Results 271 to 280 of about 240,479 (306)
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Production of human matrix metalloproteinase 3 (stromelysin) in Escherichia coli

Gene, 1994
Full-length human matrix metalloproteinase 3 (prostomelysin or proMMP-3) was produced in Escherichia coli as an intracellular insoluble aggregate that could be solubilized and refolded to yield an activatable proenzyme. The refolded protein was purified to > 95% homogeneity.
S A, Rosenfeld   +6 more
openaire   +2 more sources

Matrix Metalloproteinase-3 Gene Polymorphisms Are Associated with Ischemic Stroke

Journal of Interferon & Cytokine Research, 2012
Stroke is a heterogeneous disease caused by different pathogenic mechanisms. Several candidate genes for stroke have been proposed, but few have been replicated. Matrix metalloproteinases (MMPs) are expressed following stroke. We investigated the association of single nucleotide polymorphisms (SNPs) of the MMP3 gene with stroke in the Korean population.
Su Kang, Kim   +5 more
openaire   +2 more sources

An Aberrant Cerebellar Development in Mice Lacking Matrix Metalloproteinase-3

Molecular Neurobiology, 2011
Cell-cell and cell-matrix interactions are necessary for neuronal patterning and brain wiring during development. Matrix metalloproteinases (MMPs) are proteolytic enzymes capable of remodelling the pericellular environment and regulating signaling pathways through cleavage of a large degradome. MMPs have been suggested to affect cerebellar development,
Inge, Van Hove   +8 more
openaire   +2 more sources

Role of matrix metalloproteinase-3 in neurodegeneration.

Journal of neurochemistry, 2013
Matrix metalloproteinase-3 (MMP-3) is a member of the class of zinc-dependent proteases known to degrade the extracellular matrix. MMP-3 activity is regulated at three different levels: gene expression, proteolytic activation of the zymogen, and inhibition by the endogenous tissue inhibitors of metalloproteinase.
Eun-Mee, Kim, Onyou, Hwang
openaire   +1 more source

Serum matrix metalloproteinase-3 levels are elevated in myasthenia gravis

Journal of Neuroimmunology, 2008
MMP-3 is capable of degrading a variety of proteins, including agrin, which plays a critical role in neuromuscular signalling by controlling acetylcholine receptor clustering. The degradation of agrin by MMP-3 may disrupt the neuromuscular junction leading to a failure of neuromuscular transmission and muscle weakness.
Fredrik R, Romi   +2 more
openaire   +2 more sources

Association between matrix metalloproteinase-3 gene polymorphism and moyamoya disease

Journal of Clinical Neuroscience, 2015
Genetic factors play an important role in the etiology and pathogenesis of moyamoya disease (MMD). Recently, several studies suggested the decreased expression of matrix metalloproteinase-3 (MMP3) was associated with an increased risk of MMD. This case-control study was performed to examine the association between MMP3 polymorphisms and the risk of MMD,
Junpeng, Ma, Chao, You
openaire   +2 more sources

The biofilm matrix: multitasking in a shared space

Nature Reviews Microbiology, 2022
Hans-Curt Flemming   +2 more
exaly  

AB1053 MATRIX METALLOPROTEINASE-3: A BIOMARKER OF SPONDYLOARTHRITIS

Scientific Abstracts, 2023
M. Slouma   +8 more
openaire   +1 more source

Extracellular vesicle–matrix interactions

Nature Reviews Materials, 2023
, Jae-won Shin
exaly  

Membrane-type matrix metalloproteinase 3

2004
Motoharu Seiki, Hiroyuki Nakamura
openaire   +1 more source

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