Polyester modification of the mammalian TRPM8 channel protein: implications for structure and function.
about
Roles of TRPM8 Ion Channels in Cancer: Proliferation, Survival, and InvasionRole of β-hydroxybutyrate, its polymer poly-β-hydroxybutyrate and inorganic polyphosphate in mammalian health and diseaseMolecular complementarity between simple, universal molecules and ions limited phenotype space in the precursors of cellsImplications of Human Transient Receptor Potential Melastatin 8 (TRPM8) Channel Gating from Menthol Binding Studies of the Sensing DomainPolyhydroxybutyrate targets mammalian mitochondria and increases permeability of plasmalemmal and mitochondrial membranes.The TRPM8 protein is a testosterone receptor: II. Functional evidence for an ionotropic effect of testosterone on TRPM8The TRPM8 protein is a testosterone receptor: I. Biochemical evidence for direct TRPM8-testosterone interactions.Regulation of the temperature-dependent activation of transient receptor potential vanilloid 1 (TRPV1) by phospholipids in planar lipid bilayers.Microscopic heat pulse-induced calcium dynamics in single WI-38 fibroblasts.TRPM8 channel as a novel molecular target in androgen-regulated prostate cancer cells.New insights in the formation of polyhydroxyalkanoate granules (carbonosomes) and novel functions of poly(3-hydroxybutyrate).Post-Translational Modifications of TRP Channels.Trafficking of ThermoTRP Channels.Mitochondrial Ca2+ uptake pathways.Methyl-esterified 3-hydroxybutyrate oligomers protect bacteria from hydroxyl radicals.Inorganic polyphosphate regulates neuronal excitability through modulation of voltage-gated channelsPhaM is the physiological activator of poly(3-hydroxybutyrate) (PHB) synthase (PhaC1) in Ralstonia eutropha.To be or not to be a poly(3-hydroxybutyrate) (PHB) depolymerase: PhaZd1 (PhaZ6) and PhaZd2 (PhaZ7) of Ralstonia eutropha, highly active PHB depolymerases with no detectable role in mobilization of accumulated PHB.Mitochondrial permeability transition pore induction is linked to formation of the complex of ATPase C-subunit, polyhydroxybutyrate and inorganic polyphosphate.Bidirectional modulation of thermal and chemical sensitivity of TRPM8 channels by the initial region of the N-terminal domain.New Insights into PhaM-PhaC-Mediated Localization of Polyhydroxybutyrate Granules in Ralstonia eutropha H16.
P2860
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P2860
Polyester modification of the mammalian TRPM8 channel protein: implications for structure and function.
description
2013 nî lūn-bûn
@nan
2013 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Polyester modification of the ...... ns for structure and function.
@ast
Polyester modification of the ...... ns for structure and function.
@en
Polyester modification of the ...... ns for structure and function.
@nl
type
label
Polyester modification of the ...... ns for structure and function.
@ast
Polyester modification of the ...... ns for structure and function.
@en
Polyester modification of the ...... ns for structure and function.
@nl
prefLabel
Polyester modification of the ...... ns for structure and function.
@ast
Polyester modification of the ...... ns for structure and function.
@en
Polyester modification of the ...... ns for structure and function.
@nl
P2093
P2860
P1433
P1476
Polyester modification of the ...... ns for structure and function.
@en
P2093
Alejandro Cohen
Dieter Jendrossek
Eleonora Zakharian
Evgeny Pavlov
Tibor Rohacs
Yann Bikard
P2860
P304
P356
10.1016/J.CELREP.2013.06.022
P577
2013-07-11T00:00:00Z