Probing the efficiency of proteolytic events by positional proteomics.
about
Granzyme B inhibits vaccinia virus production through proteolytic cleavage of eukaryotic initiation factor 4 gamma 3Protease signalling: the cutting edgeQuantitative proteomics and terminomics to elucidate the role of ubiquitination and proteolysis in adaptive immunityHuman and mouse granzyme M display divergent and species-specific substrate specificities.A subset of membrane-altering agents and γ-secretase modulators provoke nonsubstrate cleavage by rhomboid proteasesImportance of extended protease substrate recognition motifs in steering BNIP-2 cleavage by human and mouse granzymes B.Targeting proteases in cardiovascular diseases by mass spectrometry-based proteomics.Profiling protease activities by dynamic proteomics workflows.Unbiased selective isolation of protein N-terminal peptides from complex proteome samples using phospho tagging (PTAG) and TiO(2)-based depletionTime-resolved analysis of the matrix metalloproteinase 10 substrate degradome.Natural substrates of plant proteases: how can protease degradomics extend our knowledge?Proteomic identification of protease cleavage sites: cell-biological and biomedical applications.Blessing or curse? Proteomics in granzyme research.Proteomic Identification of Cysteine Cathepsin Substrates Shed from the Surface of Cancer Cells.The application of terminomics for the identification of protein start sites and proteoforms in bacteria.Identification of Serpinb6b as a species-specific mouse granzyme A inhibitor suggests functional divergence between human and mouse granzyme A.All human granzymes target hnRNP K that is essential for tumor cell viability.Selecting protein N-terminal peptides by combined fractional diagonal chromatography.
P2860
Q21559400-F3FB5048-5447-4348-B079-9CCCF69C83BFQ26852301-C5AC13AA-3F0C-48DE-BE79-6239DED4DD96Q28069531-BF2BAD76-BC05-4820-A750-06461887CF21Q33896439-C92C459F-965F-47F9-BC72-0E7057CA8332Q35054154-298DD3D8-8DA1-40A6-95B0-CEE763669A4BQ35246562-3E6005B8-E8B3-4210-A82E-EBC0B301D898Q35897743-392DBE1C-D5B6-4175-92A2-EDCF4E335E32Q36199807-87C54286-3560-4849-B384-28882FB80428Q36211839-D3D2BA78-265C-45C0-866F-49DE4B335D05Q37563920-601C78DE-2FEF-4BCF-9BBD-2A6EA0AAB3AEQ37946960-C221E222-1758-4628-9AD1-E1C38348D2D7Q38151761-A1AD06C7-6798-4DF3-94BC-114989D73EE4Q38200060-5B771CB3-F25A-4925-8BA6-DED4C273220FQ38409707-8E0A13AE-B26D-4849-AD4E-452AC918980FQ38600690-6852D7C0-ACDB-424F-86D5-BE95912B6B29Q38656362-9B893B46-689E-4A74-AF1F-DB9E3153300BQ41819977-E7B158ED-0CFE-4A18-8189-CDA3FB438039Q49052034-22558BF5-8ABD-4D3E-952B-AF7987F1765A
P2860
Probing the efficiency of proteolytic events by positional proteomics.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Probing the efficiency of proteolytic events by positional proteomics.
@en
type
label
Probing the efficiency of proteolytic events by positional proteomics.
@en
prefLabel
Probing the efficiency of proteolytic events by positional proteomics.
@en
P2093
P2860
P356
P1476
Probing the efficiency of proteolytic events by positional proteomics.
@en
P2093
Dion Kaiserman
Francis Impens
Joël Vandekerckhove
Kenny Helsens
Kim Plasman
Kimberly Demeyer
Kris Gevaert
Marc Goethals
P2860
P304
M110.003301
P356
10.1074/MCP.M110.003301
P577
2010-11-03T00:00:00Z