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Search results 201 to 221 out of 221 for Eif5a

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0.018s

Type

Details

Score

Publication

1903841 | -

First Author:	Schnier J
Year:	1991
Journal:	Mol Cell Biol
Title:	Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae.
Volume:	11
Issue:	6
Pages:	3105-14

•

Publication

16928980 | -

First Author:	Swaney S
Year:	2006
Journal:	J Biomol Screen
Title:	Characterization of a high-throughput screening assay for inhibitors of elongation factor p and ribosomal peptidyl transferase activity.
Volume:	11
Issue:	7
Pages:	736-42

•

Protein Domain

IPR015365 | Elong-fact-P_C

Type:

Domain

Description:

Elongation factor P (EF-P) stimulates the peptidyltransferase activity in the prokaryotic 70S ribosome. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF-P binds near the streptomycine binding site of the 16S rRNA in the 30S subunit. EF-P interacts with domains 2 and 5 of the 23S rRNA. The L16 ribosomal protein of the 50S or its N-terminal fragment are required for EF-P mediated peptide bond synthesis, whereas L11, L15, and L7/L12 are not required in this reaction, suggesting that EF-P may function at a different ribosomal site than most other translation factors. EF-P is essential for cell viability and is required for protein synthesis [, , , ]. EF-P is mainly present in bacteria. The EF-P homologs in archaea and eukaryotes are the initiation factors aIF5A and eIF5A, respectively. EF-P has 3 domains (domains I, II, and III). Domains II and III are S1-like domains. This entry includes domain III (the second S1 domain of EF_P). Domains II and III of have structural homology to the eIF5A domain C, suggesting that domains II and III evolved by duplication. These domains adopt an OB-fold, with five β-strands forming a β-barrel in a Greek-key topology [].

•

Protein Domain

IPR001059 | Transl_elong_P/YeiP_cen

Type:

Domain

Description:

Elongation factor P (EF-P) is a prokaryotic protein translation factor required for efficient peptide bond synthesis on 70S ribosomes from fMet-tRNAfMet [, ]. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF-P binds near the streptomycine binding site of the 16S rRNA in the 30S subunit. EF-P interacts with domains 2 and 5 of the 23S rRNA. The L16 ribosomal protein of the 50S or its N-terminal fragment are required for EF-P mediated peptide bond synthesis, whereas L11, L15, and L7/L12 are not required in this reaction, suggesting that EF-P may function at a different ribosomal site than most other translation factors. EF-P is essential for cell viability and is required for protein synthesis. EF-P is mainly present in bacteria. The EF-P homologs in archaea and eukaryotes are the initiation factors aIF5A and eIF5A, respectively. EF-P has 3 domains (domains I, II, and III). Domains II and III are S1-like domains and have structural homology to the eIF5A domain C, suggesting that domains II and III evolved by duplication. This entry reresents the central domain of elongation factor P and its homologues. It forms an oligonucleotide-binding (OB) fold, though it is not clear if this region is involved in binding nucleic acids [].

•

Publication

39081972 | J:359064

First Author:	Perez Garcia G
Year:	2023
Journal:	Front Dement
Title:	Beneficial effects of physical exercise and an orally active mGluR2/3 antagonist pro-drug on neurogenesis and behavior in an Alzheimer's amyloidosis model.
Volume:	2

Pages:	1198006

•

Publication

29321164 | J:258681

First Author:	Fujimura K
Year:	2018
Journal:	Cancer Res
Title:	KRAS Oncoprotein Expression Is Regulated by a Self-Governing eIF5A-PEAK1 Feed-Forward Regulatory Loop.
Volume:	78
Issue:	6
Pages:	1444-1456

•

Publication

37271289 | J:356305

First Author:	Gobert AP
Year:	2023
Journal:	Gastroenterology
Title:	Hypusination Maintains Intestinal Homeostasis and Prevents Colitis and Carcinogenesis by Enhancing Aldehyde Detoxification.
Volume:	165
Issue:	3
Pages:	656-669.e8

•

Publication

15210970 | -

First Author:	Hanawa-Suetsugu K
Year:	2004
Journal:	Proc Natl Acad Sci U S A
Title:	Crystal structure of elongation factor P from Thermus thermophilus HB8.
Volume:	101
Issue:	26
Pages:	9595-600

•

Publication

12640443 | -

First Author:	Yuan P
Year:	2003
Journal:	Nat Struct Biol
Title:	A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa.
Volume:	10
Issue:	4
Pages:	264-70

•

Publication

9493264 | -

First Author:	Liao DI
Year:	1998
Journal:	Structure
Title:	Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site.
Volume:	6
Issue:	1
Pages:	23-32

•

Publication

9753699 | -

First Author:	Peat TS
Year:	1998
Journal:	Structure
Title:	Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 A resolution.
Volume:	6
Issue:	9
Pages:	1207-14

•

Publication

9195040 | -

First Author:	Aoki H
Year:	1997
Journal:	Biochimie
Title:	Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction.
Volume:	79
Issue:	1
Pages:	7-11

•

Protein

Q66JR8

Organism:	Mus musculus/domesticus
Length:	211
Fragment?:	false

•

Protein

Q8VHU9

Organism:	Mus musculus/domesticus
Length:	61
Fragment?:	true

•

Protein

Q8CH67

Organism:	Mus musculus/domesticus
Length:	41
Fragment?:	true

•

Protein

J3QPS8

Organism:	Mus musculus/domesticus
Length:	76
Fragment?:	false

•

Protein

P63242

Organism:	Mus musculus/domesticus
Length:	154
Fragment?:	false

•

Protein

Q8BGY2

Organism:	Mus musculus/domesticus
Length:	153
Fragment?:	false

•

Protein

A0A0A0MQM0

Organism:	Mus musculus/domesticus
Length:	149
Fragment?:	true

•

Publication

12932732 | -

First Author:	Andersen GR
Year:	2003
Journal:	Trends Biochem Sci
Title:	Elongation factors in protein biosynthesis.
Volume:	28
Issue:	8
Pages:	434-41

•

Publication

15922593 | -

First Author:	Nilsson J
Year:	2005
Journal:	Curr Opin Struct Biol
Title:	Elongation factors on the ribosome.
Volume:	15
Issue:	3
Pages:	349-54

•

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