GrM - Human and mouse granzyme M display divergent and species-specific substrate specificities
Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap, instrument model
SUBMITTER: 
Petra Van Damme
PROVIDER: PRD000347 | Pride | 2012-05-23
REPOSITORIES: pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| PRIDE_Exp_Complete_Ac_15475.pride.mgf.gz | Mgf | |||
| PRIDE_Exp_Complete_Ac_15475.pride.mztab.gz | Mztab | |||
| PRIDE_Exp_Complete_Ac_15475.xml.gz | Xml |
Items per page: 5 1 - 3 of 3 |
Publications
Human and mouse granzyme M display divergent and species-specific substrate specificities.
de Poot Stefanie A H SA Westgeest Marijn M Hostetter Daniel R DR Van Damme Petra P Plasman Kim K Demeyer Kimberly K Broekhuizen Roel R Gevaert Kris K Craik Charles S CS Bovenschen Niels N
The Biochemical journal 20110801 3
Cytotoxic lymphocyte protease GrM (granzyme M) is a potent inducer of tumour cell death and a key regulator of inflammation. Although hGrM (human GrM) and mGrM (mouse GrM) display extensive sequence homology, the substrate specificity of mGrM remains unknown. In the present study, we show that hGrM and mGrM have diverged during evolution. Positional scanning libraries of tetrapeptide substrates revealed that mGrM is preferred to cleave after a methionine residue, whereas hGrM clearly favours a l ...[more]
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