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Hongli Zhan, Ph.D. - Publications

Affiliations: 
Rice University, Houston, TX 
Area:
Structure and function of genetic regulatory proteins
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16 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
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  0.661
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  0.534
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  0.489
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  0.674
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  0.572
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  0.667
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  0.68
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  0.678
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