Year |
Citation |
Score |
2023 |
Li H, Hu L, Cuffee CW, Mohamed M, Li Q, Liu Q, Zhou L, Liu Q. Correction: Interdomain interactions dictate the function of the Candida albicans Hsp110 protein Msi3. The Journal of Biological Chemistry. 299: 102879. PMID 36669421 DOI: 10.1016/j.jbc.2023.102879 |
0.363 |
|
2021 |
Li H, Musayev FN, Yang J, Su J, Liu Q, Wang W, Fang X, Zhou L, Liu Q. A novel and unique ATP hydrolysis to AMP by a human Hsp70 BiP. Protein Science : a Publication of the Protein Society. PMID 34941000 DOI: 10.1002/pro.4267 |
0.448 |
|
2021 |
Wang W, Liu Q, Liu Q, Hendrickson WA. Conformational equilibria in allosteric control of Hsp70 chaperones. Molecular Cell. PMID 34453889 DOI: 10.1016/j.molcel.2021.07.039 |
0.392 |
|
2021 |
Li H, Hu L, Cuffee C, Mohamed M, Li Q, Liu Q, Zhou L, Liu Q. Interdomain interactions dictate the function of the C. albicans Hsp110 protein Msi3. The Journal of Biological Chemistry. 101082. PMID 34403698 DOI: 10.1016/j.jbc.2021.101082 |
0.415 |
|
2021 |
Wang Y, Li H, Sun C, Liu Q, Zhou L, Liu Q. Purification and biochemical characterization of Msi3, an essential Hsp110 molecular chaperone in Candida albicans. Cell Stress & Chaperones. PMID 34047887 DOI: 10.1007/s12192-021-01213-5 |
0.371 |
|
2019 |
Li H, Zhu H, Sarbeng EB, Liu Q, Tian X, Yang Y, Lyons C, Zhou L, Liu Q. An unexpected second binding site for polypeptide substrates is essential for Hsp70 chaperone activity. The Journal of Biological Chemistry. PMID 31806707 DOI: 10.1074/Jbc.Ra119.009686 |
0.34 |
|
2018 |
Yang J, Zong Y, Su J, Li H, Zhu H, Columbus L, Zhou L, Liu Q. A Novel Conformation of the Polypeptide-Binding Pocket Supports an Active Substrate Release from Hsp70S Biophysical Journal. 114. DOI: 10.1016/J.Bpj.2017.11.3019 |
0.302 |
|
2017 |
Yang J, Zong Y, Su J, Li H, Zhu H, Columbus L, Zhou L, Liu Q. Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s. Nature Communications. 8: 1201. PMID 29084938 DOI: 10.1038/S41467-017-01310-Z |
0.399 |
|
2016 |
Liu Q, Li H, Yang Y, Tian X, Su J, Zhou L, Liu Q. A disulfide-bonded DnaK dimer is maintained in an ATP-bound state. Cell Stress & Chaperones. PMID 27975204 DOI: 10.1007/S12192-016-0752-Y |
0.381 |
|
2016 |
Liu Q, Craig EA. Molecular biology: Mature proteins braced by a chaperone. Nature. PMID 27783595 DOI: 10.1038/nature20470 |
0.491 |
|
2015 |
Yang J, Nune M, Zong Y, Zhou L, Liu Q. Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP. Structure (London, England : 1993). 23: 2191-2203. PMID 26655470 DOI: 10.1016/J.Str.2015.10.012 |
0.392 |
|
2015 |
Sarbeng EB, Liu Q, Tian X, Yang J, Li H, Wong JL, Zhou L, Liu Q. A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock protein. The Journal of Biological Chemistry. 290: 8849-62. PMID 25635056 DOI: 10.1074/Jbc.M114.596288 |
0.426 |
|
2014 |
Liu Q, Qi R, Sarbeng E, Liu Q, Le K, Xu X, Xu H, Yang J, Wong J, Vorvis C, Hendrickson W, Zhou L. Allosteric Opening of the Polypeptide-Binding Site When an Hsp70 Binds ATP Biophysical Journal. 106: 2-7. DOI: 10.1016/J.Bpj.2013.11.1446 |
0.384 |
|
2013 |
Qi R, Sarbeng EB, Liu Q, Le KQ, Xu X, Xu H, Yang J, Wong JL, Vorvis C, Hendrickson WA, Zhou L, Liu Q. Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP. Nature Structural & Molecular Biology. 20: 900-7. PMID 23708608 DOI: 10.1038/Nsmb.2583 |
0.404 |
|
2012 |
Xu X, Marni F, Wu S, Su Z, Musayev F, Shrestha S, Xie C, Gao W, Liu Q, Zhou L. Local and global interpretations of a disease-causing mutation near the ligand entry path in hyperpolarization-activated cAMP-gated channel. Structure (London, England : 1993). 20: 2116-23. PMID 23103389 DOI: 10.1016/J.Str.2012.09.017 |
0.309 |
|
2012 |
Marni F, Wu S, Shah GM, Xu XP, Hackett AR, Xie C, Shrestha S, Liu L, Liu Q, Zhou L. Normal-mode-analysis-guided investigation of crucial intersubunit contacts in the cAMP-dependent gating in HCN channels Biophysical Journal. 103: 19-28. PMID 22828328 DOI: 10.1016/J.Bpj.2012.05.030 |
0.337 |
|
2012 |
Wu S, Gao W, Xie C, Xu X, Vorvis C, Marni F, Hackett AR, Liu Q, Zhou L. Inner activation gate in S6 contributes to the state-dependent binding of cAMP in full-length HCN2 channel. The Journal of General Physiology. 140: 29-39. PMID 22689828 DOI: 10.1085/Jgp.201110749 |
0.325 |
|
2012 |
Xu X, Sarbeng EB, Vorvis C, Kumar DP, Zhou L, Liu Q. Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity. The Journal of Biological Chemistry. 287: 5661-72. PMID 22157767 DOI: 10.1074/Jbc.M111.275057 |
0.344 |
|
2011 |
Xu X, Vysotskaya ZV, Liu Q, Zhou L. Structural and Biochemical Study of CAMP-Dependent Regulation of Human HCN4 Channel Biophysical Journal. 100: 1-4. DOI: 10.1016/J.Bpj.2010.12.778 |
0.316 |
|
2008 |
Schiller D, Cheng YC, Liu Q, Walter W, Craig EA. Residues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tethering. Molecular and Cellular Biology. 28: 4424-33. PMID 18426906 DOI: 10.1128/Mcb.00007-08 |
0.705 |
|
2007 |
Liu Q, Hendrickson WA. Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1 Cell. 131: 106-120. PMID 17923091 DOI: 10.1016/J.Cell.2007.08.039 |
0.337 |
|
2004 |
D'Silva P, Liu Q, Walter W, Craig EA. Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane Nature Structural and Molecular Biology. 11: 1084-1091. PMID 15489862 DOI: 10.1038/Nsmb846 |
0.611 |
|
2003 |
Liu Q, D'Silva P, Walter W, Marszalek J, Craig EA. Regulated cycling of mitochondrial Hsp70 at the protein import channel Science. 300: 139-141. PMID 12677068 DOI: 10.1126/Science.1083379 |
0.609 |
|
2001 |
Liu Q, Krzewska J, Liberek K, Craig EA. Mitochondrial Hsp70 Ssc1: Role in Protein Folding Journal of Biological Chemistry. 276: 6112-6118. PMID 11096111 DOI: 10.1074/Jbc.M009519200 |
0.62 |
|
1999 |
Sakuragi S, Liu Q, Craig E. Interaction between the nucleotide exchange factor Mge1 and the mitochondrial Hsp70 Ssc1. The Journal of Biological Chemistry. 274: 11275-82. PMID 10196216 DOI: 10.1074/Jbc.274.16.11275 |
0.623 |
|
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