 |
Anderson WF, Takeda Y, Echols H, Matthews BW. The structure of a repressor: crystallographic data for the Cro regulatory protein of bacteriophage lambda. Journal of Molecular Biology. 130: 507-10. PMID 480362 DOI: 10.1016/0022-2836(79)90437-6 |
0.373 |
|
| 1979 |
Grütter MG, Hawkes RB, Matthews BW. Molecular basis of thermostability in the lysozyme from bacteriophage T4. Nature. 277: 667-669. PMID 423967 DOI: 10.1038/277667A0 |
0.46 |
|
| 1978 |
Woodbury RG, Katunuma N, Kobayashi K, Titani K, Neurath H, Anderson WF, Matthews BW. Covalent structure of a group-specific protease from rat small intestine. Appendix: crystallographic data for a group specific protease from rat intestine. Biochemistry. 17: 811-9. PMID 629933 DOI: 10.1021/Bi00598A010 |
0.417 |
|
| 1978 |
Remington SJ, Anderson WF, Owen J, Ten Eyck LF, Grainger CT, Matthews BW. Structure of the lysozyme from bacteriophage T4: an electron density map at 2.4 A resolution. Journal of Molecular Biology. 118: 81-98. PMID 625058 DOI: 10.1016/0022-2836(78)90245-0 |
0.641 |
|
| 1978 |
Remington SJ, Matthews BW. A general method to assess similarity of protein structures, with applications to T4 bacteriophage lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 75: 2180-4. PMID 276859 DOI: 10.1073/Pnas.75.5.2180 |
0.66 |
|
| 1977 |
Weaver LH, Kester WR, Matthews BW. A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substances. Journal of Molecular Biology. 114: 119-32. PMID 909082 DOI: 10.1016/0022-2836(77)90286-8 |
0.369 |
|
| 1977 |
Holmes MA, Remington SJ, Schwendimann B, Christie GE, Matthews BW. Crystallographic data for sturgeon holo-D-glyceraldehyde-3-phosphate dehydrogenase: a holo-D-glyceraldehyde-3-phosphate dehydrogenase with crystallographic 2-fold symmetry. Journal of Molecular Biology. 112: 651-2. PMID 875036 DOI: 10.1016/S0022-2836(77)80169-1 |
0.583 |
|
| 1977 |
Matthews BW, Fenna RE, Remington SJ. An evaluation of electron micrographs of bacteriochlorophyll a-protein crystals in terms of the structure determined by x-ray crystallography. Journal of Ultrastructure Research. 58: 316-30. PMID 850296 DOI: 10.1016/S0022-5320(77)90022-3 |
0.637 |
|
| 1977 |
Remington SJ, Eyck LF, Matthews BW. Atomic coordinates for T4 phage lysozyme. Biochemical and Biophysical Research Communications. 75: 265-70. PMID 322662 DOI: 10.1016/0006-291X(77)91038-5 |
0.585 |
|
| 1976 |
Matthews BW. Comparison of the predicted and observed secondary structure of T4 phage lysozyme. Biochimica Et Biophysica Acta. 405: 442-51. PMID 1180967 DOI: 10.1016/0005-2795(75)90109-9 |
0.371 |
|
| 1975 |
Fenna RE, Matthews BW. Chlorophyll arrangement in a bacteriochlorophyll protein from chlorobium limicola Nature. 258: 573-577. DOI: 10.1038/258573A0 |
0.397 |
|
| 1974 |
Fenna RE, Matthews BW, Olson JM, Shaw EK. Structure of a bacteriochlorophyll-protein from the green photosynthetic bacterium Chlorobium limicola: crystallographic evidence for a trimer. Journal of Molecular Biology. 84: 231-40. PMID 4830866 DOI: 10.1016/0022-2836(74)90581-6 |
0.373 |
|
| 1974 |
Matthews BW, Remington SJ. The three dimensional structure of the lysozyme from bacteriophage T4. Proceedings of the National Academy of Sciences of the United States of America. 71: 4178-82. PMID 4530293 DOI: 10.1073/Pnas.71.10.4178 |
0.66 |
|
| 1973 |
Blow DM, Matthews BW. Parameter refinement in the multiple isomorphous‐replacement method Acta Crystallographica Section A. 29: 56-62. DOI: 10.1107/S0567739473000124 |
0.496 |
|
| 1972 |
Matthews BW, Colman PM, Jansonius JN, Titani K, Walsh KA, Neurath H. Structure of thermolysin. Nature: New Biology. 238: 41-3. PMID 18663850 DOI: 10.1038/Newbio238041A0 |
0.334 |
|
| 1972 |
Colman PM, Jansonius JN, Matthews BW. The structure of thermolysin: an electron density map at 2-3 A resolution. Journal of Molecular Biology. 70: 701-24. PMID 5083153 DOI: 10.1016/0022-2836(72)90569-4 |
0.369 |
|
| 1972 |
Colman PM, Weaver LH, Matthews BW. Rare earths as isomorphous calcium replacements for protein crystallography. Biochemical and Biophysical Research Communications. 46: 1999-2005. PMID 5018664 DOI: 10.1016/0006-291X(72)90750-4 |
0.333 |
|
| 1971 |
Colman PM, Matthews BW. Symmetry, molecular weight and crystallographic data for sweet potato -amylase. Journal of Molecular Biology. 60: 163-8. PMID 5572101 DOI: 10.1016/0022-2836(71)90455-4 |
0.307 |
|
| 1970 |
Cohen GH, Matthews BW, Davies DR. The relation between gamma-and alpha-chymotrypsin. II. Direct comparison of the electron densities at 5-5 Angstrom resolution. Acta Crystallographica. Section B: Structural Crystallography and Crystal Chemistry. 26: 1062-9. PMID 5537151 |
0.37 |
|
| 1969 |
Cohen GH, Silverton EW, Matthews BW, Braxton H, Davies DR. Structure of gamma-chymotrypsin at 5.5 A resolution. Journal of Molecular Biology. 44: 129-41. PMID 5822897 DOI: 10.1016/0022-2836(69)90409-4 |
0.45 |
|
| 1969 |
Birktoft JJ, Matthews BW, Blow DM. Atomic co-ordinates for tosyl-alpha-chymotrypsin. Biochemical and Biophysical Research Communications. 36: 131-7. PMID 5796747 DOI: 10.1016/0006-291X(69)90659-7 |
0.519 |
|
| 1968 |
Sigler PB, Blow DM, Matthews BW, Henderson R. Structure of crystalline -chymotrypsin. II. A preliminary report including a hypothesis for the activation mechanism. Journal of Molecular Biology. 35: 143-64. PMID 5760561 DOI: 10.1016/S0022-2836(68)80043-9 |
0.733 |
|
| 1968 |
Matthews BW, Cohen GH, Silverton EW, Braxton H, Davies DR. Relation between gamma- and alpha-chymotrypsin. Journal of Molecular Biology. 36: 179-83. PMID 5760536 DOI: 10.1016/0022-2836(68)90228-3 |
0.356 |
|
| 1968 |
Terry WD, Matthews BW, Davies DR. Crystallographic studies of a human immunoglobulin. Nature. 220: 239-41. PMID 4176457 DOI: 10.1038/220239A0 |
0.407 |
|
| 1967 |
Matthews BW, Sigler PB, Henderson R, Blow DM. Three-dimensional structure of tosyl-alpha-chymotrypsin. Nature. 214: 652-6. PMID 6049071 DOI: 10.1038/214652A0 |
0.766 |
|
| 1966 |
Sigler PB, Jeffery BA, Matthews BW, Blow DM. An x-ray diffraction study of inhibited derivatives of alpha-chymotrypsin. Journal of Molecular Biology. 15: 175-92. PMID 5912039 DOI: 10.1016/S0022-2836(66)80219-X |
0.655 |
|
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