Year |
Citation |
Score |
2019 |
Clerico EM, Meng W, Pozhidaeva A, Bhasne K, Petridis C, Gierasch LM. Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines. The Biochemical Journal. 476: 1653-1677. PMID 31201219 DOI: 10.1042/Bcj20170380 |
0.343 |
|
2018 |
Meng W, Clerico EM, McArthur N, Gierasch LM. Allosteric landscapes of eukaryotic cytoplasmic Hsp70s are shaped by evolutionary tuning of key interfaces. Proceedings of the National Academy of Sciences of the United States of America. 115: 11970-11975. PMID 30397123 DOI: 10.1073/Pnas.1811105115 |
0.323 |
|
2018 |
Thakur AK, Meng W, Gierasch LM. Local and non-local topological information in the denatured state ensemble of a β-barrel protein. Protein Science : a Publication of the Protein Society. PMID 30252171 DOI: 10.1002/Pro.3516 |
0.507 |
|
2017 |
English CA, Sherman W, Meng W, Gierasch LM. The Hsp70 interdomain linker is a dynamic switch that enables allosteric communication between two structured domains. The Journal of Biological Chemistry. PMID 28754691 DOI: 10.1074/Jbc.M117.789313 |
0.34 |
|
2015 |
Clerico EM, Tilitsky JM, Meng W, Gierasch LM. How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions. Journal of Molecular Biology. 427: 1575-88. PMID 25683596 DOI: 10.1016/J.Jmb.2015.02.004 |
0.345 |
|
2014 |
Cho JH, Meng W, Sato S, Kim EY, Schindelin H, Raleigh DP. Energetically significant networks of coupled interactions within an unfolded protein. Proceedings of the National Academy of Sciences of the United States of America. 111: 12079-84. PMID 25099351 DOI: 10.1073/Pnas.1402054111 |
0.717 |
|
2013 |
Meng W, Luan B, Lyle N, Pappu RV, Raleigh DP. The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9. Biochemistry. 52: 2662-71. PMID 23480024 DOI: 10.1021/Bi301667U |
0.755 |
|
2013 |
Meng W, Lyle N, Luan B, Raleigh DP, Pappu RV. Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure. Proceedings of the National Academy of Sciences of the United States of America. 110: 2123-8. PMID 23341588 DOI: 10.1073/Pnas.1216979110 |
0.703 |
|
2012 |
Lyle NJ, Meng W, Raleigh DP, Pappu RV. Simulations of Denatured Protein Ensembles Reproduce and Rationalize Experimental Observations of Persistent Contacts Between Residues Distal in Protein Sequence Biophysical Journal. 102: 630a. DOI: 10.1016/J.Bpj.2011.11.3433 |
0.679 |
|
2011 |
Meng W, Raleigh DP. Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions. Proteins. 79: 3500-10. PMID 21915914 DOI: 10.1002/Prot.23145 |
0.671 |
|
2011 |
Mi D, Meng WQ, Sun YQ. Unifying model for two-state and downhill protein folding. Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics. 83: 041901. PMID 21599197 DOI: 10.1103/PHYSREVE.83.041901 |
0.395 |
|
2011 |
Meng W, Raleigh D. Backbone 1H,15N,13C and 13CB chemical shifts of folded state and denatured state for the N-terminal domain of ribosomal protein L9 (NTL9) V3AI4A double mutant Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr17675 |
0.672 |
|
2009 |
Meng W, Shan B, Tang Y, Raleigh DP. Native like structure in the unfolded state of the villin headpiece helical subdomain, an ultrafast folding protein. Protein Science : a Publication of the Protein Society. 18: 1692-701. PMID 19598233 DOI: 10.1002/Pro.152 |
0.711 |
|
2009 |
Raleigh DP, Shan B, Meng W, Cho J, Taskent H. Characterization of the Unfolded State Under Native Conditions: A Missing Piece of the Protein Folding Puzzle Biophysical Journal. 96: 220a. DOI: 10.1016/J.Bpj.2008.12.1921 |
0.725 |
|
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