Year |
Citation |
Score |
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 |
0.662 |
|
2013 |
Swint-Kruse L, Tungtur S, Zhan H, Becker NA, Maher LJ, Riepe J. In Vitro Thermodynamics of DNA Binding Correlate with In Vivo Transcription Repression by a Synthetic Laci/Galr Paralog Biophysical Journal. 104: 576a. DOI: 10.1016/J.Bpj.2012.11.3198 |
0.535 |
|
2011 |
Tungtur S, Skinner H, Zhan H, Swint-Kruse L, Beckett D. In vivo tests of thermodynamic models of transcription repressor function. Biophysical Chemistry. 159: 142-51. PMID 21715082 DOI: 10.1016/J.Bpc.2011.06.005 |
0.49 |
|
2011 |
Swint-Kruse L, Manley M, Tungtur S, Zhan H. Correlating in Vitro Measurements of Protein-DNA Binding Affinities with in Vivo Repression and Impact on the Growth Rate of the Host Organism Biophysical Journal. 100: 321a. DOI: 10.1016/J.Bpj.2010.12.1955 |
0.503 |
|
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 |
0.569 |
|
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 |
0.692 |
|
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 |
0.683 |
|
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 |
0.596 |
|
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 |
0.675 |
|
2008 |
Zhan H, Taraban M, Trewhella J, Swint-Kruse L. Subdividing repressor function: DNA binding affinity, selectivity, and allostery can be altered by amino acid substitution of nonconserved residues in a LacI/GalR homologue. Biochemistry. 47: 8058-69. PMID 18616293 DOI: 10.1021/Bi800443K |
0.573 |
|
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 |
0.668 |
|
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 |
0.615 |
|
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 |
0.676 |
|
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 |
0.681 |
|
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+ |
0.666 |
|
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 |
0.679 |
|
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