Skip to search formSkip to main contentSkip to account menu

MMP3 protein, human

Known as: Matrix Metalloproteinase-3, MMP3, Stromelysin 1 
Stromelysin-1 (477 aa, ~54 kDa) is encoded by the human MMP3 gene. This protein is involved in cleavage of fibronectin, laminin and proteoglycans.
National Institutes of Health

Related topics

Related topics

11 relations
Enzyme GeneHydrolysisMMP-3 activityMMP3 gene

Broader (1)

Matrix Metalloproteinase 3

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2009
Highly Cited
2009
Neuroprotective Effect of Ghrelin in the 1-Methyl-4-Phenyl-1,2,3,6-Tetrahydropyridine Mouse Model of Parkinson’s Disease by Blocking Microglial Activation
Ghrelin is an endogenous ligand for growth hormone (GH) secretagogue receptor 1a (GHS-R1a) and is produced and released mainly… 
Highly Cited
2007
Highly Cited
2007
Platelet rich plasma (PRP) enhances anabolic gene expression patterns in flexor digitorum superficialis tendons
Platelet rich plasma (PRP) has recently been investigated for use in tissue regeneration studies that seek to utilize the… 
Highly Cited
2002
Highly Cited
2002
Increased matrix metalloproteinase-3 serum levels in rheumatic diseases: relationship with synovitis and steroid treatment
Objective: To determine matrix metalloproteinase-3 (MMP-3) serum levels in patients with rheumatic diseases and to study the… 
Highly Cited
2001
Highly Cited
2001
Conformational Dependence of Collagenase (Matrix Metalloproteinase-1) Up-regulation by Elastin Peptides in Cultured Fibroblasts*
We have established that treatment of cultured human skin fibroblasts with tropoelastin or with heterogenic peptides, obtained… 
Highly Cited
2000
Highly Cited
2000
Increased production of matrix metalloproteinase‐3 and tissue inhibitor of metalloproteinase‐1 by inflamed mucosa in inflammatory bowel disease
Inflammatory bowel diseases (IBD) are characterized by a sustained inflammatory cascade that gives rise to the release of… 
Review
1999
Review
1999
Measurement of Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases in Blood and Tissues: Clinical and Experimental Applications
ABSTRACT: The balance between production and activation of MMPs and their inhibition by TIMPs is a crucial aspect of cancer… 
Highly Cited
1992
Highly Cited
1992
The role of the C-terminal domain in collagenase and stromelysin specificity.
Highly Cited
1988
Highly Cited
1988
The complete primary structure of human matrix metalloproteinase-3. Identity with stromelysin.
Highly Cited
1986
Highly Cited
1986
Primary structure and cDNA cloning of human fibroblast collagenase inhibitor.
We report the primary structure and cDNA cloning of human fibroblast collagenase inhibitor, a glycoprotein that appears to play a… 
Highly Cited
1983
Highly Cited
1983
Purification and characterization of a rabbit bone metalloproteinase that degrades proteoglycan and other connective-tissue components.
A metalloproteinase, 'proteoglycanase', that degrades proteoglycan and insoluble type IV collagen as well as casein was purified… 
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)