Heat shock protein 47 and 65 KDa FK506 binding protein weakly but synergistically interact during collagen folding in the endoplasmic reticulum.

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Heat shock protein 47 and 65 KDa FK506 binding protein weakly but synergistically interact during collagen folding in the endoplasmic reticulum.

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

@yue

2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年论文

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2017年论文

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2017年论文

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Heat shock protein 47 and 65 K ...... in the endoplasmic reticulum.

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label

Heat shock protein 47 and 65 K ...... in the endoplasmic reticulum.

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Heat shock protein 47 and 65 K ...... in the endoplasmic reticulum.

@en

P1476

Heat shock protein 47 and 65 K ...... in the endoplasmic reticulum.

@en

P2093

Hans Peter Bachinger

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Paul Holden

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Yoshihiro Ishikawa

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P2860

Chaperones and folding of MHC class I molecules in the endoplasmic reticulum

Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex

Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes

A novel mutation in LEPRE1 that eliminates only the KDEL ER- retrieval sequence causes non-lethal osteogenesis imperfecta

An interaction map of endoplasmic reticulum chaperones and foldases

HSP47: a tissue-specific, transformation-sensitive, collagen-binding heat shock protein of chicken embryo fibroblasts

Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition

Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta

Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis

Protein folding and quality control in the ER

P31

scholarly article

P356

10.1074/JBC.M117.802298

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P407

English

P577

2017-08-31T00:00:00Z

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P698

28860186

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P921

endoplasmic reticulum

protein folding

P932

5655501

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