Evidence map›Paper›PMID 23798033›Full record

ReviewExtremophiles : life under extreme conditions2013

Thermodynamic and functional characteristics of deep-sea enzymes revealed by pressure effects.

Eiji Ohmae, Yurina Miyashita, Chiaki Kato

Abstract readReview
PubMed Publisher
In one paragraph

Review in Extremophiles : life under extreme conditions, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Enzymes from piezophiles.Seminars in cell & developmental biology · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Extreme biophysics: Enzymes under pressure.Journal of computational chemistry · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Eiji OhmaeDepartment of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan. ohmae@hiroshima-u.ac.jp
Yurina Miyashita
Chiaki Kato
Hiroshima University · JPJapan Agency for Marine-Earth Science and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydrostatic pressure analysis is an ideal approach for studying protein dynamics and hydration. The development of full ocean depth submersibles and high pressure biological techniques allows us to investigate enzymes from deep-sea organisms at the molecular level. The aim of this review was to overview the thermodynamic and functional characteristics of deep-sea enzymes as revealed by pressure axis analysis after giving a brief introduction to the thermodynamic principles underlying the effects of pressure on the structural stability and function of enzymes.

Indexed as

ThermodynamicsAmino Acid SequenceAquatic OrganismsBacteriaBacterial ProteinsEnzymesHydrostatic PressureMolecular Sequence DataBacterial ProteinsEnzymes

Identifiers

PMID23798033
OpenAlexW2038991486

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.