The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
about
Requirement of the Lec35 gene for all known classes of monosaccharide-P-dolichol-dependent glycosyltransferase reactions in mammalsRescue of functional delF508-CFTR channels in cystic fibrosis epithelial cells by the alpha-glucosidase inhibitor miglustatMajor histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly statusIdentification and functional analysis of a defect in the human ALG9 gene: definition of congenital disorder of glycosylation type IL.Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" molecular chaperonesCalreticulin controls the rate of assembly of CD1d molecules in the endoplasmic reticulumERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectinsInteractions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulumIntegral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosisGlycoprotein Quality Control and Endoplasmic Reticulum StressInvolvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteinsNMR structure of the calreticulin P-domainStructural Basis of Carbohydrate Recognition by CalreticulinStructural and Functional Relationships between the Lectin and Arm Domains of CalreticulinCell wall 1,6-beta-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II, and the molecular chaperone BiP/Kar2p.Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulinCalnexin associates exclusively with individual CD3 delta and T cell antigen receptor (TCR) alpha proteins containing incompletely trimmed glycans that are not assembled into multisubunit TCR complexesThe evolutionary history of calreticulin and calnexin genes in green plantsThe molecular basis of oculocutaneous albinism type 1 (OCA1): sorting failure and degradation of mutant tyrosinases results in a lack of pigmentationFolding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss of Ca2+ from the endoplasmic reticulumProtein disulfide isomerase acts as a molecular chaperone during the assembly of procollagenFunctional relationship between calreticulin, calnexin, and the endoplasmic reticulum luminal domain of calnexinCalnexin influences folding of human class I histocompatibility proteins but not their assembly with beta 2-microglobulinLectins and traffic in the secretory pathwayDifferential modulation of SERCA2 isoforms by calreticulin.Intracellular transport and secretion of salivary proteins.Unique biochemical nature of carp retinol-binding protein. N-linked glycosylation and uncleavable NH2-terminal signal peptide.Immunoaffinity purification and identification of the molecular chaperone calnexin.Cellular effects of deoxynojirimycin analogues: inhibition of N-linked oligosaccharide processing and generation of free glucosylated oligosaccharidesCharacterization of the biosynthesis of human immunodeficiency virus type 1 Env from infected T-cells and the effects of glucose trimming of Env on virion infectivity.Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment.Protein glycosylation in development and disease.TAPBPR bridges UDP-glucose:glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway.Calreticulin: one protein, one gene, many functions.N-glycomic profiling of a glucosidase II mutant of Dictyostelium discoideum by ''off-line'' liquid chromatography and mass spectrometryOligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome.Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradationUDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality controlBiP availability distinguishes states of homeostasis and stress in the endoplasmic reticulum of living cells.Endoplasmic reticulum stress and the unfolded protein responses in retinal degeneration.
P2860
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P2860
The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
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
The molecular chaperone calnex ...... gnizing unfolded glycoproteins
@ast
The molecular chaperone calnex ...... gnizing unfolded glycoproteins
@en
The molecular chaperone calnex ...... gnizing unfolded glycoproteins
@nl
type
label
The molecular chaperone calnex ...... gnizing unfolded glycoproteins
@ast
The molecular chaperone calnex ...... gnizing unfolded glycoproteins
@en
The molecular chaperone calnex ...... gnizing unfolded glycoproteins
@nl
prefLabel
The molecular chaperone calnex ...... gnizing unfolded glycoproteins
@ast
The molecular chaperone calnex ...... gnizing unfolded glycoproteins
@en
The molecular chaperone calnex ...... gnizing unfolded glycoproteins
@nl
P2093
P2860
P356
P1476
The molecular chaperone calnex ...... gnizing unfolded glycoproteins
@en
P2093
A. Vassilakos
D. B. Williams
F. E. Ware
M. A. Lehrman
M. R. Jackson
P. A. Peterson
P2860
P304
P356
10.1074/JBC.270.9.4697
P407
P577
1995-03-03T00:00:00Z