Sort   by:  
 Page size 
Complementary positional proteomics of human and mouse granzyme M treated K-562 lysates
2012-05-23 | PRD000347 | Pride
Elucidating the true physiological functions of granzymes has been challenging since the origin of the granzyme studied, the use of non-physiological granzyme concentrations and the interspecies use of granzymes, with extrapolation of all these data to orthologous granzymes has led to inconsistencie...
ORGANISM(S): Homo sapiens (Human) 
2015-09-30 | PXD000570 | Pride
Background. Dendritic cell (DC)-based neoantigen vaccination holds potential as a safe and effective adjuvant therapy for patients with early-stage, resectable NSCLC, a tumor type typically characterized by high mutational loads. DCs have the unique ability to elicit robust antitumoral T-cell respon...
ORGANISM(S): Homo sapiens (Human) 
2024-03-17 | PXD044799 | Pride
Despite its growing popularity and use, bottom-up proteomics remains a complex analytical methodology. Its general workflow consists of three main steps: sample preparation, liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) and computational data analysis. Quality assessment of th...
ORGANISM(S): Homo sapiens (Human) 
2020-07-28 | PXD014524 | Pride
Cytotoxic lymphocyte protease granzyme M (GrM) is a potent inducer of tumor cell death in vitro and in vivo. The apoptotic phenotype and mechanism by which it induces cell death however, remain poorly understood and controversial. Here, we show that GrM-induced cell death was largely caspase-depende...
ORGANISM(S): Homo sapiens (Human) 
2013-11-27 | PXD000252 | Pride
Granzymes are a family of structurally related serine proteases involved in immunity. To date four out of five human granzymes have been assigned orthologues in mice; however for granzyme H, no clear murine orthologue has been suggested and its role in cytotoxicity remains controversial. In this stu...
ORGANISM(S): Mus musculus (Mouse) 
2013-11-27 | PXD000152 | Pride
Sort   by:  
 Page size