228 related articles for article (PubMed ID: 35078937)
1. 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]
2. Grp94 Works Upstream of BiP in Protein Remodeling Under Heat Stress.
Amankwah YS; Collins P; Fleifil Y; Unruh E; Ruiz Márquez KJ; Vitou K; Kravats AN
J Mol Biol; 2022 Oct; 434(19):167762. PubMed ID: 35905823
[TBL] [Abstract][Full Text] [Related]
3. 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]
4. Structural transitions modulate the chaperone activities of Grp94.
Amankwah YS; Fleifil Y; Unruh E; Collins P; Wang Y; Vitou K; Bates A; Obaseki I; Sugoor M; Alao JP; McCarrick RM; Gewirth DT; Sahu ID; Li Z; Lorigan GA; Kravats AN
Proc Natl Acad Sci U S A; 2024 Mar; 121(12):e2309326121. PubMed ID: 38483986
[TBL] [Abstract][Full Text] [Related]
5. The ER Chaperones BiP and Grp94 Regulate the Formation of Insulin-Like Growth Factor 2 (IGF2) Oligomers.
Jin Y; Kotler JLM; Wang S; Huang B; Halpin JC; Street TO
J Mol Biol; 2021 Jun; 433(13):166963. PubMed ID: 33811917
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. 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]
8. Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation.
Kuznetsov G; Chen LB; Nigam SK
J Biol Chem; 1994 Sep; 269(37):22990-5. PubMed ID: 7916014
[TBL] [Abstract][Full Text] [Related]
9. Enhanced binding to the molecular chaperone BiP slows thyroglobulin export from the endoplasmic reticulum.
Muresan Z; Arvan P
Mol Endocrinol; 1998 Mar; 12(3):458-67. PubMed ID: 9514162
[TBL] [Abstract][Full Text] [Related]
10. Nascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones, GRP94, ERp72, BiP, calreticulin, and cyclophilin B.
Zhang J; Herscovitz H
J Biol Chem; 2003 Feb; 278(9):7459-68. PubMed ID: 12397072
[TBL] [Abstract][Full Text] [Related]
11. Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones.
Dollins DE; Warren JJ; Immormino RM; Gewirth DT
Mol Cell; 2007 Oct; 28(1):41-56. PubMed ID: 17936703
[TBL] [Abstract][Full Text] [Related]
12. Mechanisms of Protein Quality Control in the Endoplasmic Reticulum by a Coordinated Hsp40-Hsp70-Hsp90 System.
Kotler JLM; Street TO
Annu Rev Biophys; 2023 May; 52():509-524. PubMed ID: 37159299
[TBL] [Abstract][Full Text] [Related]
13. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum.
Melnick J; Dul JL; Argon Y
Nature; 1994 Aug; 370(6488):373-5. PubMed ID: 7913987
[TBL] [Abstract][Full Text] [Related]
14. Insight into the Nucleotide Based Modulation of the Grp94 Molecular Chaperone Using Multiscale Dynamics.
Alao JP; Obaseki I; Amankwah YS; Nguyen Q; Sugoor M; Unruh E; Popoola HO; Tehver R; Kravats AN
J Phys Chem B; 2023 Jun; 127(24):5389-5409. PubMed ID: 37294929
[TBL] [Abstract][Full Text] [Related]
15. The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains.
Melnick J; Aviel S; Argon Y
J Biol Chem; 1992 Oct; 267(30):21303-6. PubMed ID: 1400441
[TBL] [Abstract][Full Text] [Related]
16. 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]
17. The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum.
Alder NN; Shen Y; Brodsky JL; Hendershot LM; Johnson AE
J Cell Biol; 2005 Jan; 168(3):389-99. PubMed ID: 15684029
[TBL] [Abstract][Full Text] [Related]
18. GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum.
Marzec M; Eletto D; Argon Y
Biochim Biophys Acta; 2012 Mar; 1823(3):774-87. PubMed ID: 22079671
[TBL] [Abstract][Full Text] [Related]
19. HOP3, a member of the HOP family in Arabidopsis, interacts with BiP and plays a major role in the ER stress response.
Fernández-Bautista N; Fernández-Calvino L; Muñoz A; Castellano MM
Plant Cell Environ; 2017 Aug; 40(8):1341-1355. PubMed ID: 28155228
[TBL] [Abstract][Full Text] [Related]
20. 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]
[Next] [New Search]