Controlling the activity of a phosphatase and tensin homolog (PTEN) by membrane potential. - Test2 - elhamkhani - TriplyDB

Controlling the activity of a phosphatase and tensin homolog (PTEN) by membrane potential.

Controlling the activity of a phosphatase and tensin homolog (PTEN) by membrane potential.

http://www.wikidata.org/entity/Q34979031

about

Voltage-Controlled Enzymes: The New JanusBifrons Endogenous voltage gradients as mediators of cell-cell communication: strategies for investigating bioelectrical signals during pattern formation PtdIns(4,5)P2-mediated cell signaling: emerging principles and PTEN as a paradigm for regulatory mechanism Phosphoinositides: tiny lipids with giant impact on cell regulation Re-membering the body: applications of computational neuroscience to the top-down control of regeneration of limbs and other complex organs Voltage sensitive phosphatases: emerging kinship to protein tyrosine phosphatases from structure-function research Differential regulation of proton-sensitive ion channels by phospholipids: a comparative study between ASICs and TRPV1 A human phospholipid phosphatase activated by a transmembrane control module.Endogenous Voltage Potentials and the Microenvironment: Bioelectric Signals that Reveal, Induce and Normalize Cancer.Detection and manipulation of phosphoinositides.Discovery and functional characterization of a neomorphic PTEN mutation.Characterization of the Functional Domains of a Mammalian Voltage-Sensitive Phosphatase.Allosteric substrate switching in a voltage-sensing lipid phosphatase Phosphoinositide 5- and 3-phosphatase activities of a voltage-sensing phosphatase in living cells show identical voltage dependence Simple scheme of lipid enzyme can explain complex lives of phosphoinositides Molecular bioelectricity in developmental biology: new tools and recent discoveries: control of cell behavior and pattern formation by transmembrane potential gradients.Voltage sensor of ion channels and enzymes.Domain-to-domain coupling in voltage-sensing phosphatase.A method to control phosphoinositides and to analyze PTEN function in living cells using voltage sensitive phosphatases.Coupling of Ci-VSP modules requires a combination of structure and electrostatics within the linker.Voltage-sensor transitions of the inward-rectifying K+ channel KAT1 indicate a latching mechanism biased by hydration within the voltage sensor.

P2860

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P2860

Controlling the activity of a phosphatase and tensin homolog (PTEN) by membrane potential.

http://www.wikidata.org/entity/Q34979031

description

2011 nî lūn-bûn

@nan

2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

@zh-hk

2011年論文

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2011年論文

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2011年论文

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name

Controlling the activity of a ...... (PTEN) by membrane potential.

@ast

Controlling the activity of a ...... (PTEN) by membrane potential.

@en

Controlling the activity of a phosphatase and tensin homolog

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type

label

Controlling the activity of a ...... (PTEN) by membrane potential.

@ast

Controlling the activity of a ...... (PTEN) by membrane potential.

@en

Controlling the activity of a phosphatase and tensin homolog

@nl

prefLabel

Controlling the activity of a ...... (PTEN) by membrane potential.

@ast

Controlling the activity of a ...... (PTEN) by membrane potential.

@en

Controlling the activity of a phosphatase and tensin homolog

@nl

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JBC.M110.201749

P1433

Journal of Biological Chemistry

P1476

Controlling the activity of a phosphatase and tensin homolog (PTEN) by membrane potential

@en

P2093

Carlos A Villalba-Galea

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

Christian R Halaszovich

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Daniela N Schreiber

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Dominik Oliver

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Francisco Bezanilla

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Jérôme Lacroix

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P2860

Evidence that the tandem-pleckstrin-homology-domain-containing protein TAPP1 interacts with Ptd(3,4)P2 and the multi-PDZ-domain-containing protein MUPP1 in vivo

The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

Critical role of PIP5KI{gamma}87 in InsP3-mediated Ca(2+) signaling

Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association

Allosteric activation of PTEN phosphatase by phosphatidylinositol 4,5-bisphosphate

A phosphorylation-dependent intramolecular interaction regulates the membrane association and activity of the tumor suppressor PTEN.

Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers

TPIP: a novel phosphoinositide 3-phosphatase

Essential role of phosphoinositide metabolism in synaptic vesicle recycling

A PTEN-like phosphatase with a novel substrate specificity

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17945-17953

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scholarly article

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10.1074/JBC.M110.201749

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20

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286

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Michael G Leitner

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21454672

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3093869

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