Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.
about
TMTC1 and TMTC2 are novel endoplasmic reticulum tetratricopeptide repeat-containing adapter proteins involved in calcium homeostasisN-linked sugar-regulated protein folding and quality control in the ERMolecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradationTyrosinase degradation is prevented when EDEM1 lacks the intrinsically disordered regionSerum Glycopatterns as Novel Potential Biomarkers for Diagnosis of Acute-on-Chronic Hepatitis B Liver FailureC-terminus glycans with critical functional role in the maturation of secretory glycoproteins.The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis.The transmembrane domain of the molecular chaperone Cosmc directs its localization to the endoplasmic reticulum.'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocksReglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation.Boosting in planta production of antigens derived from the porcine reproductive and respiratory syndrome virus (PRRSV) and subsequent evaluation of their immunogenicity.Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis.Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology.Interaction of members of the heat shock protein-70 family with the macrophage mannose receptor.Hsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligaseER stress and the decline and fall of pancreatic beta cells in type 1 diabetes.How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD.Sorting things out through endoplasmic reticulum quality control.Protein folding in the endoplasmic reticulumSignal peptide of cellulase.Protein folding and secretion: mechanistic insights advancing recombinant protein production in S. cerevisiae.Sequence-based protein stabilization in the absence of glycosylation.CD39 reveals novel insights into the role of transmembrane domains in protein processing, apical targeting and activity.N-Glycan-dependent and -independent quality control of human δ opioid receptor N-terminal variants.Alteration and localization of glycan-binding proteins in human hepatic stellate cells during liver fibrosis.Intracellular cysteine 346 is essentially involved in regulating Panx1 channel activity.Synthesis of Glc1Man9-Glycoprotein Probes by a Misfolding/Enzymatic Glucosylation/Misfolding Sequence.Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins.
P2860
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P2860
Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年學術文章
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name
Lectin chaperones help direct ...... in the endoplasmic reticulum.
@en
Lectin chaperones help direct ...... in the endoplasmic reticulum.
@nl
type
label
Lectin chaperones help direct ...... in the endoplasmic reticulum.
@en
Lectin chaperones help direct ...... in the endoplasmic reticulum.
@nl
prefLabel
Lectin chaperones help direct ...... in the endoplasmic reticulum.
@en
Lectin chaperones help direct ...... in the endoplasmic reticulum.
@nl
P2860
P1476
Lectin chaperones help direct ...... in the endoplasmic reticulum.
@en
P2093
Bradley R Pearse
Daniel N Hebert
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P304
P356
10.1016/J.BBAMCR.2009.10.008
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P577
2009-11-03T00:00:00Z