Year |
Citation |
Score |
2023 |
Meissner JM, Akhmetova K, Szul T, Viktorova EG, Sha B, Bhatt JM, Lee EJ, Kahn RA, Belov GA, Chesnokov I, Sztul E. The Arf-GEF GBF1 undergoes multi-domain structural shifts to activate Arf at the Golgi. Frontiers in Cell and Developmental Biology. 11: 1233272. PMID 37745300 DOI: 10.3389/fcell.2023.1233272 |
0.324 |
|
2023 |
Seo HS, Yu D, Popov I, Tao J, Angermeier A, Sha B, Axelrod J, Chang C, Wang J. Prickle and Ror modulate Dishevelled-Vangl interaction to regulate non-canonical Wnt signaling during convergent extension. Biorxiv : the Preprint Server For Biology. PMID 37693429 DOI: 10.1101/2023.08.29.555374 |
0.725 |
|
2020 |
Yang W, Gibson SA, Yan Z, Wei H, Tao J, Sha B, Qin H, Benveniste EN. Protein kinase 2 (CK2) controls CD4 T cell effector function in the pathogenesis of colitis. Mucosal Immunology. PMID 31988467 DOI: 10.1038/s41385-020-0258-x |
0.69 |
|
2020 |
Zhang F, Gannon M, Chen Y, Yan S, Zhang S, Feng W, Tao J, Sha B, Liu Z, Saito T, Saido T, Keene CD, Jiao K, Roberson ED, Xu H, et al. β-amyloid redirects norepinephrine signaling to activate the pathogenic GSK3β/tau cascade. Science Translational Medicine. 12. PMID 31941827 DOI: 10.1126/Scitranslmed.Aay6931 |
0.707 |
|
2019 |
Chen S, Henderson A, Petriello M, Romano KA, Gearing M, Miao J, Schell M, Sandoval-EspinolaEspinola WJ, Tao J, Sha B, Graham M, Crooke R, Kleinridders A, Balskus EP, Rey FE, et al. Trimethylamine N-Oxide Binds and Activates PERK to Promote Metabolic Dysfunction. Cell Metabolism. PMID 31543404 DOI: 10.1016/J.Cmet.2019.08.021 |
0.721 |
|
2019 |
Zheng Z, Shang Y, Tao J, Zhang J, Sha B. Endoplasmic Reticulum Stress Signaling Pathways: Activation and Diseases. Current Protein & Peptide Science. PMID 31223084 DOI: 10.2174/1389203720666190621103145 |
0.748 |
|
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 |
0.789 |
|
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 |
0.347 |
|
2017 |
Wang P, Li J, Sha B. Preliminary X-Ray Crystallographic Studies of the N-Terminal Domains of Hsp104 from Yeast Candida albicans and Saccharomyces cerevisiae Crystallography Reports. 62: 1171-1176. DOI: 10.1134/S1063774517070331 |
0.472 |
|
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 |
0.388 |
|
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 |
0.521 |
|
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 |
0.472 |
|
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 |
0.446 |
|
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 |
0.633 |
|
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 |
0.754 |
|
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 |
0.785 |
|
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 |
0.666 |
|
2010 |
Tao J, Petrova K, Ron D, Sha B. Crystal structure of P58(IPK) TPR fragment reveals the mechanism for its molecular chaperone activity in UPR. Journal of Molecular Biology. 397: 1307-15. PMID 20184891 DOI: 10.1016/J.Jmb.2010.02.028 |
0.786 |
|
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 |
0.673 |
|
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 |
0.644 |
|
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 |
0.413 |
|
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 |
0.674 |
|
2008 |
Tao J, Wu Y, Ron D, Sha B. Preliminary X-ray crystallographic studies of mouse UPR responsive protein P58(IPK) TPR fragment. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 64: 108-10. PMID 18259061 DOI: 10.1107/S1744309108000833 |
0.792 |
|
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 |
0.717 |
|
2006 |
Wu Y, Sha B. Crystal structure of yeast mitochondrial outer membrane translocon member Tom70p. Nature Structural & Molecular Biology. 13: 589-93. PMID 16767096 DOI: 10.1038/Nsmb1106 |
0.693 |
|
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 |
0.634 |
|
2006 |
Josyula R, Jin Z, Fu Z, Sha B. Crystal structure of yeast mitochondrial peripheral membrane protein Tim44p C-terminal domain. Journal of Molecular Biology. 359: 798-804. PMID 16647716 DOI: 10.1016/J.Jmb.2006.04.020 |
0.791 |
|
2006 |
Wu Y, McCombs D, Nagy L, DeLucas L, Sha B. Preliminary X-ray crystallographic studies of yeast mitochondrial protein Tom70p. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 62: 265-7. PMID 16511318 DOI: 10.1107/S1744309106004702 |
0.664 |
|
2006 |
Josyula R, Jin Z, McCombs D, DeLucas L, Sha B. Preliminary crystallographic studies of yeast mitochondrial peripheral membrane protein Tim44p. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 62: 172-4. PMID 16511294 DOI: 10.1107/S1744309106002053 |
0.779 |
|
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 |
0.626 |
|
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 |
0.458 |
|
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 |
0.397 |
|
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 |
0.399 |
|
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 |
0.439 |
|
2002 |
Li S, Finley J, Liu ZJ, Qiu SH, Chen H, Luan CH, Carson M, Tsao J, Johnson D, Lin G, Zhao J, Thomas W, Nagy LA, Sha B, DeLucas LJ, et al. Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain. The Journal of Biological Chemistry. 277: 48596-601. PMID 12221106 DOI: 10.1074/Jbc.M208512200 |
0.474 |
|
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 |
0.487 |
|
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 |
0.458 |
|
2002 |
Qian X, Hou W, Zhengang L, Sha B. Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1. The Biochemical Journal. 361: 27-34. PMID 11743879 DOI: 10.1042/Bj3610027 |
0.437 |
|
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 |
0.468 |
|
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 |
0.475 |
|
2001 |
Qian X, Li Z, Sha B. Cloning, expression, purification and preliminary X-ray crystallographic studies of yeast Hsp40 Sis1 complexed with Hsp70 Ssa1 C-terminal lid domain Acta Crystallographica Section D: Biological Crystallography. 57: 748-750. PMID 11320326 DOI: 10.1107/S0907444901004863 |
0.457 |
|
2000 |
Sha B, Lee S, Cyr DM. The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1 Structure. 8: 799-807. PMID 10997899 DOI: 10.1016/S0969-2126(00)00170-2 |
0.449 |
|
1999 |
Sha B, Luo M. PI transfer protein: The specific recognition of phospholipids and its functions Biochimica Et Biophysica Acta - Molecular and Cell Biology of Lipids. 1441: 268-277. PMID 10570254 DOI: 10.1016/S1388-1981(99)00162-6 |
0.417 |
|
1999 |
Phillips SE, Sha B, Topalof L, Xie Z, Alb JG, Klenchin VA, Swigart P, Cockcroft S, Martin TFJ, Luo M, Bankaitis VA. Yeast Sec14p deficient in phosphatidylinositol transfer activity is functional in vivo Molecular Cell. 4: 187-197. PMID 10488334 DOI: 10.1016/S1097-2765(00)80366-4 |
0.353 |
|
1999 |
Sha B, Cyr D. Purification, crystallization and preliminary X-ray crystallographic studies of S. cerevisiae Hsp40 Sis1 Acta Crystallographica Section D: Biological Crystallography. 55: 1234-1236. PMID 10329795 DOI: 10.1107/S090744499900476X |
0.447 |
|
1999 |
Harris A, Sha B, Luo M. Structural similarities between influenza virus matrix protein M1 and human immunodeficiency virus matrix and capsid proteins: An evolutionary link between negative-stranded RNA viruses and retroviruses Journal of General Virology. 80: 863-869. PMID 10211954 DOI: 10.1099/0022-1317-80-4-863 |
0.364 |
|
1998 |
Sha B, Phillips SE, Bankaitis VA, Luo M. Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol- transfer protein Nature. 391: 506-510. PMID 9461221 DOI: 10.1038/35179 |
0.5 |
|
1997 |
Sha B, Phillips SE, Bankaitis VA, Luo M. Crystallization and preliminary X-ray diffraction studies of the Saccharomyces cerevisiae phospholipid-transfer protein Sec14p. Acta Crystallographica. Section D, Biological Crystallography. 53: 784-6. PMID 15299870 DOI: 10.1107/S0907444997006872 |
0.415 |
|
1997 |
Sha B, Luo M. Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1 Nature Structural Biology. 4: 239-244. PMID 9164466 DOI: 10.1038/Nsb0397-239 |
0.391 |
|
1997 |
Sha B, Luo M. Crystallization and preliminary X-ray crystallographic studies of type A influenza virus matrix protein M1 Acta Crystallographica Section D: Biological Crystallography. 53: 458-460. DOI: 10.1107/S0907444997000152 |
0.357 |
|
Show low-probability matches. |