Detalhe da pesquisa
1.
The endoplasmic reticulum chaperone BiP is a closure-accelerating cochaperone of Grp94.
Proc Natl Acad Sci U S A;
119(5)2022 02 01.
Artigo
em Inglês
| MEDLINE
| ID: mdl-35078937
2.
The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation.
J Biol Chem;
294(16): 6387-6396, 2019 04 19.
Artigo
em Inglês
| MEDLINE
| ID: mdl-30787103
3.
Mechanisms of Protein Quality Control in the Endoplasmic Reticulum by a Coordinated Hsp40-Hsp70-Hsp90 System.
Annu Rev Biophys;
52: 509-524, 2023 05 09.
Artigo
em Inglês
| MEDLINE
| ID: mdl-37159299
4.
Electrostatics Drive the Molecular Chaperone BiP to Preferentially Bind Oligomerized States of a Client Protein.
J Mol Biol;
434(13): 167638, 2022 07 15.
Artigo
em Inglês
| MEDLINE
| ID: mdl-35597552
5.
The ER Chaperones BiP and Grp94 Regulate the Formation of Insulin-Like Growth Factor 2 (IGF2) Oligomers.
J Mol Biol;
433(13): 166963, 2021 06 25.
Artigo
em Inglês
| MEDLINE
| ID: mdl-33811917
6.
The Enzymatic Activity of Inosine 5'-Monophosphate Dehydrogenase May Not Be a Vulnerable Target for Staphylococcus aureus Infections.
ACS Infect Dis;
7(11): 3062-3076, 2021 11 12.
Artigo
em Inglês
| MEDLINE
| ID: mdl-34590817