A helical processing pipeline for EM structure determination of membrane proteins

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Organization of the influenza virus replication machinery The Electron Microscopy eXchange (EMX) initiative.Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: insights from Torpedo postsynaptic membranes

P2860

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P2860

A helical processing pipeline for EM structure determination of membrane proteins

Item

http://www.wikidata.org/entity/Q35683176

description

2011 nî lūn-bûn

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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

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2011年論文

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2011年论文

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2011年论文

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2011年论文

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name

A helical processing pipeline for EM structure determination of membrane proteins

@ast

A helical processing pipeline for EM structure determination of membrane proteins

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type

Item

label

A helical processing pipeline for EM structure determination of membrane proteins

@ast

A helical processing pipeline for EM structure determination of membrane proteins

@en

prefLabel

A helical processing pipeline for EM structure determination of membrane proteins

@ast

A helical processing pipeline for EM structure determination of membrane proteins

@en

P1476

A helical processing pipeline for EM structure determination of membrane proteins

@en

P2093

Andrew Ward

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

Clinton S Potter

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

Lauren S Fisher

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

Nigel Unwin

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

Ronald A Milligan

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

P2860

Lipid-protein interactions in double-layered two-dimensional AQP0 crystals.

Towards atomic resolution structural determination by single-particle cryo-electron microscopy

3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry.

Structural determinants of water permeation through aquaporin-1

A structural model for the catalytic cycle of Ca(2+)-ATPase

Structure and gating mechanism of the acetylcholine receptor pore

3.88 Å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy

Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks.

Hydrogen-bonding networks and RNA bases revealed by cryo electron microscopy suggest a triggering mechanism for calcium switches.

Accurate determination of local defocus and specimen tilt in electron microscopy

P304

350-362

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P31

scholarly article

P356

10.1016/J.YMETH.2011.09.013

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P433

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

P478

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

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Bridget Carragher

P577

2011-09-20T00:00:00Z

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P5875

51688014

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21964395

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P932

3262078

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A helical processing pipeline for EM structure determination of membrane proteins

about

P2860

P2860

A helical processing pipeline for EM structure determination of membrane proteins

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932