These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
244 related articles for article (PubMed ID: 22223641)
1. The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domain. Wu S; Hong F; Gewirth D; Guo B; Liu B; Li Z J Biol Chem; 2012 Feb; 287(9):6735-42. PubMed ID: 22223641 [TBL] [Abstract][Full Text] [Related]
2. Drosophila glycoprotein 93 Is an ortholog of mammalian heat shock protein gp96 (grp94, HSP90b1, HSPC4) and retains disulfide bond-independent chaperone function for TLRs and integrins. Morales C; Wu S; Yang Y; Hao B; Li Z J Immunol; 2009 Oct; 183(8):5121-8. PubMed ID: 19786553 [TBL] [Abstract][Full Text] [Related]
3. gp96, an endoplasmic reticulum master chaperone for integrins and Toll-like receptors, selectively regulates early T and B lymphopoiesis. Staron M; Yang Y; Liu B; Li J; Shen Y; Zúñiga-Pflücker JC; Aguila HL; Goldschneider I; Li Z Blood; 2010 Mar; 115(12):2380-90. PubMed ID: 19965672 [TBL] [Abstract][Full Text] [Related]
4. Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone. Liu B; Yang Y; Qiu Z; Staron M; Hong F; Li Y; Wu S; Li Y; Hao B; Bona R; Han D; Li Z Nat Commun; 2010 Sep; 1(6):79. PubMed ID: 20865800 [TBL] [Abstract][Full Text] [Related]
5. Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin. Liu B; Li Z Blood; 2008 Aug; 112(4):1223-30. PubMed ID: 18509083 [TBL] [Abstract][Full Text] [Related]
6. GRP94/gp96 in Cancer: Biology, Structure, Immunology, and Drug Development. Wu BX; Hong F; Zhang Y; Ansa-Addo E; Li Z Adv Cancer Res; 2016; 129():165-90. PubMed ID: 26916005 [TBL] [Abstract][Full Text] [Related]
7. Mapping the Interactome of a Major Mammalian Endoplasmic Reticulum Heat Shock Protein 90. Hong F; Mohammad Rachidi S; Lundgren D; Han D; Huang X; Zhao H; Kimura Y; Hirano H; Ohara O; Udono H; Meng S; Liu B; Li Z PLoS One; 2017; 12(1):e0169260. PubMed ID: 28056051 [TBL] [Abstract][Full Text] [Related]
8. α7 helix region of αI domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: a potential therapeutic target for cancer metastasis. Hong F; Liu B; Chiosis G; Gewirth DT; Li Z J Biol Chem; 2013 Jun; 288(25):18243-8. PubMed ID: 23671277 [TBL] [Abstract][Full Text] [Related]
9. Morales C; Li Z J Biol Chem; 2017 Apr; 292(16):6657-6666. PubMed ID: 28275054 [No Abstract] [Full Text] [Related]
11. A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone. Yamada S; Ono T; Mizuno A; Nemoto TK Eur J Biochem; 2003 Jan; 270(1):146-54. PubMed ID: 12492485 [TBL] [Abstract][Full Text] [Related]
12. Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94. Chu F; Maynard JC; Chiosis G; Nicchitta CV; Burlingame AL Protein Sci; 2006 Jun; 15(6):1260-9. PubMed ID: 16731965 [TBL] [Abstract][Full Text] [Related]
13. Endoplasmic reticulum chaperone gp96 is essential for infection with vesicular stomatitis virus. Bloor S; Maelfait J; Krumbach R; Beyaert R; Randow F Proc Natl Acad Sci U S A; 2010 Apr; 107(15):6970-5. PubMed ID: 20351288 [TBL] [Abstract][Full Text] [Related]
14. Murine but not human basophil undergoes cell-specific proteolysis of a major endoplasmic reticulum chaperone. Liu B; Staron M; Li Z PLoS One; 2012; 7(6):e39442. PubMed ID: 22724016 [TBL] [Abstract][Full Text] [Related]
16. The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains. Prodromou C; Panaretou B; Chohan S; Siligardi G; O'Brien R; Ladbury JE; Roe SM; Piper PW; Pearl LH EMBO J; 2000 Aug; 19(16):4383-92. PubMed ID: 10944121 [TBL] [Abstract][Full Text] [Related]
17. Biophysical analysis of the endoplasmic reticulum-resident chaperone/heat shock protein gp96/GRP94 and its complex with peptide antigen. Linderoth NA; Simon MN; Rodionova NA; Cadene M; Laws WR; Chait BT; Sastry S Biochemistry; 2001 Feb; 40(5):1483-95. PubMed ID: 11170476 [TBL] [Abstract][Full Text] [Related]
18. Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages. Yang Y; Liu B; Dai J; Srivastava PK; Zammit DJ; Lefrançois L; Li Z Immunity; 2007 Feb; 26(2):215-26. PubMed ID: 17275357 [TBL] [Abstract][Full Text] [Related]
19. Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity. Street TO; Lavery LA; Verba KA; Lee CT; Mayer MP; Agard DA J Mol Biol; 2012 Jan; 415(1):3-15. PubMed ID: 22063096 [TBL] [Abstract][Full Text] [Related]
20. Endoplasmic reticulum chaperone gp96 in macrophages is essential for protective immunity during Gram-negative pneumonia. Anas AA; de Vos AF; Hoogendijk AJ; van Lieshout MH; van Heijst JW; Florquin S; Li Z; van 't Veer C; van der Poll T J Pathol; 2016 Jan; 238(1):74-84. PubMed ID: 26365983 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]