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Proteomicsintracellular MMP-2 proteolysis in cardiac tissue
Induced proteolysis of rat heart extracts with recombinant MMP-2 followed by subtiligase-N-terminomics
ORGANISM(S): Rattus (ncbitaxon:10114) 
2023-11-01 | MSV000093229 | MassIVE
ProteomicsProteomic mapping of MYHCA cleavage sites by MMP-2
Myosin S1(S1) fragments were incubated with full-length MMP-2, the catalytic domain of MMP-2, or APMA activated MMP-2 under similar conditions. Samples were collected at 5 min, 30 min, 1 h, 4 h, and 8 h time intervals (Supplementary file 6).
ORGANISM(S): Oryctolagus Cuniculus (ncbitaxon:9986) 
2025-06-17 | MSV000098239 | MassIVE
TranscriptomicsGene expression profiles using microarrays in mdx and mdx/MMP-2-/- mice at 1 and 3 months of age
Matrix metalloprotease (MMP) -2 has been reported to be up-regulated in skeletal muscle in the lethal X-linked muscle disorder Duchenne muscular dystrophy (DMD), which is caused by loss of dystrophin. However, the role of MMP-2 in dystrophin-deficient muscle is not well known. The aim of this study ...
ORGANISM(S): Mus musculus 
2011-02-19 | E-GEOD-27129 | biostudies-arrayexpress
TranscriptomicsWhole genome expression signature of SWCNT and MWCNT vs. asbestos subchronic exposures to human pleural mesothelial cells
Malignant mesothelioma is one of the most aggressive forms of cancer known. Recent studies have shown that carbon nanotubes (CNTs) are biopersistent and induce mesothelioma in animals, but the underlying mechanisms are not known. Here, we investigate the effect of long-term exposure to CNTs on the a...
ORGANISM(S): Homo sapiens 
2015-11-23 | E-GEOD-48855 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of mouse C57Bl6 MMP-7 and MMP-10 deficient mice Pseudomonas aeruginosa exposed airway epithelium.
Airway epithelium is the initial point of host-pathogen interaction in Pseudomonas aeruginosa infection, an important pathogen in cystic fibrosis and nosocomial pneumonia. We used global gene expression analysis to determine airway epithelial transcriptional responses dependent on matrilysin (MMP-7)...
ORGANISM(S): Mus musculus 
2008-06-15 | E-GEOD-7957 | biostudies-arrayexpress
ModelsKaragiannis2004_CollagenIproteolysis
This a model from the article: A theoretical model of type I collagen proteolysis by matrix metalloproteinase (MMP) 2 and membrane type 1 MMP in the presence of tissue inhibitor of metalloproteinase 2. Karagiannis ED, Popel AS. J Biol Chem 2004 Sep 10;...
2005-01-01 | MODEL0911270007 | BioModels
TranscriptomicsGene expression profiles using microarrays in mdx and mdx/MMP-2-/- mice at 1 and 3 months of age
Matrix metalloprotease (MMP) -2 has been reported to be up-regulated in skeletal muscle in the lethal X-linked muscle disorder Duchenne muscular dystrophy (DMD), which is caused by loss of dystrophin. However, the role of MMP-2 in dystrophin-deficient muscle is not well known. The aim of this study ...
ORGANISM(S): Mus musculus 
2011-02-19 | GSE27129 | GEO
ProteomicsMulti-layered proteomic analysis for colorectal cancer
Matrix metalloproteinase-2 (MMP-2) plays a role in cell migration and invasion that involve degradation of extracellular matrix proteins as well as vascular remodeling. Increased expression of MMP-2 has often been observed in the tumors of colorectal cancer (CRC) patients. In order to unveil the per...
ORGANISM(S): Homo sapiens (Human) 
2021-08-26 | PXD018304 | Pride
Mmp-2 Silac Plasma Label-free Focal adhesion kinase Secretome Colorectal cancer 
TranscriptomicsUpregulation of Expression of Matrix Metalloproteinases in Alveolar Macrophages of HIV1+ Smokers with Early Emphysema
HIV1+ smokers develop emphysema at an earlier age and with a higher incidence than HIV1- smokers. Based on the knowledge that human alveolar macrophages (AM) are capable of producing proteases that degrade extracellular matrix components, we hypothesized that upregulation of AM matrix metalloprotein...
ORGANISM(S): Homo sapiens 
2016-03-24 | E-GEOD-10038 | biostudies-arrayexpress
GenomicsThe MMP-2 histone H3 N-terminal tail protease is selectively targeted to the transcription start sites of active genes [RNA-seq]
The MMP-2 histone H3 N-terminal tail protease is selectively targeted to the transcription start sites of active genes [RNA-seq]
PRJNA934554 | ENA
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