Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway. - Test2 - elhamkhani - TriplyDB

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

http://www.wikidata.org/entity/Q27932327

about

Distinct Peptide Binding Specificities of Src Homology 3 (SH3) Protein Domains Can Be Determined by Modulation of Local Energetics across the Binding Interface Scaffold Protein Ahk1, Which Associates with Hkr1, Sho1, Ste11, and Pbs2, Inhibits Cross Talk Signaling from the Hkr1 Osmosensor to the Kss1 Mitogen-Activated Protein Kinase Interaction with the SH3 domain protein Bem1 regulates signaling by the Saccharomyces cerevisiae p21-activated kinase Ste20 Yeast adaptor protein, Nbp2p, is conserved regulator of fungal Ptc1p phosphatases and is involved in multiple signaling pathways A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function.Ptc1p regulates cortical ER inheritance via Slt2p.Disruption of iron homeostasis in Saccharomyces cerevisiae by high zinc levels: a genome-wide study.Identifying functional mechanisms of gene and protein regulatory networks in response to a broader range of environmental stresses.Genome-wide survey of yeast mutations leading to activation of the yeast cell integrity MAPK pathway: novel insights into diverse MAPK outcomes.A type 2C protein phosphatase FgPtc3 is involved in cell wall integrity, lipid metabolism, and virulence in Fusarium graminearum.An integrated pathway system modeling of Saccharomyces cerevisiae HOG pathway: a Petri net based approach.Screening the budding yeast genome reveals unique factors affecting K2 toxin susceptibility.Phosphoproteomic analyses reveal novel cross-modulation mechanisms between two signaling pathways in yeast Role for cER and Mmr1p in anchorage of mitochondria at sites of polarized surface growth in budding yeast.A global perspective of the genetic basis for carbonyl stress resistance.Mechanisms regulating the protein kinases of Saccharomyces cerevisiae.Function and regulation in MAPK signaling pathways: lessons learned from the yeast Saccharomyces cerevisiae Genetic networks inducing invasive growth in Saccharomyces cerevisiae identified through systematic genome-wide overexpression Master and commander in fungal pathogens: the two-component system and the HOG signaling pathway.PTC1 is required for vacuole inheritance and promotes the association of the myosin-V vacuole-specific receptor complex.Control of high osmolarity signalling in the yeast Saccharomyces cerevisiae.Type 2C protein phosphatases in fungi.Role of the osmotic stress regulatory pathway in morphogenesis and secondary metabolism in filamentous fungi Response to hyperosmotic stress Normal function of the yeast TOR pathway requires the type 2C protein phosphatase Ptc1.Differential genetic interactions of yeast stress response MAPK pathways.A framework for mapping, visualisation and automatic model creation of signal-transduction networks.Wide-Ranging Effects of the Yeast Ptc1 Protein Phosphatase Acting Through the MAPK Kinase Mkk1.Identification of a complex genetic network underlying Saccharomyces cerevisiae colony morphology.Robustness and fragility in the yeast high osmolarity glycerol (HOG) signal-transduction pathway.Involvement of two type 2C protein phosphatases BcPtc1 and BcPtc3 in the regulation of multiple stress tolerance and virulence of Botrytis cinerea.Genetic interactions between protein phosphatases CaPtc2p and CaPph3p in response to genotoxins and rapamycin in Candida albicans.Expression of CaPTC7 is developmentally regulated during serum-induced morphogenesis in the human fungal pathogen Candida albicans.Genomics of cellular proliferation in periodic environmental fluctuations.

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P2860

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

http://www.wikidata.org/entity/Q27932327

description

2004 nî lūn-bûn

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2004 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2004 թվականի հունվարին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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name

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

@ast

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

@en

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

@nl

type

label

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

@ast

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

@en

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

@nl

prefLabel

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

@ast

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

@en

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

@nl

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SJ.EMBOJ.7600036

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The EMBO Journal

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Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

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Irene M Ota

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

James Mapes

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P2860

The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family

MP1: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade

Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways.

MAP kinase pathways in the yeast Saccharomyces cerevisiae

Ptc1, a type 2C Ser/Thr phosphatase, inactivates the HOG pathway by dephosphorylating the mitogen-activated protein kinase Hog1

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae

Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry

Mutations in a protein tyrosine phosphatase gene (PTP2) and a protein serine/threonine phosphatase gene (PTC1) cause a synthetic growth defect in Saccharomyces cerevisiae.

A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules.

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10.1038/SJ.EMBOJ.7600036

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