PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor. - Wikidata - wikimedia - TriplyDB

PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor.

PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor.

http://www.wikidata.org/entity/Q43033193

about

RegPhos: a system to explore the protein kinase-substrate phosphorylation network in humans The acidic A-domain of Arabidopsis TOC159 occurs as a hyperphosphorylated protein Plant mitochondrial dynamics and the role of membrane lipids Starches--from current models to genetic engineering Computational phosphoproteomics: from identification to localization MASCP gator: an overview of the Arabidopsis proteomic aggregation portal Somatic embryogenesis: life and death processes during apical-basal patterning.Role of plastid protein phosphatase TAP38 in LHCII dephosphorylation and thylakoid electron flow 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 Changes in the Phosphoproteome and Metabolome Link Early Signaling Events to Rearrangement of Photosynthesis and Central Metabolism in Salinity and Oxidative Stress Response in Arabidopsis.Phosphoproteomics in photosynthetic organisms.Towards understanding the crosstalk between protein post-translational modifications: Homo- and heterotypic PTM pair distances on protein surfaces are not random.Peroxiredoxins and Redox Signaling in Plants.Large-scale phosphoprotein analysis in Medicago truncatula roots provides insight into in vivo kinase activity in legumes.Sucrose-induced receptor kinase SIRK1 regulates a plasma membrane aquaporin in Arabidopsis.Selective mRNA sequestration by OLIGOURIDYLATE-BINDING PROTEIN 1 contributes to translational control during hypoxia in Arabidopsis.Improving the performance of protein kinase identification via high dimensional protein-protein interactions and substrate structure data.Meta-Analysis of Arabidopsis thaliana Phospho-Proteomics Data Reveals Compartmentalization of Phosphorylation Motifs.Mapping Biological Networks from Quantitative Data-Independent Acquisition Mass Spectrometry: Data to Knowledge Pipelines.The Molecular Biology Database Collection: 2008 update.Detection and characterization of 3D-signature phosphorylation site motifs and their contribution towards improved phosphorylation site prediction in proteins.Web-queryable large-scale data sets for hypothesis generation in plant biology.PostMod: sequence based prediction of kinase-specific phosphorylation sites with indirect relationship PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update.Early cytokinin response proteins and phosphoproteins of Arabidopsis thaliana identified by proteome and phosphoproteome profiling.Motif-All: discovering all phosphorylation motifs.Large-scale phosphoproteome analysis in seedling leaves of Brachypodium distachyon L.PlantPhos: using maximal dependence decomposition to identify plant phosphorylation sites with substrate site specificity.Engineering α-amylase levels in wheat grain suggests a highly sophisticated level of carbohydrate regulation during development.Metabolic control of redox and redox control of metabolism in plants.Toward a complete in silico, multi-layered embryonic stem cell regulatory network.P(3)DB: An Integrated Database for Plant Protein Phosphorylation.AtPID: the overall hierarchical functional protein interaction network interface and analytic platform for Arabidopsis Prediction of protein phosphorylation sites by using the composition of k-spaced amino acid pairs.Mass spectrometric identification of in vivo phosphorylation sites of differentially expressed proteins in elongating cotton fiber cells.Arabinogalactan glycosyltransferases target to a unique subcellular compartment that may function in unconventional secretion in plants.Proteome and phosphoproteome characterization reveals new response and defense mechanisms of Brachypodium distachyon leaves under salt stress.Quantitative phosphoproteomic profiling of fiber differentiation and initiation in a fiberless mutant of cotton.

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PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor.

http://www.wikidata.org/entity/Q43033193

description

2007 nî lūn-bûn

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PhosPhAt: a database of phosph ...... hosphorylation site predictor.

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PhosPhAt: a database of phosph ...... hosphorylation site predictor.

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PhosPhAt: a database of phosph ...... hosphorylation site predictor.

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Jan Hummel

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Joachim Selbig

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Pawel Durek

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Waltraud X Schulze

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P2860

ProMEX: a mass spectral reference database for proteins and protein phosphorylation sites

Gene ontology: tool for the unification of biology

Combining metal oxide affinity chromatography (MOAC) and selective mass spectrometry for robust identification of in vivo protein phosphorylation sites.

Plant Methods: putting the spotlight on technological innovation in the plant sciences

Probability-based protein identification by searching sequence databases using mass spectrometry data

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

Sequence and structure-based prediction of eukaryotic protein phosphorylation sites

SH2 and SH3 domains: from structure to function

Differential multisite phosphorylation of the trehalose-6-phosphate synthase gene family in Arabidopsis thaliana: a mass spectrometry-based process for multiparallel peptide library phosphorylation analysis.

A method of comparing the areas under receiver operating characteristic curves derived from the same cases.

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10.1093/NAR/GKM812

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Database issue

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36

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Joshua L. Heazlewood

Wolfram Weckwerth

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2007-11-04T00:00:00Z

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5862762

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17984086

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Arabidopsis thaliana

phosphorylation

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2238998

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