NMR analysis of the interaction of picornaviral proteinases Lb and 2A with their substrate eukaryotic initiation factor 4GII.

about

4EBP-Dependent Signaling Supports West Nile Virus Growth and Protein Expression.Structures and Corresponding Functions of Five Types of Picornaviral 2A Proteins.Irreversible inactivation of ISG15 by a viral leader protease enables alternative infection detection strategies.

P2860

Q37378827-A8D0D30A-6E1C-4967-9F11-BD73033099E0 Q40091495-AF50646F-38D0-408E-A9A4-79FA8FC891AB Q49790187-778F3EEC-B478-435A-8561-B3030B390234

P2860

NMR analysis of the interaction of picornaviral proteinases Lb and 2A with their substrate eukaryotic initiation factor 4GII.

Item

http://www.wikidata.org/entity/Q39719726

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

NMR analysis of the interactio ...... ryotic initiation factor 4GII.

@en

NMR analysis of the interactio ...... ryotic initiation factor 4GII.

@nl

type

Item

label

NMR analysis of the interactio ...... ryotic initiation factor 4GII.

@en

NMR analysis of the interactio ...... ryotic initiation factor 4GII.

@nl

prefLabel

NMR analysis of the interactio ...... ryotic initiation factor 4GII.

@en

NMR analysis of the interactio ...... ryotic initiation factor 4GII.

@nl

P1476

NMR analysis of the interactio ...... ryotic initiation factor 4GII.

@en

P2093

Carla Sousa-Blin

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

Georg Kontaxis

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

Katharina Ruzicska

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

Martina Aumayr

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

Sofiya Fedosyuk

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

P2860

A novel functional human eukaryotic translation initiation factor 4G

The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins

Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: identification of the L-protease cleavage site in vitro

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

The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis

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

Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes

Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E

Investigating the substrate specificity and oligomerisation of the leader protease of foot and mouth disease virus using NMR

Crystallization of eIF4E complexed with eIF4GI peptide and glycerol reveals distinct structural differences around the cap-binding site

P304

1979-1996

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

P31

scholarly article

P356

10.1002/PRO.2807

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

P433

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

P478

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

P50

Tim Skern

P577

2015-09-19T00:00:00Z

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

P5875

282046191

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

P698

26384734

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

P932

4815241

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

NMR analysis of the interaction of picornaviral proteinases Lb and 2A with their substrate eukaryotic initiation factor 4GII.

about

P2860

P2860

NMR analysis of the interaction of picornaviral proteinases Lb and 2A with their substrate eukaryotic initiation factor 4GII.

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