143 related articles for article (PubMed ID: 3612810)
1. The glucose-regulated protein grp94 is related to heat shock protein hsp90.
Sorger PK; Pelham HR
J Mol Biol; 1987 Mar; 194(2):341-4. PubMed ID: 3612810
[TBL] [Abstract][Full Text] [Related]
2. ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94).
Mazzarella RA; Green M
J Biol Chem; 1987 Jun; 262(18):8875-83. PubMed ID: 3036833
[TBL] [Abstract][Full Text] [Related]
3. The 5'-flanking region of the human calreticulin gene shares homology with the human GRP78, GRP94, and protein disulfide isomerase promoters.
McCauliffe DP; Yang YS; Wilson J; Sontheimer RD; Capra JD
J Biol Chem; 1992 Feb; 267(4):2557-62. PubMed ID: 1733953
[TBL] [Abstract][Full Text] [Related]
4. Expression of heat shock proteins (HSP27, HSP60, HSP70, HSP90, GRP78, GRP94) in hepatitis B virus-related hepatocellular carcinomas and dysplastic nodules.
Lim SO; Park SG; Yoo JH; Park YM; Kim HJ; Jang KT; Cho JW; Yoo BC; Jung GH; Park CK
World J Gastroenterol; 2005 Apr; 11(14):2072-9. PubMed ID: 15810071
[TBL] [Abstract][Full Text] [Related]
5. Molecular cloning of bovine (Bos taurus) cDNA encoding a 94-kDa glucose-regulated protein and developmental changes in its mRNA and protein content in the mammary gland.
Watanabe A; Uchida I; Nakata K; Fujimoto Y; Oikawa S
Comp Biochem Physiol B Biochem Mol Biol; 2001 Dec; 130(4):547-57. PubMed ID: 11691631
[TBL] [Abstract][Full Text] [Related]
6. Common sets of nuclear factors binding to the conserved promoter sequence motif of two coordinately regulated ER protein genes, GRP78 and GRP94.
Liu ES; Lee AS
Nucleic Acids Res; 1991 Oct; 19(19):5425-31. PubMed ID: 1923827
[TBL] [Abstract][Full Text] [Related]
7. Analysis of the structure and synthesis of GRP94, an abundant stress protein of the endoplasmic reticulum.
Qu D; Mazzarella RA; Green M
DNA Cell Biol; 1994 Feb; 13(2):117-24. PubMed ID: 8179819
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. 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]
10. Ethanol-responsive genes in neural cells include the 78-kilodalton glucose-regulated protein (GRP78) and 94-kilodalton glucose-regulated protein (GRP94) molecular chaperones.
Miles MF; Wilke N; Elliot M; Tanner W; Shah S
Mol Pharmacol; 1994 Nov; 46(5):873-9. PubMed ID: 7969074
[TBL] [Abstract][Full Text] [Related]
11. adapt78, a stress-inducible mRNA, is related to the glucose-regulated protein family of genes.
Leahy KP; Davies KJ; Dull M; Kort JJ; Lawrence KW; Crawford DR
Arch Biochem Biophys; 1999 Aug; 368(1):67-74. PubMed ID: 10415113
[TBL] [Abstract][Full Text] [Related]
12. cDNA cloning and expression of grp94 in the Pacific oyster Crassostrea gigas.
Kawabe S; Yokoyama Y
Comp Biochem Physiol B Biochem Mol Biol; 2009 Nov; 154(3):290-7. PubMed ID: 19595786
[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. A pathogen-induced gene of barley encodes a HSP90 homologue showing striking similarity to vertebrate forms resident in the endoplasmic reticulum.
Walther-Larsen H; Brandt J; Collinge DB; Thordal-Christensen H
Plant Mol Biol; 1993 Mar; 21(6):1097-108. PubMed ID: 8490130
[TBL] [Abstract][Full Text] [Related]
15. Leishmania infantum: gene cloning of the GRP94 homologue, its expression as recombinant protein, and analysis of antigenicity.
Larreta R; Soto M; Alonso C; Requena JM
Exp Parasitol; 2000 Oct; 96(2):108-15. PubMed ID: 11052869
[TBL] [Abstract][Full Text] [Related]
16. Lead induces the expression of endoplasmic reticulum chaperones GRP78 and GRP94 in vascular endothelial cells via the JNK-AP-1 pathway.
Shinkai Y; Yamamoto C; Kaji T
Toxicol Sci; 2010 Apr; 114(2):378-86. PubMed ID: 20071421
[TBL] [Abstract][Full Text] [Related]
17. The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin.
Lin HY; Masso-Welch P; Di YP; Cai JW; Shen JW; Subjeck JR
Mol Biol Cell; 1993 Nov; 4(11):1109-19. PubMed ID: 8305733
[TBL] [Abstract][Full Text] [Related]
18. Endoplasmic reticulum chaperone GRP94 subunit assembly is regulated through a defined oligomerization domain.
Wearsch PA; Nicchitta CV
Biochemistry; 1996 Dec; 35(51):16760-9. PubMed ID: 8988013
[TBL] [Abstract][Full Text] [Related]
19. Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy.
Jahn M; Tych K; Girstmair H; Steinmaßl M; Hugel T; Buchner J; Rief M
Structure; 2018 Jan; 26(1):96-105.e4. PubMed ID: 29276035
[TBL] [Abstract][Full Text] [Related]
20. Conformation-defective herpes simplex virus 1 glycoprotein B activates the promoter of the grp94 gene that codes for the 94-kD stress protein in the endoplasmic reticulum.
Ramakrishnan M; Tugizov S; Pereira L; Lee AS
DNA Cell Biol; 1995 May; 14(5):373-84. PubMed ID: 7748487
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]