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.
113 related articles for article (PubMed ID: 14754890)
1. Identification of the N-terminal peptide binding site of glucose-regulated protein 94. Gidalevitz T; Biswas C; Ding H; Schneidman-Duhovny D; Wolfson HJ; Stevens F; Radford S; Argon Y J Biol Chem; 2004 Apr; 279(16):16543-52. PubMed ID: 14754890 [TBL] [Abstract][Full Text] [Related]
2. Radicicol-sensitive peptide binding to the N-terminal portion of GRP94. Vogen S; Gidalevitz T; Biswas C; Simen BB; Stein E; Gulmen F; Argon Y J Biol Chem; 2002 Oct; 277(43):40742-50. PubMed ID: 12189140 [TBL] [Abstract][Full Text] [Related]
3. Structural transitions accompanying the activation of peptide binding to the endoplasmic reticulum Hsp90 chaperone GRP94. Wearsch PA; Voglino L; Nicchitta CV Biochemistry; 1998 Apr; 37(16):5709-19. PubMed ID: 9548957 [TBL] [Abstract][Full Text] [Related]
4. Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94. II. Ligand-mediated activation of GRP94 molecular chaperone and peptide binding activity. Wassenberg JJ; Reed RC; Nicchitta CV J Biol Chem; 2000 Jul; 275(30):22806-14. PubMed ID: 10816560 [TBL] [Abstract][Full Text] [Related]
5. Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones. Schulte TW; Akinaga S; Murakata T; Agatsuma T; Sugimoto S; Nakano H; Lee YS; Simen BB; Argon Y; Felts S; Toft DO; Neckers LM; Sharma SV Mol Endocrinol; 1999 Sep; 13(9):1435-48. PubMed ID: 10478836 [TBL] [Abstract][Full Text] [Related]
6. Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation. Soldano KL; Jivan A; Nicchitta CV; Gewirth DT J Biol Chem; 2003 Nov; 278(48):48330-8. PubMed ID: 12970348 [TBL] [Abstract][Full Text] [Related]
7. 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]
8. Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design. Immormino RM; Metzger LE; Reardon PN; Dollins DE; Blagg BS; Gewirth DT J Mol Biol; 2009 May; 388(5):1033-42. PubMed ID: 19361515 [TBL] [Abstract][Full Text] [Related]
9. Adenosine nucleotides and the regulation of GRP94-client protein interactions. Rosser MF; Trotta BM; Marshall MR; Berwin B; Nicchitta CV Biochemistry; 2004 Jul; 43(27):8835-45. PubMed ID: 15236592 [TBL] [Abstract][Full Text] [Related]
10. Ligand recognition by the TPR domain of the import factor Toc64 from Arabidopsis thaliana. Panigrahi R; Adina-Zada A; Whelan J; Vrielink A PLoS One; 2013; 8(12):e83461. PubMed ID: 24391770 [TBL] [Abstract][Full Text] [Related]
11. 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]
12. Dimerization characteristics of the 94-kDa glucose-regulated protein. Nemoto T; Matsusaka T; Ota M; Takagi T; Collinge DB; Walther-Larsen H J Biochem; 1996 Aug; 120(2):249-56. PubMed ID: 8889807 [TBL] [Abstract][Full Text] [Related]