Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
about
Calumenin, a Ca2+-binding protein retained in the endoplasmic reticulum with a novel carboxyl-terminal sequence, HDEFEffect of the R569W missense mutation on the biosynthesis of myeloperoxidaseImmune responses in hookworm infectionsSuppressive roles of calreticulin in prostate cancer growth and metastasisInteractions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulumInvolvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteinsNMR structure of the calreticulin P-domainYeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum.Proteomic analysis of human neutrophil granulesEndoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunitThe Ca(2+) status of the endoplasmic reticulum is altered by induction of calreticulin expression in transgenic plantsImpaired p53 expression, function, and nuclear localization in calreticulin-deficient cellsFunctional relationship between calreticulin, calnexin, and the endoplasmic reticulum luminal domain of calnexinDifferential modulation of SERCA2 isoforms by calreticulin.A hookworm allergen which strongly resembles calreticulin.Fluorescence tracing of intracellular proteins.Polypeptide binding properties of the chaperone calreticulin.Structure of human promyeloperoxidase (proMPO) and the role of the propeptide in processing and maturation.The structure of calreticulin C-terminal domain is modulated by physiological variations of calcium concentration.Calreticulin: one protein, one gene, many functions.Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradationImpact of missense mutations on biosynthesis of myeloperoxidase.Functional consequence of positive selection revealed through rational mutagenesis of human myeloperoxidase.Selective fusion of azurophilic granules with Leishmania-containing phagosomes in human neutrophils.Inhibition of type I insulin-like growth factor receptor tyrosine kinase by picropodophyllin induces apoptosis and cell cycle arrest in T lymphoblastic leukemia/lymphoma.Overexpression of a Triticum aestivum Calreticulin gene (TaCRT1) Improves Salinity Tolerance in Tobacco.The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules.Mutations in the carboxyl-terminal hydrophobic sequence of human cytomegalovirus glycoprotein B alter transport and protein chaperone bindingN-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin.Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexesRegulation of calreticulin gene expression by calcium.Protein folding in the endoplasmic reticulum: lessons from the human chorionic gonadotropin beta subunitProconvertase proteolytic processing of an enzymatically active myeloperoxidase precursorCalreticulin is essential for cardiac developmentThe function of calreticulin in plant immunity: new discoveries for an old protein.Cellular response to unfolded proteins in the endoplasmic reticulum of plants.Trypanosoma cruzi calreticulin is a lectin that binds monoglucosylated oligosaccharides but not protein moieties of glycoproteins.Cystic fibrosis transmembrane conductance regulator recruitment to phagosomes in neutrophils.A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation.Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules.
P2860
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P2860
Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
description
1995 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մարտին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1995
@ast
im März 1995 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1995/03/03)
@sk
vědecký článek publikovaný v roce 1995
@cs
wetenschappelijk artikel (gepubliceerd op 1995/03/03)
@nl
наукова стаття, опублікована в березні 1995
@uk
name
Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
@ast
Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
@en
Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
@nl
type
label
Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
@ast
Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
@en
Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
@nl
prefLabel
Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
@ast
Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
@en
Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
@nl
P2093
P2860
P356
P1476
Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
@en
P2093
R. A. Clark
S. J. McCormick
W. M. Nauseef
P2860
P304
P356
10.1074/JBC.270.9.4741
P407
P577
1995-03-03T00:00:00Z