Pyrococcus horikoshii

"Pyrococcus horikoshii" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

Anaerobic hyperthermophilic species of ARCHAEA, isolated from hydrothermal fluid samples. It is obligately heterotrophic with coccoid cells that require TRYPTOPHAN for growth.

Descriptor ID

D043902

MeSH Number(s)

B02.200.825.800.650.400

Concept/Terms

Pyrococcus horikoshii

Below are MeSH descriptors whose meaning is more general than "Pyrococcus horikoshii".

Organisms [B]
Archaea [B02]
Euryarchaeota [B02.200]
Thermococcales [B02.200.825]
Thermococcaceae [B02.200.825.800]
Pyrococcus [B02.200.825.800.650]
Pyrococcus horikoshii [B02.200.825.800.650.400]

Below are MeSH descriptors whose meaning is related to "Pyrococcus horikoshii".

Below are MeSH descriptors whose meaning is more specific than "Pyrococcus horikoshii".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Pyrococcus horikoshii" by people in Harvard Catalyst Profiles by year, and whether "Pyrococcus horikoshii" was a major or minor topic of these publication.

Bar chart showing 5 publications over 5 distinct years, with a maximum of 1 publications in 2010 and 2013 and 2015 and 2017 and 2018

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
2010	1	0	1
2013	1	0	1
2015	1	0	1
2017	0	1	1
2018	0	1	1

Below are the most recent publications written about "Pyrococcus horikoshii" by people in Profiles.

A facile approach for the in vitro assembly of multimeric membrane transport proteins. Elife. 2018 06 11; 7.

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Alteration of molecular assembly of peroxiredoxins from hyperthermophilic archaea. J Biochem. 2017 Dec 01; 162(6):415-422.

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Transport domain unlocking sets the uptake rate of an aspartate transporter. Nature. 2015 Feb 05; 518(7537):68-73.

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Comparison of the intrinsic dynamics of aminoacyl-tRNA synthetases. Protein J. 2014 Apr; 33(2):184-98.

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Dph3 is an electron donor for Dph1-Dph2 in the first step of eukaryotic diphthamide biosynthesis. J Am Chem Soc. 2014 Feb 05; 136(5):1754-7.

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Transport dynamics in a glutamate transporter homologue. Nature. 2013 Oct 03; 502(7469):114-8.

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Reconstitution of diphthine synthase activity in vitro. Biochemistry. 2010 Nov 09; 49(44):9649-57.

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Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis. Mol Biosyst. 2011 Jan; 7(1):74-81.

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The 3-4 loop of an archaeal glutamate transporter homolog experiences ligand-induced structural changes and is essential for transport. Proc Natl Acad Sci U S A. 2010 Jul 20; 107(29):12840-5.

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Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme. Nature. 2010 Jun 17; 465(7300):891-6.

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