A quantitative proteomics design for systematic identification of protease cleavage events.
about
Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo.Mapping proteolytic processing in the secretome of gastric cancer-associated myofibroblasts reveals activation of MMP-1, MMP-2, and MMP-3The Online Protein Processing Resource (TOPPR): a database and analysis platform for protein processing eventsN-terminal proteomics and ribosome profiling provide a comprehensive view of the alternative translation initiation landscape in mice and menGlobal identification of peptidase specificity by multiplex substrate profiling.Proteolytic characteristics of cathepsin D related to the recognition and cleavage of its target proteins.Recognition of higher order patterns in proteins: immunologic kernels.Global profiling of proteolysis during rupture of Plasmodium falciparum from the host erythrocyte.A bead-based cleavage method for large-scale identification of protease substrates.The Apaf-1-binding protein Aven is cleaved by Cathepsin D to unleash its anti-apoptotic potentialSampling From the Proteome to the Human Leukocyte Antigen-DR (HLA-DR) Ligandome Proceeds Via High SpecificityResin-assisted enrichment of N-terminal peptides for characterizing proteolytic processing.A limit to the divergent allele advantage model supported by variable pathogen recognition across HLA-DRB1 allele lineages.Mass spectrometry-based proteomics strategies for protease cleavage site identification.A review on recent developments in mass spectrometry instrumentation and quantitative tools advancing bacterial proteomics.Proteomic identification of protease cleavage sites: cell-biological and biomedical applications.Proteomic Identification of Cysteine Cathepsin Substrates Shed from the Surface of Cancer Cells.Fast profiling of protease specificity reveals similar substrate specificities for cathepsins K, L and S.Peptidase specificity from the substrate cleavage collection in the MEROPS database and a tool to measure cleavage site conservation.Procathepsin E is highly abundant but minimally active in pancreatic ductal adenocarcinoma tumors.Overexpression of Cathepsin E Interferes with Neuronal Differentiation of P19 Embryonal Teratocarcinoma Cells by Degradation of N-cadherin.Protein C-terminal enzymatic labeling identifies novel caspase cleavages during the apoptosis of multiple myeloma cells induced by kinase inhibition.Metacaspases versus caspases in development and cell fate regulation.A SILAC-based approach identifies substrates of caspase-dependent cleavage upon TRAIL-induced apoptosis.Degradomics reveals that cleavage specificity profiles of caspase-2 and effector caspases are alike.Cacidases: caspases can cleave after aspartate, glutamate and phosphoserine residues.Global Protease Activity Profiling Provides Differential Diagnosis of Pancreatic Cysts.Selecting protein N-terminal peptides by combined fractional diagonal chromatography.Protease Substrate Profiling by N-Terminal COFRADIC.ProC-TEL: Profiling of Protein C-Termini by Enzymatic Labeling.Synthesis and in vitro biochemical evaluation of oxime bond-linked daunorubicin-GnRH-III conjugates developed for targeted drug delivery.
P2860
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P2860
A quantitative proteomics design for systematic identification of protease cleavage events.
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
A quantitative proteomics desi ...... n of protease cleavage events.
@en
type
label
A quantitative proteomics desi ...... n of protease cleavage events.
@en
prefLabel
A quantitative proteomics desi ...... n of protease cleavage events.
@en
P2093
P2860
P356
P1476
A quantitative proteomics desi ...... on of protease cleavage events
@en
P2093
Bart Ghesquière
Evy Timmerman
Francis Impens
Joël Vandekerckhove
Kenny Helsens
Kris Gevaert
Niklaas Colaert
Pieter-Jan De Bock
P2860
P304
P356
10.1074/MCP.M110.001271
P50
P577
2010-07-13T00:00:00Z