Controlling the activity of a phosphatase and tensin homolog (PTEN) by membrane potential.
about
Voltage-Controlled Enzymes: The New JanusBifronsEndogenous voltage gradients as mediators of cell-cell communication: strategies for investigating bioelectrical signals during pattern formationPtdIns(4,5)P2-mediated cell signaling: emerging principles and PTEN as a paradigm for regulatory mechanismPhosphoinositides: tiny lipids with giant impact on cell regulationRe-membering the body: applications of computational neuroscience to the top-down control of regeneration of limbs and other complex organsVoltage sensitive phosphatases: emerging kinship to protein tyrosine phosphatases from structure-function researchDifferential regulation of proton-sensitive ion channels by phospholipids: a comparative study between ASICs and TRPV1A 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 phosphatasePhosphoinositide 5- and 3-phosphatase activities of a voltage-sensing phosphatase in living cells show identical voltage dependenceSimple scheme of lipid enzyme can explain complex lives of phosphoinositidesMolecular 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.
description
2011 nî lūn-bûn
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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
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
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
@nl
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
P2093
P2860
P356
P1476
Controlling the activity of a phosphatase and tensin homolog (PTEN) by membrane potential
@en
P2093
Carlos A Villalba-Galea
Christian R Halaszovich
Daniela N Schreiber
Dominik Oliver
Francisco Bezanilla
Jérôme Lacroix
P2860
P304
17945-17953
P356
10.1074/JBC.M110.201749
P407
P577
2011-03-17T00:00:00Z