TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death. - Test2 - elhamkhani - TriplyDB

TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death.

TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death.

http://www.wikidata.org/entity/Q37412484

about

Knockout of Eva1a leads to rapid development of heart failure by impairing autophagy.Structure of the WD40-domain of human ATG16L1.Proteomics Insights into Autophagy.The WD40 domain of ATG16L1 is required for its non-canonical role in lipidation of LC3 at single membranes.Quantitative proteomics reveals EVA1A-related proteins involved in neuronal differentiation.Sorting out "non-canonical" autophagy.Liver-specific deletion of Eva1a/Tmem166 aggravates acute liver injury by impairing autophagy.On the Role of Basal Autophagy in Adult Neural Stem Cells and Neurogenesis

P2860

Q37745166-965000DA-5A5F-4874-8604-AD38A1BD2543 Q40144442-9DB54987-C243-430D-8162-6050E8004B47 Q42514979-82E4014F-37B4-4EE1-BDB0-2174DEADB180 Q47556315-95A8CC01-6595-4CEC-8D9C-0D76F456F1C6 Q48024429-66B5C79D-F090-4407-A417-F1150117EFFC Q50066701-C0761D27-5091-48B4-AF4D-BE90EEA1B3DE Q55687008-96F646E8-1E37-4F20-9CCA-B33983D6F7C4 Q57817410-3788B18E-9084-44B4-9835-443D65AF2220

P2860

TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death.

http://www.wikidata.org/entity/Q37412484

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 04 August 2016

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death.

@en

TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death.

@nl

type

label

TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death.

@en

TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death.

@nl

prefLabel

TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death.

@en

TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death.

@nl

P1433

Q37412484-54DBBE6B-91CE-4116-B3C0-9EF7F87C11D8

P1476

Q37412484-4F10A5BE-7D88-4389-8B34-FFB824CC9C87

P2093

Q37412484-0D156376-5C44-413A-AEF8-C6DE5C647A8E

Q37412484-27DE9A8D-D288-41EE-A7E2-14FD8A79F3D3

Q37412484-2B3DFEFD-1433-46A9-B5C5-01C7E7E8C274

Q37412484-360570DD-3ED2-4E83-8B7C-D6BD8F1C932A

Q37412484-53BB8A2F-6E1A-428D-BCAF-DF95B16CCAA1

Q37412484-8E2E7C5B-17F6-4B9D-8EE2-1D7998437098

Q37412484-8ED0F8C1-748A-422A-B190-C51FD7162E21

Q37412484-AC685E14-E4D1-409C-B0F6-96E960A7B3CD

Q37412484-B11C3B4F-1C3A-47BB-8731-09918DDF61B4

Q37412484-BE3E7D41-FE16-48C2-A5BF-07F7113FD2E9

P2860

Q37412484-043A42E2-7A0C-4BE3-BE34-251343A754E3

Q37412484-05F17084-C074-4B29-8CF1-ABC1D9BC0422

Q37412484-092880CE-CF23-4E47-AF65-CD1D8ED70392

Q37412484-0D23FD05-B89E-4E4F-A903-F4630C9F5190

Q37412484-1418DE19-9F44-47FE-B567-7A29F040BBB8

Q37412484-1B627A2A-EBF6-4F0E-BFF5-0354CF91DF6D

Q37412484-219DF744-D7A9-45AA-BE24-0BF16D258793

Q37412484-28428F49-2642-4CA5-9B55-99957E1428B8

Q37412484-2A434553-C651-479A-9BA6-84C97EB00442

Q37412484-30A223D4-3266-4B84-8D6E-FA4412E652FD

P304

Q37412484-3D1ACF90-BD00-490C-B225-770E56A882D8

P31

Q37412484-D8FA69BD-6AF1-4849-87CA-1F0EA6D97C56

P356

Q37412484-AEF2DFC7-2CFD-4675-86B0-C2B9037084AD

P433

Q37412484-ACEC1B88-E2A0-4509-96E1-513484EFD5B6

P478

Q37412484-F38445C3-9112-4BE6-ACEB-E55D691CF24E

P577

Q37412484-D2B8DFBE-7E66-4659-AEBE-8718C3793C81

P698

Q37412484-91C4E413-B7A2-49FD-B119-7E855E016E47

P921

Q37412484-D79A93E1-E367-45BF-B22F-FAC4E175A505

P932

Q37412484-91946EA7-2AE4-4FB6-93D7-AA68E530C045

P356

P1433

Cell Death and Disease

P1476

TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death.

@en

P2093

Beiqi Hongdu

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

Chentong Xu

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

Dalong Ma

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

Dan Xia

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

Ge Li

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

Jia Hu

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

Liujing Qu

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

Ning Li

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

Qihua He

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

Wei Liu

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

P2860

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes

PHF23 (plant homeodomain finger protein 23) negatively regulates cell autophagy by promoting ubiquitination and degradation of E3 ligase LRSAM1

Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy.

TMEM59 defines a novel ATG16L1-binding motif that promotes local activation of LC3

FIP200 regulates targeting of Atg16L1 to the isolation membrane

A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation

Mammalian autophagy: core molecular machinery and signaling regulation

LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing

The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy

P304

e2323

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

P31

scholarly article

P356

10.1038/CDDIS.2016.230

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

P433

8

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

P478

7

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

P577

2016-08-04T00:00:00Z

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

P698

27490928

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

P921

P932

5108317

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