PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update. - Wikidata - wikimedia - TriplyDB

PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update.

PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update.

http://www.wikidata.org/entity/Q33601095

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Plant mitochondrial dynamics and the role of membrane lipids Computational phosphoproteomics: from identification to localization MASCP gator: an overview of the Arabidopsis proteomic aggregation portal DAO1 catalyzes temporal and tissue-specific oxidative inactivation of auxin in Arabidopsis thaliana Identification of Phosphoinositide-Binding Protein PATELLIN2 as a Substrate of Arabidopsis MPK4 MAP Kinase during Septum Formation in Cytokinesis.Quantitative phosphoproteomics analysis of nitric oxide-responsive phosphoproteins in cotton leaf Enrichment and Analysis of Intact Phosphoproteins in Arabidopsis Seedlings Modulation of plant growth in vivo and identification of kinase substrates using an analog-sensitive variant of CYCLIN-DEPENDENT KINASE A;1 MASCP Gator: an aggregation portal for the visualization of Arabidopsis proteomics data Signal integration by chloroplast phosphorylation networks: an update Proteome-wide survey of phosphorylation patterns affected by nuclear DNA polymorphisms in Arabidopsis thaliana Protein Bioinformatics Databases and Resources.Sucrose-induced receptor kinase SIRK1 regulates a plasma membrane aquaporin in Arabidopsis.Management and dissemination of MS proteomic data with PROTICdb: example of a quantitative comparison between methods of protein extraction.Construction of protein phosphorylation networks by data mining, text mining and ontology integration: analysis of the spindle checkpoint.Meta-Analysis of Arabidopsis thaliana Phospho-Proteomics Data Reveals Compartmentalization of Phosphorylation Motifs.Transgenic tobacco overexpressing Brassica juncea HMG-CoA synthase 1 shows increased plant growth, pod size and seed yield.Identification of critical functional residues of receptor-like kinase ERECTA.The Musite open-source framework for phosphorylation-site prediction.pep2pro: a new tool for comprehensive proteome data analysis to reveal information about organ-specific proteomes in Arabidopsis thaliana.Motif-All: discovering all phosphorylation motifs.Large-scale phosphoproteome analysis in seedling leaves of Brachypodium distachyon L.Altered germination and subcellular localization patterns for PUB44/SAUL1 in response to stress and phytohormone treatments.Identification and analysis of phosphorylation status of proteins in dormant terminal buds of poplar.PhosTryp: a phosphorylation site predictor specific for parasitic protozoa of the family trypanosomatidae.Medicago PhosphoProtein Database: a repository for Medicago truncatula phosphoprotein data.GabiPD - The GABI Primary Database integrates plant proteomic data with gene-centric information Integrating phosphoproteomics in systems biology.P(3)DB: An Integrated Database for Plant Protein Phosphorylation.Recombinant β-1,3-1,4-glucanase from Theobroma cacao impairs Moniliophthora perniciosa mycelial growth.Musite, a tool for global prediction of general and kinase-specific phosphorylation sites.Proteome and phosphoproteome characterization reveals new response and defense mechanisms of Brachypodium distachyon leaves under salt stress.The Arabidopsis Kinome: phylogeny and evolutionary insights into functional diversification The plant Polycomb repressive complex 1 (PRC1) existed in the ancestor of seed plants and has a complex duplication history Glutathione transferases Signal processing by protein tyrosine phosphorylation in plants.Comparison of phosphorylation patterns across eukaryotes by discriminative N-gram analysis Suppressor mutations in the Glutamine Dumper1 protein dissociate disturbance in amino acid transport from other characteristics of the Gdu1D phenotype.Calcium-dependent protein kinases from Arabidopsis show substrate specificity differences in an analysis of 103 substrates An evolutionary view on thylakoid protein phosphorylation uncovers novel phosphorylation hotspots with potential functional implications.

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P2860

PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update.

http://www.wikidata.org/entity/Q33601095

description

2009 nî lūn-bûn

@nan

2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

name

PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update.

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PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update.

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type

label

PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update.

@ast

PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update.

@en

prefLabel

PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update.

@ast

PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update.

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Nucleic Acids Research

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PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update.

@en

P2093

Axel Nagel

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

Daniel MacLean

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

Pawel Durek

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Robert Schmidt

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Waltraud X Schulze

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P2860

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

High throughput identification of potential Arabidopsis mitogen-activated protein kinases substrates.

An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets.

An "Electronic Fluorescent Pictograph" browser for exploring and analyzing large-scale biological data sets

PhosCalc: a tool for evaluating the sites of peptide phosphorylation from mass spectrometer data.

Post-translational regulation of nitrate reductase: mechanism, physiological relevance and environmental triggers.

Structural mechanism of plant aquaporin gating.

Coupling oxidative signals to protein phosphorylation via methionine oxidation in Arabidopsis

Extension of the visualization tool MapMan to allow statistical analysis of arrays, display of corresponding genes, and comparison with known responses.

Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a component of brassinosteroid signaling in Arabidopsis

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D828-34

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scholarly article

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10.1093/NAR/GKP810

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P433

Database issue

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P478

38

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Joshua L. Heazlewood

Alexandra M Jones

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2009-10-30T00:00:00Z

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38058639

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19880383

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Arabidopsis thaliana

phosphorylation

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2808987

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