Year |
Citation |
Score |
2018 |
Wang P, Li J, Tao J, Sha B. The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization. The Journal of Biological Chemistry. PMID 29386355 DOI: 10.1074/Jbc.Ra117.001294 |
0.7 |
|
2017 |
Wang P, Li J, Weaver C, Lucius A, Sha B. Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions. Acta Crystallographica. Section D, Structural Biology. 73: 365-372. PMID 28375147 DOI: 10.1107/S2059798317002662 |
0.717 |
|
2016 |
Wang P, Li J, Sha B. The ER stress sensor PERK luminal domain functions as a molecular chaperone to interact with misfolded proteins. Acta Crystallographica. Section D, Structural Biology. 72: 1290-1297. PMID 27917829 DOI: 10.1107/S2059798316018064 |
0.668 |
|
2015 |
Li J, Sha B. The structure of Tim50(164-361) suggests the mechanism by which Tim50 receives mitochondrial presequences. Acta Crystallographica. Section F, Structural Biology Communications. 71: 1146-51. PMID 26323300 DOI: 10.1107/S2053230X15013102 |
0.689 |
|
2012 |
Sun J, Li J, Cheng G, Sha B, Zhou W. Effects of hypothermia on NSE and S-100 protein levels in CSF in neonates following hypoxic/ischaemic brain damage. Acta Paediatrica (Oslo, Norway : 1992). 101: e316-20. PMID 22452413 DOI: 10.1111/j.1651-2227.2012.02679.x |
0.505 |
|
2011 |
Qian X, Gebert M, Höpker J, Yan M, Li J, Wiedemann N, van der Laan M, Pfanner N, Sha B. Structural basis for the function of Tim50 in the mitochondrial presequence translocase. Journal of Molecular Biology. 411: 513-9. PMID 21704637 DOI: 10.1016/J.Jmb.2011.06.020 |
0.602 |
|
2011 |
Yan M, Li J, Sha B. Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor. The Biochemical Journal. 438: 447-55. PMID 21675960 DOI: 10.1042/Bj20110500 |
0.686 |
|
2011 |
Cui W, Li J, Ron D, Sha B. The structure of the PERK kinase domain suggests the mechanism for its activation. Acta Crystallographica. Section D, Biological Crystallography. 67: 423-8. PMID 21543844 DOI: 10.1107/S0907444911006445 |
0.631 |
|
2011 |
Zheng Y, Qin H, Frank SJ, Deng L, Litchfield DW, Tefferi A, Pardanani A, Lin FT, Li J, Sha B, Benveniste EN. A CK2-dependent mechanism for activation of the JAK-STAT signaling pathway. Blood. 118: 156-66. PMID 21527517 DOI: 10.1182/Blood-2010-01-266320 |
0.509 |
|
2011 |
Cui W, Josyula R, Li J, Fu Z, Sha B. Membrane binding mechanism of yeast mitochondrial peripheral membrane protein TIM44. Protein and Peptide Letters. 18: 718-25. PMID 21342097 DOI: 10.2174/092986611795445996 |
0.578 |
|
2011 |
Tao J, Sha B. Structural insight into the protective role of P58(IPK) during unfolded protein response. Methods in Enzymology. 490: 259-70. PMID 21266255 DOI: 10.1016/B978-0-12-385114-7.00015-5 |
0.38 |
|
2010 |
Li J, Cui W, Sha B. The structural plasticity of Tom71 for mitochondrial precursor translocations. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 66: 985-9. PMID 20823510 DOI: 10.1107/S1744309110025522 |
0.696 |
|
2010 |
Zhao LJ, Liu XG, Liu YZ, Liu YJ, Papasian CJ, Sha BY, Pan F, Guo YF, Wang L, Yan H, Xiong DH, Tang ZH, Yang TL, Chen XD, Guo Y, et al. Genome-wide association study for femoral neck bone geometry. Journal of Bone and Mineral Research : the Official Journal of the American Society For Bone and Mineral Research. 25: 320-9. PMID 20175129 DOI: 10.1359/Jbmr.090726 |
0.498 |
|
2010 |
Wen H, Li J, Song T, Lu M, Kan PY, Lee MG, Sha B, Shi X. Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation. The Journal of Biological Chemistry. 285: 9322-6. PMID 20129925 DOI: 10.1074/Jbc.C109.097667 |
0.554 |
|
2009 |
Hu J, Li J, Qian X, Denic V, Sha B. The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion. Plos One. 4: e8061. PMID 19956640 DOI: 10.1371/Journal.Pone.0008061 |
0.7 |
|
2009 |
Li J, Qian X, Hu J, Sha B. Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading. The Journal of Biological Chemistry. 284: 23852-9. PMID 19581297 DOI: 10.1074/Jbc.M109.023986 |
0.69 |
|
2009 |
Li J, Qian X, Sha B. Heat shock protein 40: structural studies and their functional implications. Protein and Peptide Letters. 16: 606-12. PMID 19519518 DOI: 10.2174/092986609788490159 |
0.64 |
|
2009 |
Hu J, Li J, Qian X, Jin Z, Fu Z, Sha B. Preliminary X-ray crystallographic studies of yeast Get3. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 65: 489-91. PMID 19407384 DOI: 10.1107/S1744309109012317 |
0.659 |
|
2008 |
Hu J, Wu Y, Li J, Qian X, Fu Z, Sha B. The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1. Bmc Structural Biology. 8: 3. PMID 18211704 DOI: 10.1186/1472-6807-8-3 |
0.718 |
|
2006 |
Li J, Wu Y, Qian X, Sha B. Crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex. The Biochemical Journal. 398: 353-60. PMID 16737444 DOI: 10.1042/Bj20060618 |
0.701 |
|
2005 |
Wu Y, Li J, Jin Z, Fu Z, Sha B. The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40. Journal of Molecular Biology. 346: 1005-11. PMID 15701512 DOI: 10.1016/J.Jmb.2004.12.040 |
0.683 |
|
2005 |
Li J, Sha B. Structure-based mutagenesis studies of the peptide substrate binding fragment of type I heat-shock protein 40. The Biochemical Journal. 386: 453-60. PMID 15500443 DOI: 10.1042/Bj20041050 |
0.696 |
|
2004 |
Li J, Sha B. Peptide substrate identification for yeast Hsp40 Ydj1 by screening the phage display library. Biological Procedures Online. 6: 204-208. PMID 15472720 DOI: 10.1251/Bpo90 |
0.576 |
|
2003 |
Li J, Qian X, Sha B. The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Structure (London, England : 1993). 11: 1475-83. PMID 14656432 DOI: 10.1016/J.Str.2003.10.012 |
0.681 |
|
2003 |
Li J, Sha B. Preliminary X-ray crystallographic studies of yeast Hsp40 Ydj1 complexed with its peptide substrate. Acta Crystallographica. Section D, Biological Crystallography. 59: 1317-9. PMID 12832798 DOI: 10.1107/S0907444903010485 |
0.656 |
|
2003 |
Li J, Sha B. Crystal structure of the E. coli Hsp100 ClpB N-terminal domain. Structure (London, England : 1993). 11: 323-8. PMID 12623019 DOI: 10.1016/S0969-2126(03)00030-3 |
0.687 |
|
2002 |
Li J, Sha B. Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity. Journal of Molecular Biology. 318: 1127-37. PMID 12054807 DOI: 10.1016/S0022-2836(02)00188-2 |
0.706 |
|
2002 |
Li J, Sha B. Cloning, expression, purification and preliminary X-ray crystallographic studies of Escherichia coli Hsp100 nucleotide-binding domain 2 (NBD2). Acta Crystallographica. Section D, Biological Crystallography. 58: 1030-1. PMID 12037306 DOI: 10.1107/S0907444902006327 |
0.692 |
|
2001 |
Li J, Sha B. Cloning, expression, purification and preliminary X-ray crystallographic studies of Escherichia coli Hsp100 ClpB N-terminal domain. Acta Crystallographica. Section D, Biological Crystallography. 57: 1933-5. PMID 11717522 DOI: 10.1107/S0907444901017322 |
0.704 |
|
2001 |
Li J, Sha B. Cloning, expression, purification and preliminary X-ray crystallographic studies of Escherichia coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1). Acta Crystallographica. Section D, Biological Crystallography. 57: 909-11. PMID 11375526 DOI: 10.1107/S0907444901007296 |
0.715 |
|
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