Sort   by:  
 Page size 
GenomicsResistance to PD1 blockade in the absence of metalloprotease-mediated LAG3 shedding
Resistance to PD1 blockade in the absence of metalloprotease-mediated LAG3 shedding
PRJNA634347 | ENA
ProteomicsProteolytic processing of CD99
The adhesion molecule CD99 is essential for transendothelial migration (TEM) of leukocytes. Here we demonstrate by biochemical and cellular assays that CD99 undergoes ectodomain shedding by the metalloprotease meprin ? and subsequent intramembrane proteolysis by ?-secretase. The cleavage site in CD9...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080746 | MassIVE
ProteomicsMetalloprotease SPRTN/DVC1 Orchestrates Replication-Coupled DNA-Protein Crosslink Removal
Cytotoxicity of DNA-protein crosslinks (DPCs) is ascribed largely to their ability to block the progression of DNA replication fork. DPCs are frequently occurring in cells, either as a consequence of metabolism or exogenous agents. The mechanism of DPCs removal is not completely understood. Here, we...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080743 | MassIVE
GenomicsTranscriptomics insights into the functional role of tick Ixodes ricinus midgut proteins metalloprotease and antigen p23
Transcriptomics insights into the functional role of tick Ixodes ricinus midgut proteins metalloprotease and antigen p23
PRJNA1232073 | ENA
ProteomicsMetalloprotease-mediated cleavage of CD95 Ligand: QTOF Xevo XS data
CD95 is a member of the TNF receptor superfamily that is ubiquitously expressed in healthy and pathological tissues. Stimulation of CD95 by its physiological ligand CD95L induces its oligomerization leading in turn to the transduction of either apoptotic or non-apoptotic signals. CD95L can exist as ...
ORGANISM(S): Homo sapiens (Human) 
2023-02-20 | PXD039211 | Pride
Cd95l Metalloprotease Proteolytic cleavage 
ProteomicsCleavage preference of metalloprotease EA1
The cleavage preference of the thermophilic metalloprotease from Geobacillus sp. EA1 was characterised using mass spectrometry, confirming its similarity to thermolysin in preferring P1’ hydrophobic amino acids. While EA1 showed similar efficiencies for cleavage of short peptides with one of six hyd...
ORGANISM(S): Escherichia coli Geobacillus sp. EFT1 Bacillus thermoproteolyticus 
2025-11-25 | PXD064530 | Pride
Protease cleavage assay Thermolysin Itraq 
TranscriptomicsResistance to PD1 blockade in the absence of metalloprotease-mediated LAG3 shedding
Mechanisms of resistance to cancer immunotherapy remain poorly understood. Lymphocyte Activation Gene-3 (LAG3) signaling is regulated by A Disintegrin And Metalloprotease-10 (ADAM10) and ADAM17-mediated cell surface shedding. We developed and utilized mutant mice expressing a metalloprotease-resista...
ORGANISM(S): Mus musculus 
2020-05-22 | GSE150991 | GEO
ProteomicsBroad-range metalloprotease profiling in plants uncovers immunity provided by defence-related metalloenzyme
Plants encode for >100 metalloproteases representing >19 different protein families. Tools to study this large and diverse class of proteases have not yet been introduced into plant science. Here, we used hydroxamate-based photoaffinity probes to explore plant proteomes for metalloproteases. We dete...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) Nicotiana benthamiana 
2022-08-12 | PXD032265 | Pride
Photoaffinity labelling Arabidopsis Prp27 Metalloproteases Immunity 
ProteomicsStructure-guided mutagenesis of a mucin-selective metalloprotease from Akkermansia muciniphila alters substrate preferences
Akkermansia muciniphila, a mucin-degrading microbe found in the human gut, is often associated with positive health outcomes. The abundance of Akkermansia muciniphila is modulated by the presence and accessibility of nutrients, which can be derived from diet or host glycoproteins. In particular, the...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2022-06-09 | PXD032164 | Pride
X-ray crystallography Mucin Mucinase Microbiome O-glycosylation Molecular docking Enzyme structure Metalloprotease 
TranscriptomicsTranscriptomics insights into the functional role of tick Ixodes ricinus midgut proteins metalloprotease and antigen p23
Ticks are hematophagous ectoparasites that impact human and animal health worldwide. Tick saliva contains multiple biomolecules capable of disrupting host immunity, occasionally causing emergent tick-borne allergies like the alpha-Gal syndrome (AGS). Current results highlight a knowledge gap in char...
ORGANISM(S): Ixodes ricinus 
2025-11-04 | GSE291137 | GEO
Sort   by:  
 Page size