Structure-function studies on hsp47: pH-dependent inhibition of collagen fibril formation in vitro.
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Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognitionThe molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesisMimicking titration experiments with MD simulations: A protocol for the investigation of pH-dependent effects on proteinsXaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47.Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesisThe rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens.Molecular Consequences of the SERPINH1/HSP47 Mutation in the Dachshund Natural Model of Osteogenesis Imperfecta.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.Heat shock protein 47 and 65 KDa FK506 binding protein weakly but synergistically interact during collagen folding in the endoplasmic reticulum.Specific recognition of the collagen triple helix by chaperone HSP47. II. The HSP47-binding structural motif in collagens and related proteins.Mapping Hsp47 binding site(s) using CNBr peptides derived from type I and type II collagen.A substrate preference for the rough endoplasmic reticulum resident protein FKBP22 during collagen biosynthesis.The pH-dependent Client Release from the Collagen-specific Chaperone HSP47 Is Triggered by a Tandem Histidine Pair.Effect of FKBP65, a putative elastin chaperone, on the coacervation of tropoelastin in vitro.The pH sensitivity of murine heat shock protein 47 (HSP47) binding to collagen is affected by mutations in the breach histidine cluster.Localization of HSP47 mRNA in murine bleomycin-induced pulmonary fibrosis.
P2860
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P2860
Structure-function studies on hsp47: pH-dependent inhibition of collagen fibril formation in vitro.
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2000 nî lūn-bûn
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name
Structure-function studies on ...... gen fibril formation in vitro.
@en
Structure-function studies on ...... gen fibril formation in vitro.
@nl
type
label
Structure-function studies on ...... gen fibril formation in vitro.
@en
Structure-function studies on ...... gen fibril formation in vitro.
@nl
prefLabel
Structure-function studies on ...... gen fibril formation in vitro.
@en
Structure-function studies on ...... gen fibril formation in vitro.
@nl
P2860
P356
P1433
P1476
Structure-function studies on ...... gen fibril formation in vitro.
@en
P2093
Ananthanarayanan VS
Thomson CA
P2860
P304
P356
10.1042/BJ3490877
P407
P478
P577
2000-08-01T00:00:00Z