Analysis of protein processing by N-terminal proteomics reveals novel species-specific substrate determinants of granzyme B orthologs. - Wikidata - wikimedia - TriplyDB

Analysis of protein processing by N-terminal proteomics reveals novel species-specific substrate determinants of granzyme B orthologs.

Analysis of protein processing by N-terminal proteomics reveals novel species-specific substrate determinants of granzyme B orthologs.

http://www.wikidata.org/entity/Q39932401

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Granzyme B cleavage of autoantigens in autoimmunity Protease signalling: the cutting edge Distinct peripheral blood RNA responses to Salmonella in pigs differing in Salmonella shedding levels: intersection of IFNG, TLR and miRNA pathways Structure of granzyme C reveals an unusual mechanism of protease autoinhibition Quantitative proteomics and terminomics to elucidate the role of ubiquitination and proteolysis in adaptive immunity Leukocyte protease binding to nucleic acids promotes nuclear localization and cleavage of nucleic acid binding proteins Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster Proteome-wide substrate analysis indicates substrate exclusion as a mechanism to generate caspase-7 versus caspase-3 specificity Proteome analysis of distinct developmental stages of human natural killer (NK) cells The Online Protein Processing Resource (TOPPR): a database and analysis platform for protein processing events Granzyme B cleaves decorin, biglycan and soluble betaglycan, releasing active transforming growth factor-β1 Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics Structural determinants of limited proteolysis.Determinants of Macromolecular Specificity from Proteomics-Derived Peptide Substrate Data.N-terminal proteomics and ribosome profiling provide a comprehensive view of the alternative translation initiation landscape in mice and men In vitro and in vivo protein-bound tyrosine nitration characterized by diagonal chromatography A statistics-based platform for quantitative N-terminome analysis and identification of protease cleavage products High affinity small protein inhibitors of human chymotrypsin C (CTRC) selected by phage display reveal unusual preference for P4' acidic residues.Human and mouse granzyme M display divergent and species-specific substrate specificities.Granzyme B-induced and caspase 3-dependent cleavage of gelsolin by mouse cytotoxic T cells modifies cytoskeleton dynamics.Prediction of protease substrates using sequence and structure features.In silico prediction of the granzyme B degradome PROSPER: an integrated feature-based tool for predicting protease substrate cleavage sites.Comprehensive quantitative analysis of ovarian and breast cancer tumor peptidomes.Importance of extended protease substrate recognition motifs in steering BNIP-2 cleavage by human and mouse granzymes B.Profiling protease activities by dynamic proteomics workflows.Epitelial-to-mesenchimal transition and invasion are upmodulated by tumor-expressed granzyme B and inhibited by docosahexaenoic acid in human colorectal cancer cells.Single-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme access Conservation of the extended substrate specificity profiles among homologous granzymes across species.Methods for the proteomic identification of protease substrates.A large and accurate collection of peptidase cleavages in the MEROPS database.Interactome disassembly during apoptosis occurs independent of caspase cleavage.MS-driven protease substrate degradomics.Functional dissection of the granzyme family: cell death and inflammation.Orphan granzymes find a home.Bioinformatic approaches for predicting substrates of proteases.Cell death-independent functions of granzymes: hit viruses where it hurts.Dissecting cell death with proteomic scalpels.Proteomic identification of protease cleavage sites: cell-biological and biomedical applications.Blessing or curse? Proteomics in granzyme research.

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P2860

Analysis of protein processing by N-terminal proteomics reveals novel species-specific substrate determinants of granzyme B orthologs.

http://www.wikidata.org/entity/Q39932401

description

2008 nî lūn-bûn

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name

Analysis of protein processing ...... nants of granzyme B orthologs.

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Analysis of protein processing ...... nants of granzyme B orthologs.

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Analysis of protein processing ...... nants of granzyme B orthologs.

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Analysis of protein processing ...... nants of granzyme B orthologs.

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Analysis of protein processing ...... nants of granzyme B orthologs.

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Analysis of protein processing ...... nants of granzyme B orthologs.

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Molecular & Cellular Proteomics

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Analysis of protein processing ...... nants of granzyme B orthologs.

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P2093

Evy Timmerman

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Frederic Rousseau

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Joost Van Durme

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Joël Vandekerckhove

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Kim Plasman

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Kris Gevaert

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Marc Goethals

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Niklaas Colaert

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P2860

Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides

The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools

Proteome-wide Identification of HtrA2/Omi Substrates

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Granzyme H destroys the function of critical adenoviral proteins required for viral DNA replication and granzyme B inhibition

The major human and mouse granzymes are structurally and functionally divergent

Refinement and prediction of protein prenylation motifs

The structure of the pro-apoptotic protease granzyme B reveals the molecular determinants of its specificity

The three-dimensional structure of human granzyme B compared to caspase-3, key mediators of cell death with cleavage specificity for aspartic acid in P1

The oligomeric structure of human granzyme A is a determinant of its extended substrate specificity

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258-272

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2

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23300698

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