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diphthamide

Known as: 1H-Imidazole-2-propanaminium, alpha-(aminocarbonyl)-4-(2-amino-2-carboxyethyl)-N,N,N-trimethyl-, hydroxide, inner salt, 2-(3-carboxyamido-3-(trimethylammonio)propyl)histidine 
National Institutes of Health

Related topics

Related topics

2 relations

Broader (1)

Histidine
analogs & derivatives

Papers overview

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Review
2014
Review
2014
The diphthamide modification pathway from Saccharomyces cerevisiae – revisited
Diphthamide is a conserved modification in archaeal and eukaryal translation elongation factor 2 (EF2). Its name refers to the… 
Highly Cited
2008
Highly Cited
2008
Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development
The intracellular target of diphtheria toxin is a modified histidine residue, diphthamide, in the translation elongation factor… 
Highly Cited
2006
Highly Cited
2006
Dph3, a Small Protein Required for Diphthamide Biosynthesis, Is Essential in Mouse Development
ABSTRACT The translation elongation factor 2 in eukaryotes (eEF-2) contains a unique posttranslationally modified histidine… 
Review
2005
Review
2005
OVCA1: tumor suppressor gene.
1996
1996
A cDNA from the ovarian cancer critical region of deletion on chromosome 17p13.3.
Highly Cited
1992
Highly Cited
1992
DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae
A mutant of Saccharomyces cerevisiae defective in the S-adenosylmethionine (AdoMet)-dependent methyltransferase step of… 
Highly Cited
1992
Highly Cited
1992
Saccharomyces cerevisiae elongation factor 2. Genetic cloning, characterization of expression, and G-domain modeling.
1987
1987
Highly frequent single amino acid substitution in mammalian elongation factor 2 (EF-2) results in expression of resistance to EF-2-ADP-ribosylating toxins.
Highly Cited
1984
Highly Cited
1984
In vitro biosynthesis of diphthamide, studied with mutant Chinese hamster ovary cells resistant to diphtheria toxin
Diphthamide, a unique amino acid, is a post-translational derivative of histidine that exists in protein synthesis elongation… 
Highly Cited
1980
Highly Cited
1980
ADP-ribosylation of elongation factor 2 by diphtheria toxin. NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products.
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