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.
206 related articles for article (PubMed ID: 31501246)
1. NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90. Huck JD; Que NLS; Immormino RM; Shrestha L; Taldone T; Chiosis G; Gewirth DT J Biol Chem; 2019 Nov; 294(44):16010-16019. PubMed ID: 31501246 [TBL] [Abstract][Full Text] [Related]
2. 5'-N-ethylcarboxamidoadenosine is not a paralog-specific Hsp90 inhibitor. Liu S; Street TO Protein Sci; 2016 Dec; 25(12):2209-2215. PubMed ID: 27667530 [TBL] [Abstract][Full Text] [Related]
3. Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94. I. Evidence for allosteric regulation of ligand binding. Rosser MF; Nicchitta CV J Biol Chem; 2000 Jul; 275(30):22798-805. PubMed ID: 10816561 [TBL] [Abstract][Full Text] [Related]
4. Selective inhibition of hsp90 paralogs: Uncovering the role of helix 1 in Grp94-selective ligand binding. Que NLS; Seidler PM; Aw WJ; Chiosis G; Gewirth DT bioRxiv; 2024 Aug; ():. PubMed ID: 37577523 [TBL] [Abstract][Full Text] [Related]
5. 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]
6. Structure-activity relationship in a purine-scaffold compound series with selectivity for the endoplasmic reticulum Hsp90 paralog Grp94. Patel HJ; Patel PD; Ochiana SO; Yan P; Sun W; Patel MR; Shah SK; Tramentozzi E; Brooks J; Bolaender A; Shrestha L; Stephani R; Finotti P; Leifer C; Li Z; Gewirth DT; Taldone T; Chiosis G J Med Chem; 2015 May; 58(9):3922-43. PubMed ID: 25901531 [TBL] [Abstract][Full Text] [Related]
7. Structure Based Design of a Grp94-Selective Inhibitor: Exploiting a Key Residue in Grp94 To Optimize Paralog-Selective Binding. Que NLS; Crowley VM; Duerfeldt AS; Zhao J; Kent CN; Blagg BSJ; Gewirth DT J Med Chem; 2018 Apr; 61(7):2793-2805. PubMed ID: 29528635 [TBL] [Abstract][Full Text] [Related]
8. Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site. Huck JD; Que NL; Hong F; Li Z; Gewirth DT Cell Rep; 2017 Sep; 20(12):2800-2809. PubMed ID: 28930677 [TBL] [Abstract][Full Text] [Related]
10. Investigation of the site 2 pocket of Grp94 with KUNG65 benzamide derivatives. Pugh K; Xu H; Blagg BSJ Bioorg Med Chem Lett; 2024 Oct; 111():129893. PubMed ID: 39043265 [TBL] [Abstract][Full Text] [Related]
11. The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation. Sun M; Kotler JLM; Liu S; Street TO J Biol Chem; 2019 Apr; 294(16):6387-6396. PubMed ID: 30787103 [TBL] [Abstract][Full Text] [Related]
12. 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]
13. Biological Evaluation of 5'-( Tosh DK; Brackett CM; Jung YH; Gao ZG; Banerjee M; Blagg BSJ; Jacobson KA ACS Med Chem Lett; 2021 Mar; 12(3):373-379. PubMed ID: 33738064 [TBL] [Abstract][Full Text] [Related]
14. 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]
15. Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2. Patel PD; Yan P; Seidler PM; Patel HJ; Sun W; Yang C; Que NS; Taldone T; Finotti P; Stephani RA; Gewirth DT; Chiosis G Nat Chem Biol; 2013 Nov; 9(11):677-84. PubMed ID: 23995768 [TBL] [Abstract][Full Text] [Related]
16. Transformation of the Non-Selective Aminocyclohexanol-Based Hsp90 Inhibitor into a Grp94-Seletive Scaffold. Mishra SJ; Ghosh S; Stothert AR; Dickey CA; Blagg BS ACS Chem Biol; 2017 Jan; 12(1):244-253. PubMed ID: 27959508 [TBL] [Abstract][Full Text] [Related]
18. Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone. Immormino RM; Dollins DE; Shaffer PL; Soldano KL; Walker MA; Gewirth DT J Biol Chem; 2004 Oct; 279(44):46162-71. PubMed ID: 15292259 [TBL] [Abstract][Full Text] [Related]
19. The endoplasmic reticulum chaperone BiP is a closure-accelerating cochaperone of Grp94. Huang B; Sun M; Hoxie R; Kotler JLM; Friedman LJ; Gelles J; Street TO Proc Natl Acad Sci U S A; 2022 Feb; 119(5):. PubMed ID: 35078937 [TBL] [Abstract][Full Text] [Related]
20. Conformational Cycling within the Closed State of Grp94, an Hsp90-Family Chaperone. Huang B; Friedman LJ; Sun M; Gelles J; Street TO J Mol Biol; 2019 Aug; 431(17):3312-3323. PubMed ID: 31202885 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]