The Propeptide Domain of Membrane Type 1-Matrix Metalloproteinase Acts as an Intramolecular Chaperone when Expressed in transwith the Mature Sequence in COS-1 Cells-Reference-Cited by-同舟云学术

The Propeptide Domain of Membrane Type 1-Matrix Metalloproteinase Acts as an Intramolecular Chaperone when Expressed in transwith the Mature Sequence in COS-1 Cells

Published:2000-09 Issue:38 Volume:275 Page:29648-29653
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Cao Jian,Hymowitz Michelle,Conner Cathleen,Bahou Wadie F.,Zucker Stanley

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference30 articles.

1. A matrix metalloproteinase expressed on the surface of invasive tumour cells

2. The C-terminal Region of Membrane Type Matrix Metalloproteinase Is a Functional Transmembrane Domain Required for Pro-gelatinase A Activation

3. Membrane-Type Matrix Metalloproteinases 1 and 2 Exhibit Broad-Spectrum Proteolytic Capacities Comparable to Many Matrix Metalloproteinases

4. The Propeptide Domain of Membrane Type 1 Matrix Metalloproteinase Is Required for Binding of Tissue Inhibitor of Metalloproteinases and for Activation of Pro-gelatinase A

5. Tissue Inhibitor of Metalloproteinase-2 (TIMP-2) Binds to the Catalytic Domain of the Cell Surface Receptor, Membrane Type 1-Matrix Metalloproteinase 1 (MT1-MMP)

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