Results 271 to 280 of about 240,479 (306)
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Production of human matrix metalloproteinase 3 (stromelysin) in Escherichia coli
Gene, 1994Full-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
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Matrix Metalloproteinase-3 Gene Polymorphisms Are Associated with Ischemic Stroke
Journal of Interferon & Cytokine Research, 2012Stroke 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
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An Aberrant Cerebellar Development in Mice Lacking Matrix Metalloproteinase-3
Molecular Neurobiology, 2011Cell-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
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Role of matrix metalloproteinase-3 in neurodegeneration.
Journal of neurochemistry, 2013Matrix 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
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Serum matrix metalloproteinase-3 levels are elevated in myasthenia gravis
Journal of Neuroimmunology, 2008MMP-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
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Association between matrix metalloproteinase-3 gene polymorphism and moyamoya disease
Journal of Clinical Neuroscience, 2015Genetic 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
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The biofilm matrix: multitasking in a shared space
Nature Reviews Microbiology, 2022Hans-Curt Flemming +2 more
exaly
AB1053 MATRIX METALLOPROTEINASE-3: A BIOMARKER OF SPONDYLOARTHRITIS
Scientific Abstracts, 2023M. Slouma +8 more
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Membrane-type matrix metalloproteinase 3
2004Motoharu Seiki, Hiroyuki Nakamura
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