Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

about

Structural Analysis of the DAP5 MIF4G Domain and Its Interaction with eIF4A Cleavage of DAP5 by coxsackievirus B3 2A protease facilitates viral replication and enhances apoptosis by altering translation of IRES-containing genes.

P2860

Q27676748-7C0A75AA-DE7C-4A34-87A7-B5CF93C2C38C Q36799293-E6DC0608-9797-43A3-B5D1-1BBDA5489BEF

P2860

Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

Item

http://www.wikidata.org/entity/Q42260282

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

2009年论文

@zh

2009年论文

@zh-cn

name

Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

@en

Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

@nl

type

Item

label

Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

@en

Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

@nl

prefLabel

Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

@en

Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

@nl

P1476

Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

@en

P2093

Bhushan Nagar

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

Filipp Frank

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

Geneviève Virgili

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

P2860

The caspase-cleaved DAP5 protein supports internal ribosome entry site-mediated translation of death proteins.

DAP-5, a novel homolog of eukaryotic translation initiation factor 4G isolated as a putative modulator of gamma interferon-induced programmed cell death

A new translational regulator with homology to eukaryotic translation initiation factor 4G

Physical association of eukaryotic initiation factor 4G (eIF4G) with eIF4A strongly enhances binding of eIF4G to the internal ribosomal entry site of encephalomyocarditis virus and is required for internal initiation of translation

Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions

ExPASy: The proteomics server for in-depth protein knowledge and analysis

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G

A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery

The crystal structure of the C-terminal DAP5/p97 domain sheds light on the molecular basis for its processing by caspase cleavage

P304

15-19

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

P31

scholarly article

P356

10.1107/S1744309109044315

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

P433

Pt 1

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

P478

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

P50

Nahum Sonenberg

P577

2009-12-25T00:00:00Z

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

P698

20057060

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

P932

2805526

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

Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

about

P2860

P2860

Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932