BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.

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Structural transitions in conserved, ordered Beclin 1 domains essential to regulating autophagy.Targeting the potent Beclin 1-UVRAG coiled-coil interaction with designed peptides enhances autophagy and endolysosomal trafficking.

P2860

Q42513539-036D9FCE-8ACA-4E18-B815-7CF409D0DFCA Q55312015-C3A97BA0-33CB-4CE7-8BEE-BD35B9FB5E7D

P2860

BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.

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http://www.wikidata.org/entity/Q51130648

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

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2017年學術文章

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2017年學術文章

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BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.

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BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.

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BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.

@en

BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.

@nl

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BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.

@en

BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.

@nl

P1476

BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.

@en

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Beth Levine

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

Christopher L Colbert

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

David Neau

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

Minfei Su

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

Sangita C Sinha

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

Shane Wyborny

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

Srinivas Chakravarthy

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

Yue Li

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

P2860

Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein

Architecture and dynamics of the autophagic phosphatidylinositol 3-kinase complex

Ambra1 regulates autophagy and development of the nervous system

Beclin 2 functions in autophagy, degradation of G protein-coupled receptors, and metabolism

Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages

Global rigid body modeling of macromolecular complexes against small-angle scattering data

Electrostatics of nanosystems: application to microtubules and the ribosome

Autophagy in immunity and inflammation

Autophagy: molecular machinery for self-eating

Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes.

P304

972-984

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

P31

scholarly article

P356

10.1002/PRO.3140

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

P433

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

P478

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

P577

2017-03-12T00:00:00Z

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

P698

28218432

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P932

5405433

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

BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.

about

P2860

P2860

BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.

description

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P932