Endoplasmic reticulum protein 29 (ERp29) is a chaperone protein that in humans is encoded by the ERP29 gene. ERp29 is a reticuloplasmin, a protein which...
7 KB (860 words) - 01:55, 3 December 2023
reticulum chaperone proteins, including protein disulfide isomerase (PDI), ERp29, the Hsp70 family member BiP/Grp78, calnexin, calreticulin, and the peptidylprolyl...
34 KB (3,710 words) - 08:29, 7 July 2024
calnexin and calreticulin Non-classical molecular chaperones: HSP47 and ERp29 Folding chaperones: Protein disulfide isomerase (PDI), Peptidyl prolyl cis-trans...
29 KB (3,499 words) - 07:16, 20 February 2024
protein disulfide isomerases include: AGR2 AGR3 CASQ1 CASQ2 DNAJC10 ERP27 ERP29 ERP44 P4HB PDIA2 PDIA3 PDIA4 PDIA5 PDIA6 PDIALT TMX1 TMX2 TMX3 TMX4 TXNDC5...
19 KB (1,936 words) - 16:09, 10 July 2024
HGNC:13280 Q96HE7 5092 ERO1B HGNC:14355 Q86YB8 5093 ERP27 HGNC:26495 Q96DN0 5094 ERP29 HGNC:13799 P30040 5095 ERP44 HGNC:18311 Q9BS26 5096 ERRFI1 HGNC:18185 Q9UJM3...
277 KB (17 words) - 15:46, 9 May 2024
1097/00008571-199906000-00005. PMID 10471062. Hubbard MJ, McHugh NJ (2001). "Human ERp29: isolation, primary structural characterisation and two-dimensional gel...
11 KB (1,278 words) - 04:12, 27 May 2024
1006/geno.1996.4597. PMID 9073515. Hubbard MJ, McHugh NJ (2001). "Human ERp29: isolation, primary structural characterisation and two-dimensional gel...
11 KB (1,293 words) - 00:09, 8 June 2024
1074/jbc.274.8.5131. PMID 9988762. Hubbard MJ, McHugh NJ (2001). "Human ERp29: isolation, primary structural characterisation and two-dimensional gel...
10 KB (1,061 words) - 16:48, 31 March 2024
specific host proteins located in the late ER; for example, the host protein ERp29, a member of the protein disulfide isomerase family, has been shown to disrupt...
22 KB (2,402 words) - 16:26, 5 January 2024