Single-molecule force spectroscopy of protein-membrane interactions.

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The Role of Glycans in Bacterial Adhesion to Mucosal Surfaces: How Can Single-Molecule Techniques Advance Our Understanding?

P2860

Q56888631-A3E04CD1-6015-4A15-BA14-E6D4F53284D7

P2860

Single-molecule force spectroscopy of protein-membrane interactions.

Item

http://www.wikidata.org/entity/Q47148257

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2017 nî lūn-bûn

@nan

2017年の論文

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2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Single-molecule force spectroscopy of protein-membrane interactions.

@en

Single-molecule force spectroscopy of protein-membrane interactions.

@nl

type

Item

label

Single-molecule force spectroscopy of protein-membrane interactions.

@en

Single-molecule force spectroscopy of protein-membrane interactions.

@nl

prefLabel

Single-molecule force spectroscopy of protein-membrane interactions.

@en

Single-molecule force spectroscopy of protein-membrane interactions.

@nl

P1476

Single-molecule force spectroscopy of protein-membrane interactions.

@en

P2093

Ben O'Shaughnessy

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

Erdem Karatekin

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

Junyi Jiao

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

Lu Ma

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

Yanghui Li

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

Yiying Cai

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

Zhenyong Wu

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

P2860

PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins.

Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2 domains

Structure and Ca²⁺-binding properties of the tandem C₂ domains of E-Syt2

Direct observation of base-pair stepping by RNA polymerase

Differential detection of dual traps improves the spatial resolution of optical tweezers

Membrane fusion: grappling with SNARE and SM proteins

Signaling through C2 domains: more than one lipid target

Superdiffusive motion of membrane-targeting C2 domains.

Lateral diffusion of proteins on supported lipid bilayers: additive friction of synaptotagmin 7 C2A-C2B tandem domains.

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scholarly article

P356

10.7554/ELIFE.30493

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

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English

P478

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

P50

Pietro De Camilli

Yongli Zhang

P577

2017-10-30T00:00:00Z

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

P698

29083305

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

P932

5690283

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

Single-molecule force spectroscopy of protein-membrane interactions.

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P2860

P2860

Single-molecule force spectroscopy of protein-membrane interactions.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P31

P356

P407

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P31

P356

P407

P478

P50

P577

P698

P932