499 related articles for article (PubMed ID: 12401114)
1. Folding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss of Ca2+ from the endoplasmic reticulum.
Di Jeso B; Ulianich L; Pacifico F; Leonardi A; Vito P; Consiglio E; Formisano S; Arvan P
Biochem J; 2003 Mar; 370(Pt 2):449-58. PubMed ID: 12401114
[TBL] [Abstract][Full Text] [Related]
2. Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum.
Williams DB
J Cell Sci; 2006 Feb; 119(Pt 4):615-23. PubMed ID: 16467570
[TBL] [Abstract][Full Text] [Related]
3. Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum.
Kim PS; Arvan P
J Cell Biol; 1995 Jan; 128(1-2):29-38. PubMed ID: 7822419
[TBL] [Abstract][Full Text] [Related]
4. Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase.
Di Jeso B; Park YN; Ulianich L; Treglia AS; Urbanas ML; High S; Arvan P
Mol Cell Biol; 2005 Nov; 25(22):9793-805. PubMed ID: 16260597
[TBL] [Abstract][Full Text] [Related]
5. Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control.
Molinari M; Eriksson KK; Calanca V; Galli C; Cresswell P; Michalak M; Helenius A
Mol Cell; 2004 Jan; 13(1):125-35. PubMed ID: 14731400
[TBL] [Abstract][Full Text] [Related]
6. Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins.
Choukhi A; Ung S; Wychowski C; Dubuisson J
J Virol; 1998 May; 72(5):3851-8. PubMed ID: 9557669
[TBL] [Abstract][Full Text] [Related]
7. Mapping the ER Interactome: The P Domains of Calnexin and Calreticulin as Plurivalent Adapters for Foldases and Chaperones.
Kozlov G; Muñoz-Escobar J; Castro K; Gehring K
Structure; 2017 Sep; 25(9):1415-1422.e3. PubMed ID: 28877505
[TBL] [Abstract][Full Text] [Related]
8. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum.
Michalak M; Groenendyk J; Szabo E; Gold LI; Opas M
Biochem J; 2009 Feb; 417(3):651-66. PubMed ID: 19133842
[TBL] [Abstract][Full Text] [Related]
9. Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex.
Sargsyan E; Baryshev M; Szekely L; Sharipo A; Mkrtchian S
J Biol Chem; 2002 May; 277(19):17009-15. PubMed ID: 11884402
[TBL] [Abstract][Full Text] [Related]
10. Soluble tyrosinase is an endoplasmic reticulum (ER)-associated degradation substrate retained in the ER by calreticulin and BiP/GRP78 and not calnexin.
Popescu CI; Paduraru C; Dwek RA; Petrescu SM
J Biol Chem; 2005 Apr; 280(14):13833-40. PubMed ID: 15677452
[TBL] [Abstract][Full Text] [Related]
11. Association of the thyrotropin receptor with calnexin, calreticulin and BiP. Efects on the maturation of the receptor.
Siffroi-Fernandez S; Giraud A; Lanet J; Franc JL
Eur J Biochem; 2002 Oct; 269(20):4930-7. PubMed ID: 12383251
[TBL] [Abstract][Full Text] [Related]
12. In vitro assays of the functions of calnexin and calreticulin, lectin chaperones of the endoplasmic reticulum.
Ireland BS; Niggemann M; Williams DB
Methods Mol Biol; 2006; 347():331-42. PubMed ID: 17072021
[TBL] [Abstract][Full Text] [Related]
13. Hormonal regulation of thyroglobulin export from the endoplasmic reticulum of cultured thyrocytes.
Kim PS; Arvan P
J Biol Chem; 1993 Mar; 268(7):4873-9. PubMed ID: 8095263
[TBL] [Abstract][Full Text] [Related]
14. Defective protein folding and intracellular retention of thyroglobulin-R19K mutant as a cause of human congenital goiter.
Kim PS; Lee J; Jongsamak P; Menon S; Li B; Hossain SA; Bae JH; Panijpan B; Arvan P
Mol Endocrinol; 2008 Feb; 22(2):477-84. PubMed ID: 17916655
[TBL] [Abstract][Full Text] [Related]
15. Biosynthesis, assembly and secretion of coagulation factor VIII.
Kaufman RJ; Pipe SW; Tagliavacca L; Swaroop M; Moussalli M
Blood Coagul Fibrinolysis; 1997 Dec; 8 Suppl 2():S3-14. PubMed ID: 9607108
[TBL] [Abstract][Full Text] [Related]
16. Separate roles and different routing of calnexin and ERp57 in endoplasmic reticulum quality control revealed by interactions with asialoglycoprotein receptor chains.
Frenkel Z; Shenkman M; Kondratyev M; Lederkremer GZ
Mol Biol Cell; 2004 May; 15(5):2133-42. PubMed ID: 14978212
[TBL] [Abstract][Full Text] [Related]
17. Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding.
Ellgaard L; Frickel EM
Cell Biochem Biophys; 2003; 39(3):223-47. PubMed ID: 14716078
[TBL] [Abstract][Full Text] [Related]
18. Protein folding and quality control in the endoplasmic reticulum.
Kleizen B; Braakman I
Curr Opin Cell Biol; 2004 Aug; 16(4):343-9. PubMed ID: 15261665
[TBL] [Abstract][Full Text] [Related]
19. 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]
20. Kinetics of interactions of sendai virus envelope glycoproteins, F and HN, with endoplasmic reticulum-resident molecular chaperones, BiP, calnexin, and calreticulin.
Tomita Y; Yamashita T; Sato H; Taira H
J Biochem; 1999 Dec; 126(6):1090-100. PubMed ID: 10578061
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
