Substrate hydrolysis by matrix metalloproteinase-9. (Q45736978)

15 December 2017

Substrate hydrolysis by matrix metalloproteinase-9. (English)

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15 December 2017

Kridel SJ

1

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15 December 2017

Chen E

2

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15 December 2017

Kotra LP

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15 December 2017

Howard EW

4

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15 December 2017

Mobashery S

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15 December 2017

Smith JW

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15 December 2017

language of work or name

English

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publication date

14 March 2001

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Journal of Biological Chemistry

15 December 2017

7

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based on heuristic

inferred from page(s)

published in

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15 December 2017

276

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15 December 2017

23

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15 December 2017

20572-20578

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The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo.

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Gelatinase B is present in the cerebrospinal fluid during experimental autoimmune encephalomyelitis and cleaves myelin basic protein.

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MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes

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Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis

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MMP-9 supplied by bone marrow-derived cells contributes to skin carcinogenesis

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Matrix metalloproteinase-9 (gelatinase B) is selectively elevated in CSF during relapses and stable phases of multiple sclerosis.

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Cerebrospinal fluid levels of MMP-2, 7, and 9 are elevated in association with human immunodeficiency virus dementia

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Proteolytic remodeling of extracellular matrix

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Matrix metalloproteinases: a review

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Focalized proteolysis: spatial and temporal regulation of extracellular matrix degradation at the cell surface

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Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases

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The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction

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Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

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On the size of the active site in proteases. I. Papain

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Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed

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Substrate specificity of human collagenase 3 assessed using a phage-displayed peptide library

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Galectin-3 is a novel substrate for human matrix metalloproteinases-2 and -9.

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A 92 kDa gelatinase (MMP-9) cleavage site in native type V collagen

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Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

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Identification of a region in the integrin beta3 subunit that confers ligand binding specificity

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Gelatinase B-deficient mice are resistant to experimental bullous pemphigoid

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Leukocyte Gelatinase B Cleavage Releases Encephalitogens from Human Myelin Basic Protein

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Identifiers

DOI

10.1074/JBC.M100900200

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15 December 2017

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