ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activity
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Structural Basis of Cyclophilin B Binding by the Calnexin/Calreticulin P-domainStructural and Functional Relationships between the Lectin and Arm Domains of CalreticulinCo- and Post-Translational Protein Folding in the ERMolecular Chaperone Calnexin Regulates the Function of Drosophila Sodium Channel Paralytic.Transient covalent interactions of newly synthesized thyroglobulin with oxidoreductases of the endoplasmic reticulumCalreticulin: non-endoplasmic reticulum functions in physiology and disease.Modes of calreticulin recruitment to the major histocompatibility complex class I assembly pathwayLong-term supranutritional supplementation with selenate decreases hyperglycemia and promotes fatty liver degeneration by inducing hyperinsulinemia in diabetic db/db mice.The polypeptide binding conformation of calreticulin facilitates its cell-surface expression under conditions of endoplasmic reticulum stress.Essential glycan-dependent interactions optimize MHC class I peptide loadingStepwise assembly of fibrinogen is assisted by the endoplasmic reticulum lectin-chaperone system in HepG2 cells.The disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosisDivision of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides.Functional significance of tapasin membrane association and disulfide linkage to ERp57 in MHC class I presentationIntracellular assembly and trafficking of MHC class I molecules.The peptide-loading complex--antigen translocation and MHC class I loading.A structural overview of the PDI family of proteins.The Ca2+ pumps of the endoplasmic reticulum and Golgi apparatus.ERp57/GRP58: a protein with multiple functions.Calreticulin in the immune system: ins and outsDepletion of the thiol oxidoreductase ERp57 in tumor cells inhibits proliferation and increases sensitivity to ionizing radiation and chemotherapeuticsFunctional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteinsERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulumStructure of the human MHC-I peptide-loading complex.
P2860
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P2860
ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activity
description
article científic
@ca
article scientifique
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articolo scientifico
@it
artigo científico
@pt
bilimsel makale
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scientific article published on 05 February 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
ERp57 does not require interac ...... endently of its redox activity
@en
ERp57 does not require interac ...... ndently of its redox activity.
@nl
type
label
ERp57 does not require interac ...... endently of its redox activity
@en
ERp57 does not require interac ...... ndently of its redox activity.
@nl
prefLabel
ERp57 does not require interac ...... endently of its redox activity
@en
ERp57 does not require interac ...... ndently of its redox activity.
@nl
P2093
P2860
P356
P1476
ERp57 does not require interac ...... endently of its redox activity
@en
P2093
Breanna S Ireland
Chris Howe
Cosmin L Pocanschi
David B Williams
Guennadi Kozlov
Pekka Maattanen
Ulf Brockmeier
Yinan Zhang
P2860
P304
10160-10173
P356
10.1074/JBC.M808356200
P407
P577
2009-02-05T00:00:00Z