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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
TranscriptomicsProteolytic inactivation of the autoinhibitory prodomain is essential for the pro-tumorigenic function of membrane type-1 matrix metalloproteinase (MT1-MMP)
Invasive cancers employ pericellular proteolysis to breach the extracellular matrix and basement membrane barriers and invade the surrounding tissue. Pro-invasive, pro-tumorigenic MT1-MMP is the primary mediator of proteolytic events on the cancer cell surface. Cellular MT1-MMP is synthesized as a l...
ORGANISM(S): Homo sapiens 
2011-06-01 | E-GEOD-28655 | biostudies-arrayexpress
TranscriptomicsMulti-component epigenetic control of pro-invasive genes in cancer cells (miRNA)
To identify the epigenetic signature that controls cancer cell migration, we performed integrated gene expression, miRNA and epigenetic profiling of 486 selected invasion-associated genes in non-migratory MCF-7 breast carcinoma and highly migratory U251 glioma cells. We used a custom-built chromatin...
ORGANISM(S): Homo sapiens 
2010-01-05 | E-GEOD-18894 | biostudies-arrayexpress
ProteomicsTissue protease activity with MALDI MSI
Aberrant protease activity has been implicated in the etiology of various prevalent diseases including neurodegeneration and cancer, in particular metastasis. Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry imaging (MSI) has recently been established as a key technology for bio...
ORGANISM(S): Bos Taurus (ncbitaxon:9913) Mus Musculus (ncbitaxon:10090) 
MSV000086102 | MassIVE
ProteomicsRepurposing E3 ubiquitin ligases as cell surface protein degraders using Proteolysis Targeting Antibodies
The majority of current therapeutics targeting plasma membrane receptors function by antagonizing ligand binding or enzymatic activities. Typical mammalian proteins, however, consist of multiple domains executing discrete but coordinated activities, and saturating inhibition of one functional domain...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-05-25 | MSV000089542 | MassIVE
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
UnknownIn situ proteolysis of the Vibrio cholerae matrix protein RbmA promotes biofilm recruitment.
Not available
S-EPMC4547210 | biostudies-literature
ProteomicsExtracellular matrix proteolysis maintains synaptic plasticity during brain development
Synapses are highly dynamic during early brain development, enabling the rapid adaptations that occur as neural circuits remodel in response to experience. The extracellular matrix (ECM) has been proposed as a critical regulator of synaptic plasticity in the brain. However, the molecular mechanisms ...
ORGANISM(S): Homo sapiens (Human) 
2026-03-16 | PXD060477 | Pride
Synaptic plasticity Synapse Extracellular matrix Brain development 
ProteomicsDistinct Combinatorial Cascade of Events Generated by ECM Proteolysis Dictates Cell Behavior
It is well established that the expression profiles of multiple and possibly redundant matrix remodeling proteases (e.g. collagenases) strongly differentiates in disease and development. Although enzymatic redundancy might be inferred from their close similarity in structure, their in-vivo activity ...
ORGANISM(S): Rattus norvegicus (Rat) 
2016-09-27 | PXD003553 | Pride
Proteomics Metalloproteinase Ecm 
ProteomicsDistinct Combinatorial Cascade of Events Generated by ECM Proteolysis Dictates Cell Behavior, part 2
It is well established that the expression profiles of multiple and possibly redundant matrix remodeling proteases (e.g. collagenases) strongly differentiates in disease and development. Although enzymatic redundancy might be inferred from their close similarity in structure, their in-vivo activity ...
ORGANISM(S): Rattus norvegicus (Rat) 
2016-09-27 | PXD003796 | Pride
Proteomics Ecm 
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