Detalhe da pesquisa
1.
Structural transitions modulate the chaperone activities of Grp94.
Proc Natl Acad Sci U S A
; 121(12): e2309326121, 2024 Mar 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-38483986
2.
NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90.
J Biol Chem
; 294(44): 16010-16019, 2019 11 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-31501246
3.
Chaperome heterogeneity and its implications for cancer study and treatment.
J Biol Chem
; 294(6): 2162-2179, 2019 02 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-30409908
4.
Structures of Hsp90α and Hsp90ß bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity.
Proteins
; 87(10): 869-877, 2019 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-31141217
5.
Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2.
Nat Chem Biol
; 9(11): 677-84, 2013 Nov.
Artigo
em Inglês
| MEDLINE | ID: mdl-23995768
6.
α7 helix region of αI domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: a potential therapeutic target for cancer metastasis.
J Biol Chem
; 288(25): 18243-8, 2013 Jun 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-23671277
7.
Selective inhibition of hsp90 paralogs: Structure and binding studies uncover the role of helix 1 in Grp94-selective ligand binding.
bioRxiv
; 2023 Aug 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-37577523
8.
Selective targeting of GARP-LTGFß axis in the tumor microenvironment augments PD-1 blockade via enhancing CD8+ T cell antitumor immunity.
J Immunother Cancer
; 10(9)2022 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-36096533
9.
Thrombin contributes to cancer immune evasion via proteolysis of platelet-bound GARP to activate LTGF-ß.
Sci Transl Med
; 12(525)2020 01 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-31915300
10.
Molecular Stressors Engender Protein Connectivity Dysfunction through Aberrant N-Glycosylation of a Chaperone.
Cell Rep
; 31(13): 107840, 2020 06 30.
Artigo
em Inglês
| MEDLINE | ID: mdl-32610141
11.
Potential impact of combined inhibition of 3α-oxidoreductases and 5α-reductases on prostate cancer.
Asian J Urol
; 6(1): 50-56, 2019 Jan.
Artigo
em Inglês
| MEDLINE | ID: mdl-30775248
12.
Second international symposium on the chaperone code, 2023.
Cell Stress Chaperones
; 29(1): 88-96, 2024 Feb.
Artigo
em Inglês
| MEDLINE | ID: mdl-38316354
13.
Structure Based Design of a Grp94-Selective Inhibitor: Exploiting a Key Residue in Grp94 To Optimize Paralog-Selective Binding.
J Med Chem
; 61(7): 2793-2805, 2018 04 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-29528635
14.
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.
Cell Rep
; 20(12): 2800-2809, 2017 Sep 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-28930677
15.
Bypassing Drug Resistance Mechanisms of Prostate Cancer with Small Molecules that Target Androgen Receptor-Chromatin Interactions.
Mol Cancer Ther
; 16(10): 2281-2291, 2017 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-28775145
16.
Structural and quantum chemical studies of 8-aryl-sulfanyl adenine class Hsp90 inhibitors.
J Med Chem
; 49(16): 4953-60, 2006 Aug 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-16884307
17.
Identification of potent water soluble purine-scaffold inhibitors of the heat shock protein 90.
J Med Chem
; 49(1): 381-90, 2006 Jan 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-16392823
18.
Paralog Specific Hsp90 Inhibitors - A Brief History and a Bright Future.
Curr Top Med Chem
; 16(25): 2779-91, 2016.
Artigo
em Inglês
| MEDLINE | ID: mdl-27072700
19.
Exploring the Functional Complementation between Grp94 and Hsp90.
PLoS One
; 11(11): e0166271, 2016.
Artigo
em Inglês
| MEDLINE | ID: mdl-27824935
20.
Clients and Oncogenic Roles of Molecular Chaperone gp96/grp94.
Curr Top Med Chem
; 16(25): 2765-78, 2016.
Artigo
em Inglês
| MEDLINE | ID: mdl-27072698