Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A Unique Modification of the Eukaryotic Initiation Factor 5A Shows the Presence of the Complete Hypusine Pathway in Leishmania donovani

16 Mar 2012

Abstract excerpt

Deoxyhypusine hydroxylase (DOHH) catalyzes the final step in the post-translational synthesis of an unusual amino acid hypusine (N(€)-(4-amino-2-hydroxybutyl) lysine), which is present on only one cellular protein, eukaryotic initiation factor 5A (eIF5A). We present here the molecular and structural basis of the function of DOHH from the protozoan parasite, Leishmania donovani, which causes visceral...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Polyamine Metabolism and Applications
Share to Research on Leishmaniasis Studies
Share to Trypanosoma species research and implications

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 22438895
DOI: 10.1371/journal.pone.0033138

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A Unique Modification of the Eukaryotic Initiation Factor 5A Shows the Presence of the Complete Hypusine Pathway in Leishmania donovaniPMID 22438895Read ↗

Identification and Characterization of a Novel Deoxyhypusine Synthase in Leishmania donovaniSemantic proximity Read ↗

Specificity of the deoxyhypusine hydroxylase-eukaryotic translation initiation factor (eIF5A) interaction: identification of amino acid residues of the enzyme required for binding of its substrate, deoxyhypusine-containing eIF5A.Semantic proximity Read ↗

Deoxyhypusine hydroxylase is a Fe(II)-dependent, HEAT-repeat enzyme. Identification of amino acid residues critical for Fe(II) binding and catalysis [corrected].Semantic proximity Read ↗

Posttranslational hypusination of the eukaryotic translation initiation factor-5A regulates Fusarium graminearum virulence.Semantic proximity Read ↗

Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesis.Semantic proximity Read ↗

Eukaryotic translation initiation factor 5A and its hypusination play an important role in proliferation and differentiation of the human enteric protozoan parasite <i>Entamoeba histolytica</i>Semantic proximity Read ↗

Bromodomain factor 5 is an essential regulator of transcription in LeishmaniaSemantic proximity Read ↗

Combined structural and functional investigation of a C-3''-ketoreductase involved in the biosynthesis of dTDP-L-digitoxose.Semantic proximity Read ↗

The Drosophila deoxyhypusine hydroxylase homologue nero and its target eIF5A are required for cell growth and the regulation of autophagy.Semantic proximity Read ↗

Functional analysis of the Mycobacterium tuberculosis FAD-dependent thymidylate synthase, ThyX, reveals new amino acid residues contributing to an extended ThyX motif.Semantic proximity Read ↗

Isolation and molecular characterization of the shikimate dehydrogenase domain from the Toxoplasma gondii AROM complex.Semantic proximity Read ↗

Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.