| Year |
Citation |
Score |
| 2018 |
Liu Y, Huang A, Booth RM, Mendes GG, Merchant Z, Matthews KS, Bondos SE. Evolution of the activation domain in a Hox transcription factor. The International Journal of Developmental Biology. 62: 745-753. PMID 30604844 DOI: 10.1387/Ijdb.180151Sb |
0.391 |
|
| 2018 |
Xu JS, Hewitt MN, Gulati JS, Cruz MA, Zhan H, Liu S, Matthews KS. Lactose Repressor Hinge Domain Independently Binds DNA. Protein Science : a Publication of the Protein Society. PMID 29318690 DOI: 10.1002/Pro.3372 |
0.694 |
|
| 2015 |
Bondos SE, Swint-Kruse L, Matthews KS. Flexibility and Disorder in Gene Regulation: LacI/GalR and Hox Proteins. The Journal of Biological Chemistry. 290: 24669-77. PMID 26342073 DOI: 10.1074/Jbc.R115.685032 |
0.378 |
|
| 2015 |
Tsai SP, Howell DW, Huang Z, Hsiao HC, Lu Y, Matthews KS, Lou J, Bondos SE. The effect of protein fusions on the production and mechanical properties of protein-based materials Advanced Functional Materials. 25: 1442-1450. DOI: 10.1002/Adfm.201402997 |
0.42 |
|
| 2014 |
Hsiao HC, Gonzalez KL, Catanese DJ, Jordy KE, Matthews KS, Bondos SE. The intrinsically disordered regions of the Drosophila melanogaster Hox protein ultrabithorax select interacting proteins based on partner topology. Plos One. 9: e108217. PMID 25286318 DOI: 10.1371/Journal.Pone.0108217 |
0.834 |
|
| 2014 |
Churion K, Liu Y, Hsiao HC, Matthews KS, Bondos SE. Measuring Hox-DNA binding by electrophoretic mobility shift analysis. Methods in Molecular Biology (Clifton, N.J.). 1196: 211-30. PMID 25151166 DOI: 10.1007/978-1-4939-1242-1_13 |
0.562 |
|
| 2013 |
Liu Y, Matthews KS, Bondos SE. 149 Generating context-specific functions with intrinsically disordered domains Journal of Biomolecular Structure and Dynamics. 31: 96-97. DOI: 10.1080/07391102.2013.786391 |
0.513 |
|
| 2012 |
Bondos SE, Huang Z, Lu Y, Patterson J, Matthews KS, Lou J, Bayless K. The Transcription Factor Ultrabithorax Forms Extensible, Hierarchically Ordered Assemblies that are Readily Functionalized by Gene Fusion Biophysical Journal. 102: 717a. DOI: 10.1016/J.Bpj.2011.11.3891 |
0.358 |
|
| 2012 |
Bondos SE, Hsiao H, Catanese DJ, Jordy K, Matthews KS. Ultrabithorax, an Intrinsically Disordered Protein, Selects Protein Interactions by Topology Biophysical Journal. 102: 633a. DOI: 10.1016/J.Bpj.2011.11.3447 |
0.814 |
|
| 2011 |
Catanese DJ, Matthews KS. Disconnected Interacting Protein 1 binds with high affinity to pre-tRNA and ADAT. Biochemical and Biophysical Research Communications. 414: 506-11. PMID 21971547 DOI: 10.1016/J.Bbrc.2011.09.096 |
0.822 |
|
| 2011 |
Xu J, Liu S, Chen M, Ma J, Matthews KS. Altering residues N125 and D149 impacts sugar effector binding and allosteric parameters in Escherichia coli lactose repressor. Biochemistry. 50: 9002-13. PMID 21928765 DOI: 10.1021/Bi200896T |
0.589 |
|
| 2011 |
Xu J, Liu KW, Matthews KS, Biswal SL. Monitoring DNA binding to Escherichia coli lactose repressor using quartz crystal microbalance with dissipation. Langmuir : the Acs Journal of Surfaces and Colloids. 27: 4900-5. PMID 21410208 DOI: 10.1021/La200056H |
0.574 |
|
| 2011 |
Liu Y, Matthews KS, Bondos SE. Generating Context-Specific Functions with Intrinsically Disordered Domains Biophysical Journal. 100: 185a. DOI: 10.1016/J.Bpj.2010.12.1228 |
0.531 |
|
| 2011 |
Jamison JA, Bryant EL, Kadali SB, Wong MS, Colvin VL, Matthews KS, Calabretta MK. Altering protein surface charge with chemical modification modulates protein-gold nanoparticle aggregation Journal of Nanoparticle Research. 13: 625-636. DOI: 10.1007/S11051-010-0057-5 |
0.782 |
|
| 2011 |
Huang Z, Salim T, Brawley A, Patterson J, Matthews KS, Bondos SE. Functionalization and patterning of protein-based materials using active ultrabithorax chimeras Advanced Functional Materials. 21: 2633-2640. DOI: 10.1002/Adfm.201100067 |
0.322 |
|
| 2010 |
Zhan H, Camargo M, Matthews KS. Positions 94-98 of the lactose repressor N-subdomain monomer-monomer interface are critical for allosteric communication. Biochemistry. 49: 8636-45. PMID 20804152 DOI: 10.1021/Bi101106X |
0.579 |
|
| 2010 |
Catanese DJ, Matthews KS. High affinity, dsRNA binding by disconnected interacting protein 1. Biochemical and Biophysical Research Communications. 399: 186-91. PMID 20643095 DOI: 10.1016/J.Bbrc.2010.07.052 |
0.83 |
|
| 2010 |
Rutkauskas D, Zhan H, Matthews KS, Pavone F, Vanzi F. Dna Looping By Lactose Repressor Requires Tetramer Opening Biophysical Journal. 98: 72a. DOI: 10.1016/J.Bpj.2009.12.407 |
0.719 |
|
| 2009 |
Rutkauskas D, Zhan H, Matthews KS, Pavone FS, Vanzi F. Tetramer opening in LacI-mediated DNA looping. Proceedings of the National Academy of Sciences of the United States of America. 106: 16627-32. PMID 19805348 DOI: 10.1073/Pnas.0904617106 |
0.702 |
|
| 2009 |
Liu Y, Matthews KS, Bondos SE. Internal regulatory interactions determine DNA binding specificity by a Hox transcription factor. Journal of Molecular Biology. 390: 760-74. PMID 19481089 DOI: 10.1016/J.Jmb.2009.05.059 |
0.572 |
|
| 2009 |
Xu J, Matthews KS. Flexibility in the inducer binding region is crucial for allostery in the Escherichia coli lactose repressor. Biochemistry. 48: 4988-98. PMID 19368358 DOI: 10.1021/Bi9002343 |
0.566 |
|
| 2009 |
Greer AM, Huang Z, Oriakhi A, Lu Y, Lou J, Matthews KS, Bondos SE. The Drosophila transcription factor ultrabithorax self-assembles into protein-based biomaterials with multiple morphologies. Biomacromolecules. 10: 829-37. PMID 19296655 DOI: 10.1021/Bm801315V |
0.35 |
|
| 2009 |
Swint-Kruse L, Matthews KS. Allostery in the LacI/GalR family: variations on a theme. Current Opinion in Microbiology. 12: 129-37. PMID 19269243 DOI: 10.1016/J.Mib.2009.01.009 |
0.56 |
|
| 2009 |
Zhan H, Sun Z, Matthews KS. Functional impact of polar and acidic substitutions in the lactose repressor hydrophobic monomer.monomer interface with a buried lysine. Biochemistry. 48: 1305-14. PMID 19166325 DOI: 10.1021/Bi801357F |
0.629 |
|
| 2009 |
Rutkauskas D, Vanzi F, Zhan H, Matthews KS, Pavone FS. Single Molecule Measurements Of The Role Of Tetramer Opening In LacI-mediated DNA Looping Biophysical Journal. 96: 62a-63a. DOI: 10.1016/J.Bpj.2008.12.221 |
0.683 |
|
| 2008 |
Liu Y, Matthews KS, Bondos SE. Multiple intrinsically disordered sequences alter DNA binding by the homeodomain of the Drosophila hox protein ultrabithorax. The Journal of Biological Chemistry. 283: 20874-87. PMID 18508761 DOI: 10.1074/Jbc.M800375200 |
0.514 |
|
| 2008 |
Taraban M, Zhan H, Whitten AE, Langley DB, Matthews KS, Swint-Kruse L, Trewhella J. Ligand-induced conformational changes and conformational dynamics in the solution structure of the lactose repressor protein. Journal of Molecular Biology. 376: 466-81. PMID 18164724 DOI: 10.1016/J.Jmb.2007.11.067 |
0.694 |
|
| 2007 |
Wilson CJ, Zhan H, Swint-Kruse L, Matthews KS. The lactose repressor system: paradigms for regulation, allosteric behavior and protein folding. Cellular and Molecular Life Sciences : Cmls. 64: 3-16. PMID 17103112 DOI: 10.1007/S00018-006-6296-Z |
0.687 |
|
| 2007 |
Wilson CJ, Zhan H, Swint-Kruse L, Matthews KS. Ligand interactions with lactose repressor protein and the repressor-operator complex: the effects of ionization and oligomerization on binding. Biophysical Chemistry. 126: 94-105. PMID 16860458 DOI: 10.1016/J.Bpc.2006.06.005 |
0.763 |
|
| 2006 |
Calabretta MK, Matthews KS, Colvin VL. DNA binding to protein-gold nanocrystal conjugates. Bioconjugate Chemistry. 17: 1156-61. PMID 16984123 DOI: 10.1021/Bc0600867 |
0.812 |
|
| 2006 |
Zhan H, Swint-Kruse L, Matthews KS. Extrinsic interactions dominate helical propensity in coupled binding and folding of the lactose repressor protein hinge helix. Biochemistry. 45: 5896-906. PMID 16669632 DOI: 10.1021/Bi052619P |
0.742 |
|
| 2006 |
Bondos SE, Tan XX, Matthews KS. Physical and genetic interactions link hox function with diverse transcription factors and cell signaling proteins. Molecular & Cellular Proteomics : McP. 5: 824-34. PMID 16455680 DOI: 10.1074/Mcp.M500256-Mcp200 |
0.398 |
|
| 2005 |
Wilson CJ, Das P, Clementi C, Matthews KS, Wittung-Stafshede P. The experimental folding landscape of monomeric lactose repressor, a large two-domain protein, involves two kinetic intermediates. Proceedings of the National Academy of Sciences of the United States of America. 102: 14563-8. PMID 16203983 DOI: 10.1073/Pnas.0505808102 |
0.632 |
|
| 2005 |
Das P, Wilson CJ, Fossati G, Wittung-Stafshede P, Matthews KS, Clementi C. Characterization of the folding landscape of monomeric lactose repressor: quantitative comparison of theory and experiment. Proceedings of the National Academy of Sciences of the United States of America. 102: 14569-74. PMID 16203982 DOI: 10.1073/Pnas.0505844102 |
0.621 |
|
| 2005 |
Swint-Kruse L, Zhan H, Matthews KS. Integrated insights from simulation, experiment, and mutational analysis yield new details of LacI function. Biochemistry. 44: 11201-13. PMID 16101304 DOI: 10.1021/Bi050404+ |
0.707 |
|
| 2005 |
Calabretta M, Jamison JA, Falkner JC, Liu Y, Yuhas BD, Matthews KS, Colvin VL. Analytical ultracentrifugation for characterizing nanocrystals and their bioconjugates. Nano Letters. 5: 963-7. PMID 15884903 DOI: 10.1021/Nl047926F |
0.742 |
|
| 2004 |
Swint-Kruse L, Matthews KS. Thermodynamics, protein modification, and molecular dynamics in characterizing lactose repressor protein: strategies for complex analyses of protein structure-function. Methods in Enzymology. 379: 188-209. PMID 15051359 DOI: 10.1016/S0076-6879(04)79011-4 |
0.504 |
|
| 2004 |
Bondos SE, Catanese DJ, Tan XX, Bicknell A, Li L, Matthews KS. Hox transcription factor ultrabithorax Ib physically and genetically interacts with disconnected interacting protein 1, a double-stranded RNA-binding protein. The Journal of Biological Chemistry. 279: 26433-44. PMID 15039447 DOI: 10.1074/Jbc.M312842200 |
0.83 |
|
| 2003 |
Swint-Kruse L, Zhan H, Fairbanks BM, Maheshwari A, Matthews KS. Perturbation from a distance: mutations that alter LacI function through long-range effects. Biochemistry. 42: 14004-16. PMID 14636069 DOI: 10.1021/Bi035116X |
0.718 |
|
| 2003 |
Flynn TC, Swint-Kruse L, Kong Y, Booth C, Matthews KS, Ma J. Allosteric transition pathways in the lactose repressor protein core domains: asymmetric motions in a homodimer. Protein Science : a Publication of the Protein Society. 12: 2523-41. PMID 14573864 DOI: 10.1110/Ps.03188303 |
0.429 |
|
| 2002 |
Swint-Kruse L, Larson C, Pettitt BM, Matthews KS. Fine-tuning function: correlation of hinge domain interactions with functional distinctions between LacI and PurR. Protein Science : a Publication of the Protein Society. 11: 778-94. PMID 11910022 DOI: 10.1110/Ps.4050102 |
0.506 |
|
| 2002 |
Tan XX, Bondos S, Li L, Matthews KS. Transcription activation by ultrabithorax Ib protein requires a predicted alpha-helical region. Biochemistry. 41: 2774-85. PMID 11851425 DOI: 10.1021/Bi011967Y |
0.385 |
|
| 2002 |
Nichols NM, Matthews KS. Human p53 phosphorylation mimic, S392E, increases nonspecific DNA affinity and thermal stability. Biochemistry. 41: 170-8. PMID 11772014 DOI: 10.1021/Bi011736R |
0.766 |
|
| 2001 |
Falcon CM, Matthews KS. Engineered disulfide linking the hinge regions within lactose repressor dimer increases operator affinity, decreases sequence selectivity, and alters allostery. Biochemistry. 40: 15650-9. PMID 11747440 DOI: 10.1021/Bi0114067 |
0.567 |
|
| 2001 |
Bell CE, Barry J, Matthews KS, Lewis M. Structure of a variant of lac repressor with increased thermostability and decreased affinity for operator. Journal of Molecular Biology. 313: 99-109. PMID 11601849 DOI: 10.1006/Jmbi.2001.5041 |
0.461 |
|
| 2001 |
Nichols NM, Matthews KS. p53 unfolding detected by CD but not by tryptophan fluorescence. Biochemical and Biophysical Research Communications. 288: 111-5. PMID 11594760 DOI: 10.1006/Bbrc.2001.5764 |
0.73 |
|
| 2001 |
Moraitis MI, Xu H, Matthews KS. Ion concentration and temperature dependence of DNA binding: comparison of PurR and LacI repressor proteins. Biochemistry. 40: 8109-17. PMID 11434780 DOI: 10.1021/Bi0028643 |
0.801 |
|
| 2001 |
Nichols NM, Matthews KS. Protein-DNA binding correlates with structural thermostability for the full-length human p53 protein. Biochemistry. 40: 3847-58. PMID 11300764 DOI: 10.1021/Bi002088Z |
0.79 |
|
| 2001 |
Swint-Kruse L, Elam CR, Lin JW, Wycuff DR, Matthews KS. Plasticity of quaternary structure: Twenty-two ways to form a LacI dimer Protein Science. 10: 262-276. PMID 11266612 DOI: 10.1110/Ps.35801 |
0.48 |
|
| 2000 |
Falcon CM, Matthews KS. Operator DNA sequence variation enhances high affinity binding by hinge helix mutants of lactose repressor protein. Biochemistry. 39: 11074-83. PMID 10998245 DOI: 10.1021/Bi000924Z |
0.573 |
|
| 1999 |
Falcon CM, Matthews KS. Glycine insertion in the hinge region of lactose repressor protein alters DNA binding. The Journal of Biological Chemistry. 274: 30849-57. PMID 10521477 DOI: 10.1074/Jbc.274.43.30849 |
0.538 |
|
| 1999 |
Barry JK, Matthews KS. Thermodynamic analysis of unfolding and dissociation in lactose repressor protein. Biochemistry. 38: 6520-8. PMID 10350470 DOI: 10.1021/Bi9900727 |
0.41 |
|
| 1999 |
Ozarowski A, Barry JK, Matthews KS, Maki AH. Ligand-induced conformational changes in lactose repressor: a phosphorescence and ODMR study of single-tryptophan mutants. Biochemistry. 38: 6715-22. PMID 10346891 DOI: 10.1021/Bi990242F |
0.505 |
|
| 1999 |
Barry JK, Matthews KS. Substitutions at histidine 74 and aspartate 278 alter ligand binding and allostery in lactose repressor protein. Biochemistry. 38: 3579-90. PMID 10090744 DOI: 10.1021/Bi982577N |
0.521 |
|
| 1998 |
Xu H, Moraitis M, Reedstrom RJ, Matthews KS. Kinetic and thermodynamic studies of purine repressor binding to corepressor and operator DNA. The Journal of Biological Chemistry. 273: 8958-64. PMID 9535880 DOI: 10.1074/Jbc.273.15.8958 |
0.776 |
|
| 1998 |
Swint-Kruse L, Matthews KS, Smith PE, Pettitt BM. Comparison of simulated and experimentally determined dynamics for a variant of the Lacl DNA-binding domain, Nlac-P. Biophysical Journal. 74: 413-21. PMID 9449341 DOI: 10.1016/S0006-3495(98)77798-7 |
0.436 |
|
| 1998 |
Matthews KS, Nichols JC. Lactose repressor protein: functional properties and structure. Progress in Nucleic Acid Research and Molecular Biology. 58: 127-64. PMID 9308365 DOI: 10.1016/S0079-6603(08)60035-5 |
0.502 |
|
| 1997 |
Barry JK, Matthews KS. Ligand-induced conformational changes in lactose repressor: a fluorescence study of single tryptophan mutants. Biochemistry. 36: 15632-42. PMID 9398291 DOI: 10.1021/Bi971685R |
0.476 |
|
| 1997 |
Falcon CM, Swint-Kruse L, Matthews KS. Designed disulfide between N-terminal domains of lactose repressor disrupts allosteric linkage. The Journal of Biological Chemistry. 272: 26818-21. PMID 9341111 DOI: 10.1074/Jbc.272.43.26818 |
0.535 |
|
| 1997 |
Nichols JC, Matthews KS. Combinatorial mutations of lac repressor. Stability of monomer-monomer interface is increased by apolar substitution at position 84. The Journal of Biological Chemistry. 272: 18550-7. PMID 9228020 DOI: 10.1074/Jbc.272.30.18550 |
0.439 |
|
| 1997 |
Li L, Matthews KS. Differences in water release with DNA binding by ultrabithorax and deformed homeodomains. Biochemistry. 36: 7003-11. PMID 9188697 DOI: 10.1021/Bi962966M |
0.507 |
|
| 1997 |
Matthews KS. Protein folding and assembly minireview series Journal of Biological Chemistry. 272: 699. DOI: 10.1074/Jbc.272.2.699 |
0.4 |
|
| 1997 |
Wycuff DR, Matthews KS. Effect of leucine heptad repeat sequence variation on assembly and ligand binding parameters of lactose repressor protein Faseb Journal. 11: A1208. |
0.351 |
|
| 1996 |
Li L, von Kessler D, Beachy PA, Matthews KS. pH-dependent enhancement of DNA binding by the ultrabithorax homeodomain. Biochemistry. 35: 9832-9. PMID 8703957 DOI: 10.1021/Bi9606049 |
0.495 |
|
| 1996 |
Matthews KS. The whole lactose repressor. Science (New York, N.Y.). 271: 1245-6. PMID 8638104 DOI: 10.1126/Science.271.5253.1245 |
0.312 |
|
| 1996 |
Li L, Von Kesslet D, Peachy PA, Matthews KS. pH-dependent DNA binding by homeodomain from ultrabithorax protein Faseb Journal. 10: A1233. |
0.415 |
|
| 1995 |
Li L, Matthews KS. Characterization of mutants affecting the KRK sequence in the carboxyl-terminal domain of lac repressor. The Journal of Biological Chemistry. 270: 10640-9. PMID 7738001 DOI: 10.1074/Jbc.270.18.10640 |
0.49 |
|
| 1995 |
Chang WI, Matthews KS. Role of Asp274 in lac repressor: diminished sugar binding and altered conformational effects in mutants. Biochemistry. 34: 9227-34. PMID 7619824 DOI: 10.1021/Bi00028A036 |
0.537 |
|
| 1994 |
Liu YC, Matthews KS. trp repressor mutations alter DNA complex stoichiometry. The Journal of Biological Chemistry. 269: 1692-8. PMID 8294416 |
0.471 |
|
| 1994 |
Chen J, Alberti S, Matthews KS. Wild-type operator binding and altered cooperativity for inducer binding of lac repressor dimer mutant R3. The Journal of Biological Chemistry. 269: 12482-7. PMID 8175655 |
0.428 |
|
| 1994 |
Chang WI, Barrera P, Matthews KS. Identification and characterization of aspartate residues that play key roles in the allosteric regulation of a transcription factor: aspartate 274 is essential for inducer binding in lac repressor. Biochemistry. 33: 3607-16. PMID 8142359 DOI: 10.1021/Bi00178A018 |
0.494 |
|
| 1994 |
Chen J, Surendran R, Lee JC, Matthews KS. Construction of a dimeric repressor: dissection of subunit interfaces in Lac repressor. Biochemistry. 33: 1234-41. PMID 8110756 DOI: 10.1021/Bi00171A025 |
0.352 |
|
| 1994 |
Chen J, Matthews KS. Subunit dissociation affects DNA binding in a dimeric lac repressor produced by C-terminal deletion. Biochemistry. 33: 8728-35. PMID 8038163 DOI: 10.1021/Bi00195A014 |
0.506 |
|
| 1993 |
Liu YC, Matthews KS. Trp repressor interaction with bromodeoxyuridine-substituted operators alters UV-induced perturbation pattern in a sequence-dependent manner. Biochemistry. 32: 10532-42. PMID 8399199 DOI: 10.1021/Bi00091A002 |
0.443 |
|
| 1993 |
Chang WI, Olson JS, Matthews KS. Lysine 84 is at the subunit interface of lac repressor protein. The Journal of Biological Chemistry. 268: 17613-22. PMID 8349640 |
0.399 |
|
| 1993 |
Nichols JC, Vyas NK, Quiocho FA, Matthews KS. Model of lactose repressor core based on alignment with sugar-binding proteins is concordant with genetic and chemical data. The Journal of Biological Chemistry. 268: 17602-12. PMID 8349639 DOI: 10.2210/Pdb1Ltp/Pdb |
0.53 |
|
| 1993 |
Burns LE, Maki AH, Spotts R, Matthews KS. Characterization of the two tryptophan residues of the lactose repressor from Escherichia coli by phosphorescence and optical detection of magnetic resonance. Biochemistry. 32: 12821-9. PMID 8251503 DOI: 10.1021/Bi00210A034 |
0.345 |
|
| 1993 |
Liu YC, Matthews KS. Dependence of trp repressor-operator affinity, stoichiometry, and apparent cooperativity on DNA sequence and size. The Journal of Biological Chemistry. 268: 23239-49. PMID 8226846 |
0.352 |
|
| 1992 |
Chen J, Matthews KS. Deletion of lactose repressor carboxyl-terminal domain affects tetramer formation. The Journal of Biological Chemistry. 267: 13843-50. PMID 1629185 |
0.392 |
|
| 1992 |
Chakerian AE, Matthews KS. Effect of lac repressor oligomerization on regulatory outcome. Molecular Microbiology. 6: 963-8. PMID 1584025 DOI: 10.1111/J.1365-2958.1992.Tb02162.X |
0.56 |
|
| 1992 |
Matthews KS. DNA looping. Microbiological Reviews. 56: 123-36. PMID 1579106 |
0.454 |
|
| 1992 |
Chen J, Matthews KS. T41 mutation in lac repressor is Tyr282----Asp. Gene. 111: 145-6. PMID 1547952 DOI: 10.1016/0378-1119(92)90618-Y |
0.365 |
|
| 1991 |
Allen TD, Wick KL, Matthews KS. Identification of amino acids in lac repressor protein cross-linked to operator DNA specifically substituted with bromodeoxyuridine. The Journal of Biological Chemistry. 266: 6113-9. PMID 2007569 |
0.319 |
|
| 1991 |
Wick KL, Matthews KS. Interactions between lac repressor protein and site-specific bromodeoxyuridine-substituted operator DNA. Ultraviolet footprinting and protein-DNA cross-link formation. The Journal of Biological Chemistry. 266: 6106-12. PMID 2007568 |
0.38 |
|
| 1991 |
Gardner JA, Matthews KS. Energy transfer in lactose repressor protein modified with N-[[(iodoacetyl)amino]ethyl]-5-naphthylamine-1-sulfonate. Biochemistry. 30: 2707-12. PMID 2001358 DOI: 10.1021/Bi00224A019 |
0.33 |
|
| 1991 |
Chakerian AE, Tesmer VM, Manly SP, Brackett JK, Lynch MJ, Hoh JT, Matthews KS. Evidence for leucine zipper motif in lactose repressor protein. The Journal of Biological Chemistry. 266: 1371-4. PMID 1988425 |
0.502 |
|
| 1991 |
Chakerian AE, Matthews KS. Characterization of mutations in oligomerization domain of Lac repressor protein. The Journal of Biological Chemistry. 266: 22206-14. PMID 1939243 |
0.461 |
|
| 1991 |
Matthews KS, Chakerian AE, Gardner JA. Protein chemical modification as probe of structure-function relationships. Methods in Enzymology. 208: 468-96. PMID 1779844 DOI: 10.1016/0076-6879(91)08025-D |
0.37 |
|
| 1991 |
Spotts RO, Chakerian AE, Matthews KS. Arginine 197 of lac repressor contributes significant energy to inducer binding. Confirmation of homology to periplasmic sugar binding proteins. The Journal of Biological Chemistry. 266: 22998-3002. PMID 1744095 |
0.47 |
|
| 1990 |
He JJ, Matthews KS. Effect of amino acid alterations in the tryptophan-binding site of the trp repressor. The Journal of Biological Chemistry. 265: 731-7. PMID 2295616 |
0.446 |
|
| 1990 |
Gardner JA, Matthews KS. Characterization of two mutant lactose repressor proteins containing single tryptophans. The Journal of Biological Chemistry. 265: 21061-7. PMID 2250012 |
0.326 |
|
| 1990 |
Royer CA, Gardner JA, Beechem JM, Brochon JC, Matthews KS. Resolution of the fluorescence decay of the two tryptophan residues of lac repressor using single tryptophan mutants. Biophysical Journal. 58: 363-78. PMID 2207244 DOI: 10.1016/S0006-3495(90)82383-3 |
0.349 |
|
| 1990 |
Royer CA, Chakerian AE, Matthews KS. Macromolecular binding equilibria in the lac repressor system: studies using high-pressure fluorescence spectroscopy. Biochemistry. 29: 4959-66. PMID 2194564 DOI: 10.1021/Bi00472A028 |
0.386 |
|
| 1989 |
Chou WY, Bieber C, Matthews KS. Tryptophan and 8-anilino-1-naphthalenesulfonate compete for binding to trp repressor. The Journal of Biological Chemistry. 264: 18309-13. PMID 2808378 |
0.42 |
|
| 1989 |
Chou WY, Matthews KS. Mutation in hinge region of lactose repressor protein alters physical and functional properties. The Journal of Biological Chemistry. 264: 6171-6. PMID 2703485 |
0.372 |
|
| 1989 |
Chou WY, Matthews KS. Serine to cysteine mutations in trp repressor protein alter tryptophan and operator binding. The Journal of Biological Chemistry. 264: 18314-9. PMID 2509454 |
0.382 |
|
| 1988 |
Bae SJ, Chou WY, Matthews K, Sturtevant JM. Tryptophan repressor of Escherichia coli shows unusual thermal stability. Proceedings of the National Academy of Sciences of the United States of America. 85: 6731-2. PMID 3045823 DOI: 10.1073/Pnas.85.18.6731 |
0.361 |
|
| 1988 |
Sams CF, Matthews KS. Diethyl pyrocarbonate reaction with the lactose repressor protein affects both inducer and DNA binding. Biochemistry. 27: 2277-81. PMID 2968118 DOI: 10.1021/Bi00407A005 |
0.526 |
|
| 1987 |
Whitson PA, Hsieh WT, Wells RD, Matthews KS. Influence of supercoiling and sequence context on operator DNA binding with lac repressor. The Journal of Biological Chemistry. 262: 14592-9. PMID 3667592 |
0.326 |
|
| 1987 |
Hsieh WT, Whitson PA, Matthews KS, Wells RD. Influence of sequence and distance between two operators on interaction with the lac repressor. The Journal of Biological Chemistry. 262: 14583-91. PMID 3667591 |
0.343 |
|
| 1987 |
Whitson PA, Hsieh WT, Wells RD, Matthews KS. Supercoiling facilitates lac operator-repressor-pseudooperator interactions. The Journal of Biological Chemistry. 262: 4943-6. PMID 3549713 |
0.375 |
|
| 1987 |
Gardner JA, Matthews KS. Mapping and analysis of protein sulfhydryl groups by modification with 2-bromoacetamido-4-nitrophenol. Analytical Biochemistry. 167: 140-4. PMID 3434790 DOI: 10.1016/0003-2697(87)90143-6 |
0.332 |
|
| 1987 |
Chakerian AE, Olson JS, Matthews KS. Thermodynamic analysis of inducer binding to the lactose repressor protein: contributions of galactosyl hydroxyl groups and beta substituents. Biochemistry. 26: 7250-5. PMID 3427073 DOI: 10.1021/Bi00397A009 |
0.417 |
|
| 1987 |
Whitson PA, Matthews KS. Chemical modification of arginine residues in the lactose repressor. Biochemistry. 26: 6502-7. PMID 3322382 DOI: 10.1021/Bi00394A032 |
0.535 |
|
| 1986 |
Royer CA, Weber G, Daly TJ, Matthews KS. Dissociation of the lactose repressor protein tetramer using high hydrostatic pressure. Biochemistry. 25: 8308-15. PMID 3545291 DOI: 10.1021/Bi00373A027 |
0.379 |
|
| 1986 |
Daly TJ, Matthews KS. Allosteric regulation of inducer and operator binding to the lactose repressor. Biochemistry. 25: 5479-84. PMID 3535880 DOI: 10.1021/Bi00367A020 |
0.498 |
|
| 1986 |
Daly TJ, Matthews KS. Characterization and modification of a monomeric mutant of the lactose repressor protein. Biochemistry. 25: 5474-8. PMID 3535879 DOI: 10.1021/Bi00367A019 |
0.499 |
|
| 1986 |
Daly TJ, Olson JS, Matthews KS. Formation of mixed disulfide adducts at cysteine-281 of the lactose repressor protein affects operator and inducer binding parameters. Biochemistry. 25: 5468-74. PMID 3535878 DOI: 10.1021/Bi00367A018 |
0.588 |
|
| 1986 |
Whitson PA, Olson JS, Matthews KS. Thermodynamic analysis of the lactose repressor-operator DNA interaction. Biochemistry. 25: 3852-8. PMID 3527258 DOI: 10.1021/Bi00361A017 |
0.484 |
|
| 1986 |
Whitson PA, Matthews KS. Dissociation of the lactose repressor-operator DNA complex: Effects of size and sequence context of operator-containing DNA Biochemistry. 25: 3845-3852. PMID 3527257 DOI: 10.1021/Bi00361A016 |
0.401 |
|
| 1985 |
Manly SP, Matthews KS, Sturtevant JM. Thermal denaturation of the core protein of lac repressor. Biochemistry. 24: 3842-6. PMID 3902076 DOI: 10.1021/Bi00336A004 |
0.426 |
|
| 1985 |
Hsieh WT, Matthews KS. Lactose repressor protein modified with dansyl chloride: activity effects and fluorescence properties. Biochemistry. 24: 3043-9. PMID 3893536 DOI: 10.1021/Bi00333A036 |
0.555 |
|
| 1985 |
Chakerian AE, Pfahl M, Olson JS, Matthews KS. A mutant lactose represser with altered inducer and operator binding parameters Journal of Molecular Biology. 183: 43-51. PMID 3892017 DOI: 10.1016/0022-2836(85)90279-7 |
0.545 |
|
| 1985 |
Daly TJ, Olson JS, Matthews KS. Modification of cysteine 281 in the lac repressor protein alters inducer binding kinetics Federation Proceedings. 44: No. 7062. |
0.46 |
|
| 1984 |
Sams CF, Vyas NK, Quiocho FA, Matthews KS. Predicted structure of the sugar-binding site of the lac repressor Nature. 310: 429-430. PMID 6462229 DOI: 10.1038/310429A0 |
0.548 |
|
| 1984 |
Whitson PA, Burgum AA, Matthews KS. Trinitrobenzenesulfonate modification of the lysine residues in lactose repressor protein Biochemistry. 23: 6046-6052. PMID 6441596 DOI: 10.1021/Bi00320A023 |
0.568 |
|
| 1984 |
Manly SP, Bennett GN, Matthews KS. Enzymatic digestion of operator DNA in the presence of the lac repressor tryptic core Journal of Molecular Biology. 179: 335-350. PMID 6392563 DOI: 10.1016/0022-2836(84)90069-X |
0.501 |
|
| 1984 |
Manly SP, Matthews KS. lac operator DNA modification in the presence of proteolytic fragments of the repressor protein Journal of Molecular Biology. 179: 315-333. PMID 6392562 DOI: 10.1016/0022-2836(84)90068-8 |
0.483 |
|
| 1983 |
Manly SP, Bennett GN, Matthews KS. Perturbation of lac operator DNA modification by tryptic core protein from lac repressor Proceedings of the National Academy of Sciences of the United States of America. 80: 6219-6223. PMID 6353413 DOI: 10.1073/Pnas.80.20.6219 |
0.49 |
|
| 1981 |
Hsieh WT, Matthews KS. Tetranitromethane modification of the tyrosine residues of the lactose repressor. The Journal of Biological Chemistry. 256: 4856-62. PMID 7014561 |
0.474 |
|
| 1981 |
O'Gorman RB, Ferguson L, Betz JL, Sadler JR, Matthews KS. Determination of the ligand-binding characteristics of several tight-binding mutants of the lactose repressor protein Bba Section Nucleic Acids and Protein Synthesis. 653: 236-247. PMID 7013812 DOI: 10.1016/0005-2787(81)90159-3 |
0.577 |
|
| 1980 |
Dunaway M, Matthews KS. Hybrid tetramers of native and core lactose repressor protein. Assessment of operator and nonspecific DNA binding parameters and their relationship Journal of Biological Chemistry. 255: 10120-10127. PMID 7000773 |
0.436 |
|
| 1980 |
Dunaway M, Olson JS, Rosenberg JM, Kallai OB, Dickerson RE, Matthews KS. Kinetic studies of inducer binding to lac repressor.operator complex. The Journal of Biological Chemistry. 255: 10115-9. PMID 7000772 |
0.391 |
|
| 1980 |
O'Gorman RB, Rosenberg JM, Kallai OB, Dickerson RE, Itakura K, Riggs AD, Matthews KS. Equilibrium binding of inducer to lac repressor.operator DNA complex. The Journal of Biological Chemistry. 255: 10107-14. PMID 7000771 |
0.455 |
|
| 1980 |
O'Gorman RB, Dunaway M, Matthews KS. DNA binding characteristics of lactose repressor and the trypsin-resistant core repressor Journal of Biological Chemistry. 255: 10100-10106. PMID 7000770 |
0.391 |
|
| 1980 |
Dunaway M, Manly SP, Matthews KS. Model for lactose repressor protein and its interaction with ligands Proceedings of the National Academy of Sciences of the United States of America. 77: 7181-7185. PMID 6938962 DOI: 10.1073/Pnas.77.12.7181 |
0.511 |
|
| 1979 |
Brown RD, Matthews KS. Chemical modification of lactose repressor protein using N-substituted maleimides Journal of Biological Chemistry. 254: 5128-5134. PMID 376506 |
0.355 |
|
| 1979 |
Matthews KS. Tryptic core protein of lactose repressor binds operator DNA Journal of Biological Chemistry. 254: 3348-3353. PMID 372190 |
0.506 |
|
| 1979 |
Manly SP, Matthews KS. Activity changes in lac repressor with cysteine oxidation Journal of Biological Chemistry. 254: 3341-3347. PMID 372189 |
0.419 |
|
| 1978 |
Ellen Friedman B, Matthews KS. Inducer binding to LAC repressor: Effects of poly[d(A-T)] and trypsin digestion Biochemical and Biophysical Research Communications. 85: 497-504. PMID 369559 DOI: 10.1016/S0006-291X(78)80069-2 |
0.534 |
|
| 1978 |
Burgum AA, Matthews KS. Lactose repressor protein modified with fluorescein mercuric acetate Journal of Biological Chemistry. 253: 4279-4286. PMID 350871 |
0.321 |
|
| 1977 |
Alexander ME, Burgum AA, Noall RA, Shaw MD, Matthews KS. Modification of tyrosine residues of the lactose repressor protein Bba - Protein Structure. 493: 367-379. PMID 329889 DOI: 10.1016/0005-2795(77)90193-3 |
0.509 |
|
| 1977 |
Yang DS, Burgum AA, Matthews KS. Modification of the cysteine residues of the lactose repressor protein using chromophoric probes Bba - Protein Structure. 493: 24-36. PMID 328057 DOI: 10.1016/0005-2795(77)90257-4 |
0.467 |
|
| 1977 |
Matthews HR, Matthews KS, Opella SJ. Selectively deuterated amino acid analogues synthesis, Incorporation into proteins and NMR properties Bba - General Subjects. 497: 1-13. PMID 321035 DOI: 10.1016/0304-4165(77)90134-9 |
0.54 |
|
| 1977 |
Matthews KS, Wade-Jardetzky NG, Graber M, Conover WW, Jardetzky O. High resolution 1H NMR of a selectively deuterated analogs of the lac repressor. Biochimica Et Biophysica Acta. 490: 534-8. PMID 319837 DOI: 10.1016/0005-2795(77)90031-9 |
0.53 |
|
| 1977 |
Ellen Friedman B, Olson JS, Matthews KS. Interaction of lac repressor with inducer. Kinetic and equilibrium measurements Journal of Molecular Biology. 111: 27-39. PMID 16140 DOI: 10.1016/S0022-2836(77)80129-0 |
0.479 |
|
| 1976 |
Yang DS, Matthews KS. Lactose repressor protein reaction with 2-chloromercuri-4-nitrophenol Journal of Molecular Biology. 103: 433-437. PMID 781275 DOI: 10.1016/0022-2836(76)90322-3 |
0.519 |
|
| 1976 |
Friedman B, Olson JS, Matthews KS. Kinetic studies of inducer binding to lactose repressor protein Journal of Biological Chemistry. 251: 1171-1174. PMID 765339 |
0.39 |
|
| 1974 |
Matthews KS. Ultraviolet difference spectra of the lactose repressor protein II. Trypsin core protein Bba - Protein Structure. 359: 334-340. PMID 4605413 DOI: 10.1016/0005-2795(74)90232-3 |
0.472 |
|
| 1973 |
Matthews KS, Matthews HR, Thielmann HW, Jardetzky O. Ultraviolet difference spectra of the lactose repressor protein Bba - Protein Structure. 295: 159-165. PMID 4567971 DOI: 10.1016/0005-2795(73)90083-4 |
0.648 |
|
| 1973 |
Matthews HR, Thielmann HW, Matthews KS, Jardetzky O. NMR studies of the binding of an inducer and an anti-inducer to the lac repressor. Annals of the New York Academy of Sciences. 222: 226-9. PMID 4522430 DOI: 10.1111/J.1749-6632.1973.Tb15264.X |
0.603 |
|
| 1972 |
Matthews KS, Cole RD. Interaction of lysozyme with f2 bacteriophage. Journal of Molecular Biology. 68: 173-6. PMID 5050361 DOI: 10.1016/0022-2836(72)90271-9 |
0.466 |
|
| 1972 |
Matthews KS, Cole RD. Inhibition of the self-assembly of capsid protein from f2 phage by urea. The Journal of Biological Chemistry. 247: 609-10. PMID 5009703 |
0.472 |
|
| 1972 |
Matthews KS, Cole RD. Shell formation by capsid protein of f2 bacteriophage. Journal of Molecular Biology. 65: 1-15. PMID 4553257 DOI: 10.1016/0022-2836(72)90487-1 |
0.502 |
|
| 1972 |
Matthews KS, Cole RD. Effects of chemical modification of f2 viral coat protein on its shell-forming activity. Journal of Molecular Biology. 65: 17-23. PMID 4553256 DOI: 10.1016/0022-2836(72)90488-3 |
0.569 |
|
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