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Secreted proteases act on interstitial tissue secretomes released from multiple cell types. Thus, substrate proteins might be part of higher molecular complexes constituted by many proteins with diverse and potentially unknown cellular origin. In cell culture these might be reconstituted by mixing n...
ORGANISM(S): Mus musculus (Mouse) 
2015-05-11 | PXD001643 | Pride
We report the targeted analysis of the human dental pulp proteome and N-terminome using the positional proteomics technique TAILS, which allowed us to capture both naturally blocked and unblocked protein N-termini. Furthermore, by using a proteomically barely studied human tissue in combination with...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2018-06-26 | MSV000082509 | MassIVE
Aberrant proteolysis by cysteine cathepsins is implicated in carcinogenesis, but knowledge of cathepsin substrates mediating tumor-promoting or suppressing effects is limited. Here we characterize tumor proteome and in vivo cathepsin substrates using cathepsin knockout mice and the RIP1-Tag2 model o...
ORGANISM(S): Mus musculus (Mouse) 
2016-08-08 | PXD003637 | Pride
Dysregulated protease activity is often implicated in the initiation of inflammation and immune cell recruitment in gastrointestinal inflammatory diseases. Using N-terminomics/TAILS (terminal amine isotopic labeling of substrates), we compared proteases, along with their substrates and inhibitors, b...
ORGANISM(S): Homo sapiens (Human) 
2019-09-08 | PXD014479 | Pride
Development of a degradomics strategy which combines the isolation of mitochondria (surfactants-based method) with the dimethylation-TAILS protocol for N-terminome enrichment.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-05-17 | MSV000083795 | MassIVE
MacDonald BT, Keshishian H, Mundorff CC, Arduini A, Lai D, Bendinelli K, Popp NR, Bhandary B, Clauser KR, Specht H, Elowe NH, Laprise D, Xing Y, Kaushik VK, Carr SA, Ellinor PT. Loss-of-function mutations in the secreted enzyme ADAMTS7 (a disintegrin and metalloproteinase with thrombospondin motifs ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-12-03 | MSV000088508 | MassIVE
Mito-TAILS N-terminomics analysis of proteolytic events during EPEC infection of human epithelial cells, on whole-cell level and mitochondria.
ORGANISM(S): Homo sapiens (Human) 
2020-05-21 | PXD016994 | Pride
We report the targeted analysis of the human dental pulp proteome and N-terminome using the positional proteomics technique TAILS, which allowed us to capture both naturally blocked and unblocked protein N-termini. Furthermore, by using a proteomically barely studied human tissue in combination with...
ORGANISM(S): Homo sapiens (Human) 
2015-08-18 | PXD002264 | Pride
We report the targeted analysis of the human dental pulp stroma and the odontoblast layer using the positional proteomics technique TAILS N-terminomics, which allowed us to capture both naturally blocked and unblocked protein N-termini, and to identify differences between e.g. the dental pulp proteo...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-06-10 | MSV000083951 | MassIVE
Poly(A) tails enhance the stability and translation of most eukaryotic messenger RNAs, but difficulties in globally measuring poly(A)-tail lengths have impeded greater understanding of poly(A)-tail function. Here we describe poly(A)-tail length profiling by sequencing (PAL-seq) and apply it to measu...
ORGANISM(S): Arabidopsis thaliana 
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