A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3 (Q24648463)

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English	A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3	scientific article

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scholarly article

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A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3 (English)

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author name string

N Méthot

1

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M S Song

2

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N Sonenberg

3

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language of work or name

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publication date

October 1996

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Molecular and Cellular Biology

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16

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10

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5328-34

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The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence

1 reference

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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

1 reference

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Cloning and expression of eukaryotic initiation factor 4B cDNA: sequence determination identifies a common RNA recognition motif

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Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A

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Conserved structures and diversity of functions of RNA-binding proteins

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A novel genetic system to detect protein-protein interactions

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Use of T7 RNA polymerase to direct expression of cloned genes

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A new yeast translation initiation factor suppresses a mutation in the eIF-4A RNA helicase

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A Saccharomyces cerevisiae homologue of mammalian translation initiation factor 4B contributes to RNA helicase activity

1 reference

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The Saccharomyces cerevisiae translation initiation factor Tif3 and its mammalian homologue, eIF-4B, have RNA annealing activity

1 reference

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Improved method for high efficiency transformation of intact yeast cells

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Two structural domains of initiation factor eIF-4B are involved in binding to RNA

1 reference

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Prediction of protein conformation

1 reference

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The role of eIF-4C in protein synthesis initiation complex formation

1 reference

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Characterization of glutathione S-transferases in rat kidney. Alteration of composition by cis-platinum

1 reference

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The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes

1 reference

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Initiation of mammalian protein synthesis. II. The assembly of the initiation complex with purified initiation factors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=231531

7 April 2017

Binding and release of radiolabeled eukaryotic initiation factors 2 and 3 during 80 S initiation complex formation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=231531

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Elimination of false positives that arise in using the two-hybrid system

1 reference

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Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation

1 reference

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7 April 2017

Correlation of two-hybrid affinity data with in vitro measurements

1 reference

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Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F

1 reference

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RNA recognition: a family matter?

1 reference

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1 reference

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A mutation allowing an mRNA secondary structure diminishes translation of Saccharomyces cerevisiae iso-1-cytochrome c

1 reference

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The ATP-dependent interaction of eukaryotic initiation factors with mRNA.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=231531

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mRNAs containing extensive secondary structure in their 5' non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E

1 reference

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Purification and characterization of initiation factor IF-E3 from rabbit reticulocytes

1 reference

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A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5'-terminal cap in mRNA

1 reference

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In vitro RNA selection identifies RNA ligands that specifically bind to eukaryotic translation initiation factor 4B: the role of the RNA remotif

1 reference

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Structure of initiation factor eIF-3 from rat liver. Hydrodynamic and electron microscopic investigations.

1 reference

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Insertion mutagenesis to increase secondary structure within the 5' noncoding region of a eukaryotic mRNA reduces translational efficiency.

1 reference

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Dissociation of skeletal muscle ribosomes from normal and diabetic animals by initiation factors EIF-3

1 reference

https://pubmed.ncbi.nlm.nih.gov/8816444

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Immunochemical characterization of mammalian protein synthesis initiation factors

1 reference

https://pubmed.ncbi.nlm.nih.gov/8816444

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identification and quantitation of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional polyacrylamide gel electrophoresis

1 reference

https://pubmed.ncbi.nlm.nih.gov/8816444

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Construction and use of gene fusions to lacZ (beta-galactosidase) that are expressed in yeast

1 reference

https://pubmed.ncbi.nlm.nih.gov/8816444

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

RNA-stimulated ATPase activity of eukaryotic initiation factors

1 reference

https://pubmed.ncbi.nlm.nih.gov/8816444

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

ATP-dependent unwinding of messenger RNA structure by eukaryotic initiation factors

1 reference

https://pubmed.ncbi.nlm.nih.gov/8816444

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Eukaryotic protein synthesis initiation factor eIF-3: Determination of concentration and association with ribosomes in rabbit reticulocyte and HeLa cell lysates

1 reference

https://pubmed.ncbi.nlm.nih.gov/8816444

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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