Application of amphipols for structure-functional analysis of TRP channels. - Wikidata - wikimedia - TriplyDB

Application of amphipols for structure-functional analysis of TRP channels.

Application of amphipols for structure-functional analysis of TRP channels.

http://www.wikidata.org/entity/Q27690839

about

Structure of the full-length TRPV2 channel by cryo-EM.Labeling and functionalizing amphipols for biological applications.Amphipol-mediated screening of molecular orthoses specific for membrane protein targets.Amphipols for each season.Kv1.3 contains an alternative C-terminal ER exit motif and is recruited into COPII vesicles by Sec24a.Flotillin scaffold activity contributes to type VII secretion system assembly in Staphylococcus aureus.Using a SMALP platform to determine a sub-nm single particle cryo-EM membrane protein structure.Isolation of Escherichia coli mannitol permease, EIImtl, trapped in amphipol A8-35 and fluorescein-labeled A8-35.Molecular dynamics simulations of a membrane protein/amphipol complex.Thermal Fluctuations in Amphipol A8-35 Particles: A Neutron Scattering and Molecular Dynamics Study Novobiocin, a Newly Found TRPV1 Inhibitor, Attenuates the Expression of TRPV1 in Rat Intestine and Intestinal Epithelial Cell Line IEC-6

P2860

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P2860

Application of amphipols for structure-functional analysis of TRP channels.

http://www.wikidata.org/entity/Q27690839

description

2014 nî lūn-bûn

@nan

2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Application of amphipols for structure-functional analysis of TRP channels.

@ast

Application of amphipols for structure-functional analysis of TRP channels.

@en

Application of amphipols for structure-functional analysis of TRP channels.

@nl

type

label

Application of amphipols for structure-functional analysis of TRP channels.

@ast

Application of amphipols for structure-functional analysis of TRP channels.

@en

Application of amphipols for structure-functional analysis of TRP channels.

@nl

prefLabel

Application of amphipols for structure-functional analysis of TRP channels.

@ast

Application of amphipols for structure-functional analysis of TRP channels.

@en

Application of amphipols for structure-functional analysis of TRP channels.

@nl

P1433

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S00232-014-9684-6

P1433

Journal of Membrane Biology

P1476

Application of amphipols for structure-functional analysis of TRP channels.

@en

P2093

Cohen MR

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

Huynh KW

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Moiseenkova-Bell VY

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P2860

A capsaicin-receptor homologue with a high threshold for noxious heat

The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity

The capsaicin receptor: a heat-activated ion channel in the pain pathway

Structure of a nanobody-stabilized active state of the β(2) adrenoceptor

Crystal structure of the β2 adrenergic receptor-Gs protein complex

Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity

Structural Analyses of the Ankyrin Repeat Domain of TRPV6 and Related TRPV Ion Channels † , ‡

X-ray Crystal Structure of a TRPM Assembly Domain Reveals an Antiparallel Four-stranded Coiled-coil

Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1

Distinct properties of Ca 2+ –calmodulin binding to N- and C-terminal regulatory regions of the TRPV1 channel

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s00232-014-9684-6

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843-51

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scholarly article

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5027417

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10.1007/S00232-014-9684-6

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9-10

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247

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2014-10-01T00:00:00Z

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1001275474

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24894720

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4198461

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