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eukaryotic translation initiation factor 2 complex location
Known as:
eIF-2
, eIF2
, eukaryotic translation initiation factor 2 complex
Complex of three heterogeneous polypeptide chains, that form a ternary complex with initiator methionyl-tRNA and GTP. This ternary complex binds to…
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National Institutes of Health
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Related topics
Related topics
3 relations
EIF2S1 wt Allele
EIF2S3 gene
Eukaryotic Initiation Factor-2
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2017
Highly Cited
2017
Translation from unconventional 5′ start sites drives tumour initiation
A. Sendoel
,
Joshua G. Dunn
,
+9 authors
E. Fuchs
Nature
2017
Corpus ID: 205253261
We are just beginning to understand how translational control affects tumour initiation and malignancy. Here we use an epidermis…
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Highly Cited
2008
Highly Cited
2008
eIF2‐dependent and eIF2‐independent modes of initiation on the CSFV IRES: a common role of domain II
T. Pestova
,
Sylvain de Breyne
,
A. Pisarev
,
I. Abaeva
,
C. Hellen
EMBO Journal
2008
Corpus ID: 23879422
Specific interactions of the classical swine fever virus internal ribosomal entry site (IRES) with 40S ribosomal subunits and…
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Highly Cited
2005
Highly Cited
2005
Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation.
Mikkel A. Algire
,
David Maag
,
J. Lorsch
Molecules and Cells
2005
Corpus ID: 10128960
Highly Cited
2002
Highly Cited
2002
Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules.
N. Kedersha
,
Samantha Chen
,
+4 authors
P. Anderson
Molecular Biology of the Cell
2002
Corpus ID: 13022090
Environmental stress-induced phosphorylation of eIF2alpha inhibits protein translation by reducing the availability of eIF2-GTP…
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Highly Cited
2000
Highly Cited
2000
The joining of ribosomal subunits in eukaryotes requires eIF5B
T. Pestova
,
I. Lomakin
,
Joon-Hwa Lee
,
S. Choi
,
T. E. Dever
,
C. Hellen
Nature
2000
Corpus ID: 3739106
Initiation of eukaryotic protein synthesis begins with the ribosome separated into its 40S and 60S subunits. The 40S subunit…
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Highly Cited
2000
Highly Cited
2000
A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo.
K. Asano
,
J. Clayton
,
A. Shalev
,
A. Hinnebusch
Genes & Development
2000
Corpus ID: 38745918
Translation initiation factor 2 (eIF2) bound to GTP transfers the initiator methionyl tRNA to the 40S ribosomal subunit. The eIF5…
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Highly Cited
2000
Highly Cited
2000
Phosphorylation of serine 51 in initiation factor 2 alpha (eIF2 alpha) promotes complex formation between eIF2 alpha(P) and eIF2B and causes inhibition in the guanine nucleotide exchange activity of…
A. Sudhakar
,
A. Ramachandran
,
S. Ghosh
,
S. E. Hasnain
,
R. Kaufman
,
K. Ramaiah
Biochemistry
2000
Corpus ID: 26440875
Phosphorylation of serine 51 residue on the alpha-subunit of eukaryotic initiation factor 2 (eIF2alpha) inhibits the guanine…
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Highly Cited
1999
Highly Cited
1999
Conserved bipartite motifs in yeast eIF5 and eIF2Bϵ, GTPase‐activating and GDP–GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2
K. Asano
,
T. Krishnamoorthy
,
L. Phan
,
G. Pavitt
,
A. Hinnebusch
EMBO Journal
1999
Corpus ID: 37270769
In the initiation phase of eukaryotic translation, eIF5 stimulates the hydrolysis of GTP bound to eIF2 in the 40S ribosomal pre…
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Highly Cited
1997
Highly Cited
1997
GTP hydrolysis controls stringent selection of the AUG start codon during translation initiation in Saccharomyces cerevisiae.
H. Huang
,
H. Yoon
,
E. M. Hannig
,
T. Donahue
Genes & Development
1997
Corpus ID: 414741
We have isolated and characterized two suppressor genes, SUI4 and SUI5, that can initiate translation in the absence of an AUG…
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Highly Cited
1989
Highly Cited
1989
Activation of double-stranded RNA-dependent kinase (dsl) by the TAR region of HIV-1 mRNA: A novel translational control mechanism
I. Edery
,
R. Petryshyn
,
N. Sonenberg
Cell
1989
Corpus ID: 19592239
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