(Q28183257)

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Bone morphogenetic protein-1 (BMP-1). Identification of the minimal domain structure for procollagen C-proteinase activity

scientific article (publication date: 16 May 2003)

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Bone morphogenetic protein-1 (BMP-1). Identification of the minimal domain structure for procollagen C-proteinase activity (English)

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Laure Garrigue-Antar

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Karl E Kadler

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Karl E Kadler

series ordinal

3

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author name string

Nichola Hartigan

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1

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language of work or name

English

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publication date

16 May 2003

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published in

Journal of Biological Chemistry

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volume

278

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issue

20

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page(s)

18045-9

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cites work

Bone: formation by autoinduction

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reference URL

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retrieved

21 January 2018

Novel regulators of bone formation: molecular clones and activities

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21 January 2018

The astacin family of metalloendopeptidases

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reference URL

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21 January 2018

Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family member mammalian Tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.M211448200

retrieved

21 January 2018

Bone morphogenetic protein-1: the type I procollagen C-proteinase

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.M211448200

retrieved

21 January 2018

The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.M211448200

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21 January 2018

Bone morphogenetic protein-1 processes probiglycan

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.M211448200

retrieved

21 January 2018

Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M211448200

retrieved

21 January 2018

Metalloproteinase Activity Secreted by Fibrogenic Cells in the Processing of Prolysyl Oxidase

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.M211448200

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21 January 2018

Multiple bone morphogenetic protein 1-related mammalian metalloproteinases process pro-lysyl oxidase at the correct physiological site and control lysyl oxidase activation in mouse embryo fibroblast cultures

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.M211448200

retrieved

21 January 2018

Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M211448200

retrieved

21 January 2018

Structure and function of procollagen C-proteinase (mTolloid) domains determined by protease digestion, circular dichroism, binding to procollagen type I, and computer modeling

1 reference

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Crossref

reference URL

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21 January 2018

Identification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activity

1 reference

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M211448200

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21 January 2018

Two domains of the tolloid protein contribute to its unusual genetic interaction with decapentaplegic.

1 reference

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M211448200

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21 January 2018

Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M211448200

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21 January 2018

Mammalian tolloid metalloproteinase, and not matrix metalloprotease 2 or membrane type 1 metalloprotease, processes laminin-5 in keratinocytes and skin

1 reference

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reference URL

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21 January 2018

Crystal structure of acidic seminal fluid protein (aSFP) at 1.9 Å resolution: a bovine polypeptide of the spermadhesin family

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https://api.crossref.org/works/10.1074%2FJBC.M211448200

retrieved

21 January 2018

Identifiers

DOI

10.1074/JBC.M211448200

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PubMed publication ID

12637537

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(Q28183257)

Bone morphogenetic protein-1 (BMP-1). Identification of the minimal domain structure for procollagen C-proteinase activity

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