(Q46979602)

English

Direct binding of translation initiation factor eIF2gamma-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2B epsilon.

scientific article published on 7 March 2006

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scholarly article

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/16522633

Direct binding of translation initiation factor eIF2gamma-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2B epsilon. (English)

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/16522633

2

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/16522633

author name string

Pankaj V Alone

1

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/16522633

language of work or name

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publication date

7 March 2006

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/16522633

Journal of Biological Chemistry

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/16522633

281

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/16522633

12636-12644

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/16522633

18

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/16522633

X-ray structure of translation initiation factor eIF2gamma: implications for tRNA and eIF2alpha binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

GTP-dependent recognition of the methionine moiety on initiator tRNA by translation factor eIF2.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Functional molecular mapping of archaeal translation initiation factor 2.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Conserved sequences in the beta subunit of archaeal and eukaryal translation initiation factor 2 (eIF2), absent from eIF5, mediate interaction with eIF2gamma

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Eukaryotic translation initiation factor 5 functions as a GTPase-activating protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

The joining of ribosomal subunits in eukaryotes requires eIF5B.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Gene-specific regulation by general translation factors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Tight binding of the phosphorylated alpha subunit of initiation factor 2 (eIF2alpha) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Characterization of the minimal catalytic domain within eIF2B: the guanine-nucleotide exchange factor for translation initiation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Eukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Specific interaction of eukaryotic translation initiation factor 5 (eIF5) with the beta-subunit of eIF2

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Mutational analysis of mammalian translation initiation factor 5 (eIF5): role of interaction between the beta subunit of eIF2 and eIF5 in eIF5 function in vitro and in vivo

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Physical association of eukaryotic initiation factor (eIF) 5 carboxyl-terminal domain with the lysine-rich eIF2beta segment strongly enhances its binding to eIF3.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Related eIF3 subunits TIF32 and HCR1 interact with an RNA recognition motif in PRT1 required for eIF3 integrity and ribosome binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Development and characterization of a reconstituted yeast translation initiation system.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Identification of domains and residues within the epsilon subunit of eukaryotic translation initiation factor 2B (eIF2Bepsilon) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

The archaeal eIF2 homologue: functional properties of an ancient translation initiation factor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

GTPase-activating proteins: helping hands to complement an active site.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511700200

21 January 2018

Identifiers

10.1074/JBC.M511700200

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/16522633

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/16522633

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