(Q24294976)

GOA release 2020-03-11

author name string

Rajasekhar N V S Suragani

1

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Rajesh Kamindla

2

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N Z Ehtesham

3

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Kolluru V A Ramaiah

Biochemical and Biophysical Research Communications

4

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language of work or name

English

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publication date

30 December 2005

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published in

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volume

338

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page(s)

1766-72

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issue

4

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cites work

Inhibition of transthyretin amyloid fibril formation by 2,4-dinitrophenol through tetramer stabilization

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Identification of novel phosphorylation sites in the beta-subunit of translation initiation factor eIF-2

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Expression and purification of the subunits of human translational initiation factor 2 (eIF2): phosphorylation of eIF2 alpha and beta

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Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B

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Gene-specific regulation by general translation factors

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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 eIF2B.

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Serine 48 in initiation factor 2 alpha (eIF2 alpha) is required for high-affinity interaction between eIF2 alpha(P) and eIF2B.

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Eukaryotic translation-initiation factor eIF2beta binds to protein kinase CK2: effects on CK2alpha activity

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Modulation of protein translation by Nck-1.

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Effect of phosphorylation of the alpha-subunit of eukaryotic initiation factor 2 on the function of reversing factor in the initiation of protein synthesis

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DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45

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Identification of interprotein interactions between the subunits of eukaryotic initiation factors eIF2 and eIF2B

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

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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.

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

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Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo

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

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Homologous regions of the alpha subunit of eukaryotic translational initiation factor 2 (eIF2alpha) and the vaccinia virus K3L gene product interact with the same domain within the dsRNA-activated protein kinase (PKR)

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Expression of mutant eukaryotic initiation factor 2 alpha subunit (eIF-2 alpha) reduces inhibition of guanine nucleotide exchange activity of eIF-2B mediated by eIF-2 alpha phosphorylation

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The beta subunit of eukaryotic translation initiation factor 2 binds mRNA through the lysine repeats and a region comprising the C2-C2 motif

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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

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The molecular mechanics of eukaryotic translation

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