Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen
about
TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesisExome sequencing identifies truncating mutations in human SERPINF1 in autosomal-recessive osteogenesis imperfectaMolecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognitionHomozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfectaEmbryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesisExpressional patterns of chaperones in ten human tumor cell lines.The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesisType XXVI collagen, a new member of the collagen family, is specifically expressed in the testis and ovaryFunctional linkage between the endoplasmic reticulum protein Hsp47 and procollagen expression in human vascular smooth muscle cellsIs protein disulfide isomerase a redox-dependent molecular chaperone?Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47.Non-natural CBP2 binding peptides and peptomers modulate carcinoma cell adhesion and invasion.Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.The collagen V homotrimer [alpha1(V)](3) production is unexpectedly favored over the heterotrimer [alpha1(V)](2)alpha2(V) in recombinant expression systems.Unstable molecules form stable tissuesType I collagen is thermally unstable at body temperatureDevelopmental regulation and coordinate reexpression of FKBP65 with extracellular matrix proteins after lung injury suggest a specialized function for this endoplasmic reticulum immunophilin.Glycoprotein folding in the endoplasmic reticulum.Collagens and collagen-related diseases.Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesisA new hypothesis regarding ovarian follicle development: ovarian rigidity as a regulator of selection and health.Mechano-regulation of collagen biosynthesis in periodontal ligament.Designing follicle-environment interactions with biomaterials.The endoplasmic reticulum-resident chaperone heat shock protein 47 protects the Golgi apparatus from the effects of O-glycosylation inhibition.Structural variations in articular cartilage matrix are associated with early-onset osteoarthritis in the spondyloepiphyseal dysplasia congenita (sedc) mouse.Heat shock protein 47: a novel biomarker of phenotypically altered collagen-producing cells.Microscopic and ultrastructural modifications of postmenopausal atrophic vaginal mucosa after fractional carbon dioxide laser treatment.Design and validation of a novel splashing bioreactor system for use in mitral valve organ culture.Temporal gene expression profiling of the rat knee joint capsule during immobilization-induced joint contractures.SerpinB2 (PAI-2) Modulates Proteostasis via Binding Misfolded Proteins and Promotion of Cytoprotective Inclusion Formation.An erythroid chaperone that facilitates folding of alpha-globin subunits for hemoglobin synthesisAnalysis of the mechanism of the tight-junctional permeability increase by capsaicin treatment on the intestinal Caco-2 cells.Light and energy based therapeutics for genitourinary syndrome of menopause: Consensus and controversies.Is SPARC an evolutionarily conserved collagen chaperone?Effects of leptin deficiency on postnatal lung development in mice.The heterozygous disproportionate micromelia (dmm) mouse: morphological changes in fetal cartilage precede postnatal dwarfism and compared with lethal homozygotes can explain the mild phenotypeChaperoning erythropoiesis.R992C (p.R1192C) Substitution in collagen II alters the structure of mutant molecules and induces the unfolded protein response.Insufficient folding of type IV collagen and formation of abnormal basement membrane-like structure in embryoid bodies derived from Hsp47-null embryonic stem cells.Faithful chaperones.
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P2860
Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen
description
2000 nî lūn-bûn
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2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2000 թվականի մայիսին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
Hsp47: a molecular chaperone t ...... s correctly-folded procollagen
@ast
Hsp47: a molecular chaperone t ...... s correctly-folded procollagen
@en
Hsp47: a molecular chaperone t ...... s correctly-folded procollagen
@nl
type
label
Hsp47: a molecular chaperone t ...... s correctly-folded procollagen
@ast
Hsp47: a molecular chaperone t ...... s correctly-folded procollagen
@en
Hsp47: a molecular chaperone t ...... s correctly-folded procollagen
@nl
prefLabel
Hsp47: a molecular chaperone t ...... s correctly-folded procollagen
@ast
Hsp47: a molecular chaperone t ...... s correctly-folded procollagen
@en
Hsp47: a molecular chaperone t ...... s correctly-folded procollagen
@nl
P2093
P2860
P356
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P1476
Hsp47: a molecular chaperone t ...... s correctly-folded procollagen
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/19.10.2204
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P577
2000-05-15T00:00:00Z