295 related articles for article (PubMed ID: 11700281)
1. The action of molecular chaperones in the early secretory pathway.
Fewell SW; Travers KJ; Weissman JS; Brodsky JL
Annu Rev Genet; 2001; 35():149-91. PubMed ID: 11700281
[TBL] [Abstract][Full Text] [Related]
2. Mechanism and components of endoplasmic reticulum-associated degradation.
Hoseki J; Ushioda R; Nagata K
J Biochem; 2010 Jan; 147(1):19-25. PubMed ID: 19923195
[TBL] [Abstract][Full Text] [Related]
3. Protein quality control in the endoplasmic reticulum.
Jørgensen MM; Bross P; Gregersen N
APMIS Suppl; 2003; (109):86-91. PubMed ID: 12874956
[TBL] [Abstract][Full Text] [Related]
4. Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD).
Nishikawa S; Brodsky JL; Nakatsukasa K
J Biochem; 2005 May; 137(5):551-5. PubMed ID: 15944407
[TBL] [Abstract][Full Text] [Related]
5. GRP94 in ER quality control and stress responses.
Eletto D; Dersh D; Argon Y
Semin Cell Dev Biol; 2010 Jul; 21(5):479-85. PubMed ID: 20223290
[TBL] [Abstract][Full Text] [Related]
6. Cellular responses to endoplasmic reticulum stress and apoptosis.
Rasheva VI; Domingos PM
Apoptosis; 2009 Aug; 14(8):996-1007. PubMed ID: 19360473
[TBL] [Abstract][Full Text] [Related]
7. The endoplasmic reticulum-associated degradation and disulfide reductase ERdj5.
Ushioda R; Nagata K
Methods Enzymol; 2011; 490():235-58. PubMed ID: 21266254
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. Quality control and protein folding in the secretory pathway.
Trombetta ES; Parodi AJ
Annu Rev Cell Dev Biol; 2003; 19():649-76. PubMed ID: 14570585
[TBL] [Abstract][Full Text] [Related]
10. Quality control in the secretory pathway.
Hammond C; Helenius A
Curr Opin Cell Biol; 1995 Aug; 7(4):523-9. PubMed ID: 7495572
[TBL] [Abstract][Full Text] [Related]
11. ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER.
Ushioda R; Hoseki J; Araki K; Jansen G; Thomas DY; Nagata K
Science; 2008 Jul; 321(5888):569-72. PubMed ID: 18653895
[TBL] [Abstract][Full Text] [Related]
12. The many functions of the endoplasmic reticulum chaperones and folding enzymes.
Halperin L; Jung J; Michalak M
IUBMB Life; 2014 May; 66(5):318-26. PubMed ID: 24839203
[TBL] [Abstract][Full Text] [Related]
13. ER and aging-Protein folding and the ER stress response.
Naidoo N
Ageing Res Rev; 2009 Jul; 8(3):150-9. PubMed ID: 19491040
[TBL] [Abstract][Full Text] [Related]
14. ER chaperone functions during normal and stress conditions.
Ma Y; Hendershot LM
J Chem Neuroanat; 2004 Sep; 28(1-2):51-65. PubMed ID: 15363491
[TBL] [Abstract][Full Text] [Related]
15. Endoplasmic reticulum quality control and apoptosis.
Groenendyk J; Michalak M
Acta Biochim Pol; 2005; 52(2):381-95. PubMed ID: 15933766
[TBL] [Abstract][Full Text] [Related]
16. Protein Quality Control in the Endoplasmic Reticulum.
Adams BM; Oster ME; Hebert DN
Protein J; 2019 Jun; 38(3):317-329. PubMed ID: 31004255
[TBL] [Abstract][Full Text] [Related]
17. Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control.
Vashist S; Ng DT
J Cell Biol; 2004 Apr; 165(1):41-52. PubMed ID: 15078901
[TBL] [Abstract][Full Text] [Related]
18. Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia.
Kuznetsov G; Bush KT; Zhang PL; Nigam SK
Proc Natl Acad Sci U S A; 1996 Aug; 93(16):8584-9. PubMed ID: 8710914
[TBL] [Abstract][Full Text] [Related]
19. Protein folding and modification in the mammalian endoplasmic reticulum.
Braakman I; Bulleid NJ
Annu Rev Biochem; 2011; 80():71-99. PubMed ID: 21495850
[TBL] [Abstract][Full Text] [Related]
20. Setting the standards: quality control in the secretory pathway.
Ellgaard L; Molinari M; Helenius A
Science; 1999 Dec; 286(5446):1882-8. PubMed ID: 10583943
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
