Dynamics of protein-protein interactions at the MscL periplasmic-lipid interface. - Wikidata - wikimedia - TriplyDB

Dynamics of protein-protein interactions at the MscL periplasmic-lipid interface.

Dynamics of protein-protein interactions at the MscL periplasmic-lipid interface.

http://www.wikidata.org/entity/Q37533546

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Force transduction and lipid binding in MscL: a continuum-molecular approach Electrostatics at the membrane define MscL channel mechanosensitivity and kinetics.

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Dynamics of protein-protein interactions at the MscL periplasmic-lipid interface.

http://www.wikidata.org/entity/Q37533546

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on January 2014

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Dynamics of protein-protein interactions at the MscL periplasmic-lipid interface.

@en

Dynamics of protein-protein interactions at the MscL periplasmic-lipid interface.

@nl

type

label

Dynamics of protein-protein interactions at the MscL periplasmic-lipid interface.

@en

Dynamics of protein-protein interactions at the MscL periplasmic-lipid interface.

@nl

prefLabel

Dynamics of protein-protein interactions at the MscL periplasmic-lipid interface.

@en

Dynamics of protein-protein interactions at the MscL periplasmic-lipid interface.

@nl

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P356

J.BPJ.2013.12.006

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Biophysical Journal

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Dynamics of protein-protein interactions at the MscL periplasmic-lipid interface.

@en

P2093

Dalian Zhong

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

Li-Min Yang

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

Paul Blount

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

P2860

Two types of mechanosensitive channels in the Escherichia coli cell envelope: solubilization and functional reconstitution

Membrane topology and multimeric structure of a mechanosensitive channel protein of Escherichia coli

A large iris-like expansion of a mechanosensitive channel protein induced by membrane tension

The oligomeric state of the truncated mechanosensitive channel of large conductance shows no variance in vivo

Cysteine scanning of MscL transmembrane domains reveals residues critical for mechanosensitive channel gating.

Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel

Single residue substitutions that change the gating properties of a mechanosensitive channel in Escherichia coli

S. aureus MscL is a pentamer in vivo but of variable stoichiometries in vitro: implications for detergent-solubilized membrane proteins

Pressure-sensitive ion channel in Escherichia coli

Open channel structure of MscL and the gating mechanism of mechanosensitive channels.

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375-381

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scholarly article

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10.1016/J.BPJ.2013.12.006

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2

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106

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2014-01-01T00:00:00Z

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259915594

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