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ProteomicsComputational design of Matrix Metalloprotenaise-9 (MMP-9) resistant to auto-cleavage
Matrix metalloproteinase-9 (MMP-9) is an endopeptidase that remodels the extracellular matrix and has been implicated as a major driver in cancer metastasis. Hence, there is a high demand for MMP-9 inhibitors for therapeutic purposes. For such drug design efforts, large amounts of MMP-9 are required...
ORGANISM(S): Escherichia coli 
2023-10-24 | PXD041767 | Pride
Mmp-9 Auto-cleavage Protein engineering Auto-degradation Enzyme engineering Matrix metalloproteases 
UnknownComputational design of matrix metalloprotenaise-9 (MMP-9) resistant to auto-cleavage.
Not available
S-EPMC10422929 | biostudies-literature
UnknownComputational design of Matrix Metalloprotenaise-9 (MMP-9) resistant to auto-cleavage.
Not available
S-EPMC10120622 | biostudies-literature
UnknownCaspase-8 auto-cleavage regulates programmed cell death and collaborates with RIPK3/MLKL to prevent lymphopenia.
Not available
S-EPMC9345959 | biostudies-literature
UnknownTwo Antagonistic MALT1 Auto-Cleavage Mechanisms Reveal a Role for TRAF6 to Unleash MALT1 Activation.
Not available
S-EPMC5214165 | biostudies-literature
UnknownBacteriophage GIL01 gp7 interacts with host LexA repressor to enhance DNA binding and inhibit RecA-mediated auto-cleavage.
Not available
S-EPMC4551915 | biostudies-literature
UnknownFADD cleavage by NK cell granzyme M enhances its self-association to facilitate procaspase-8 recruitment for auto-processing leading to caspase cascade.
Not available
S-EPMC3307975 | biostudies-literature
UnknownOxidative Cleavage and Ammoxidation of Unsaturated Hydrocarbons via Heterogeneous Auto-Tandem Catalysis
Not available
S-EPMC9975833 | biostudies-literature
TranscriptomicsTranscriptome analysis of Jurkat T cells expressing MALT1 or its mutants MALT1-R149A and MALT1-C464A or the MALT1-R149A-C464A double mutant.
Purpose: study the role of MALT1 auto-proteolysis in T cell receptor mediated activation of NF-kB. Methods: Jurkat cells were generated that express wild type MALT1, the auto-cleavage deficient MALT1-R149A mutant, the catalytic inactive MALT1-C464A mutant or the R149A-C464A double mutant (RACA). Exp...
ORGANISM(S): Homo sapiens 
2014-11-28 | GSE52934 | GEO
UnknownFunctional mechanism and pathogenic potential of MYRF ICA domain mutations implicated in birth defects.
Not available
S-EPMC6972908 | biostudies-literature
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