Quantitative phosphokinome analysis of the Met pathway activated by the invasin internalin B from Listeria monocytogenes. - Wikidata - awgldk - TriplyDB

Quantitative phosphokinome analysis of the Met pathway activated by the invasin internalin B from Listeria monocytogenes.

Quantitative phosphokinome analysis of the Met pathway activated by the invasin internalin B from Listeria monocytogenes.

http://www.wikidata.org/entity/Q33628918

about

Kinome analysis of receptor-induced phosphorylation in human natural killer cells First insight into the kinome of human regulatory T cells.Exploitation of the ubiquitin system by invading bacteria Host Serine/Threonine Kinases mTOR and Protein Kinase C-α Promote InlB-Mediated Entry of Listeria monocytogenes.TCR signalling network organization at the immunological synapses of murine regulatory T cells.Analysis of differentially expressed proteins in Yersinia enterocolitica-infected HeLa cells.Chronic Toxoplasma infection is associated with distinct alterations in the synaptic protein composition

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P2860

Quantitative phosphokinome analysis of the Met pathway activated by the invasin internalin B from Listeria monocytogenes.

http://www.wikidata.org/entity/Q33628918

description

2009 nî lūn-bûn

@nan

2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Quantitative phosphokinome ana ...... B from Listeria monocytogenes.

@ast

Quantitative phosphokinome ana ...... B from Listeria monocytogenes.

@en

type

label

Quantitative phosphokinome ana ...... B from Listeria monocytogenes.

@ast

Quantitative phosphokinome ana ...... B from Listeria monocytogenes.

@en

prefLabel

Quantitative phosphokinome ana ...... B from Listeria monocytogenes.

@ast

Quantitative phosphokinome ana ...... B from Listeria monocytogenes.

@en

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MCP.M800521-MCP200

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Molecular & Cellular Proteomics

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Quantitative phosphokinome ana ...... B from Listeria monocytogenes.

@en

P2093

Claudia Hundertmark

http://www.w3.org/2001/XMLSchema#string

György Kéri

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Henrik Daub

http://www.w3.org/2001/XMLSchema#string

Jürgen Wehland

http://www.w3.org/2001/XMLSchema#string

Lothar Jänsch

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Manfred Nimtz

http://www.w3.org/2001/XMLSchema#string

Thorsten Johl

http://www.w3.org/2001/XMLSchema#string

Tobias Reinl

http://www.w3.org/2001/XMLSchema#string

P2860

Precise protein quantification based on peptide quantification using iTRAQ.

Structure of the human receptor tyrosine kinase met in complex with the Listeria invasion protein InlB

The protein kinase complement of the human genome

Nercc1, a mammalian NIMA-family kinase, binds the Ran GTPase and regulates mitotic progression

Phospho.ELM: a database of experimentally verified phosphorylation sites in eukaryotic proteins

Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain

GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands.

Molecular interaction between the Strep-tag affinity peptide and its cognate target, streptavidin

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics

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2778-2795

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scholarly article

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10.1074/MCP.M800521-MCP200

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12

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8

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2009-07-29T00:00:00Z

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19640851

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Listeria monocytogenes

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2816026

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