Evidence map›Paper›PMID 17573429›Full record

ArticleBiophysical journal2007

Structural features that govern enzymatic activity in carbonic anhydrase from a low-temperature adapted fish, Chionodraco hamatus.

Stefano Marino, Kuniko Hayakawa, Keisuke Hatada, Maurizio Benfatto, Antonia Rizzello, Michele Maffia, Luigi Bubacco

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

7 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Complete mitochondrial genome of the Antarctic crocodile icefish,Mitochondrial DNA. Part B, Resources · 2016
    Article
  4. Phosphorylation increases the catalytic activity of rainbow trout gill cytosolic carbonic anhydrase.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2016
    Article
  5. Article
  6. Article
  7. 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

7 authors at 3 institutions in 1 country.

Stefano MarinoDepartment of Biology, University of Padova, Padua, Italy.
Kuniko Hayakawa
Keisuke Hatada
Maurizio Benfatto
Antonia Rizzello
Michele Maffia
Luigi Bubacco
University of Padua · ITIstituto Nazionale di Fisica Nucleare, Laboratori Nazionali di Frascati · ITUniversity of Salento · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The carbonic anhydrase (CA) family of zinc metalloenzymes includes many known isozymes that have different subcellular distributions. The study described here focuses on identification of the structural features that define low-temperature adaptation in a Chionodraco hamatus protein, both for the reaction center, at an atomic level, and for the tertiary structure of the protein. To this aim, an x-ray absorption near-edge spectroscopy/Minuit x-ray absorption near-edge spectroscopy analysis of the reaction center was undertaken for both a structurally characterized human CAII and CA of C. hamatus. Higher structural levels were analyzed by sequence comparison and homology modeling. To establish whether the structural insights acquired in fish CAs are general, theoretical models were generated by homology modeling for three temperate-climate-adapted fish CAs. The measured structural differences between the two proteins are discussed in terms of the differences in the electrostatic potential between human CAII and CA of C. hamatus. We conclude that modulation of the interaction between the catalytic water molecule and the zinc ion could depend on the effect of the electrostatic potential distribution.

Indexed as

Models, ChemicalModels, MolecularAdaptation, PhysiologicalAnimalsBinding SitesCarbonic AnhydrasesComputer SimulationEnzyme ActivationEnzyme StabilityFishesProtein BindingProtein ConformationStructure-Activity RelationshipTemperatureCarbonic Anhydrases

Identifiers

PMID17573429
PMCPMC1989726
OpenAlexW2093830705

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.