Evidence map›Paper›PMID 17976195›Full record

ArticleThe FEBS journal2007

Purification and characterization of pepsins A1 and A2 from the Antarctic rock cod Trematomus bernacchii.

Sébastien Brier, Giovanna Maria, Vincenzo Carginale, Antonio Capasso, Yan Wu, Robert M Taylor, Nicholas B Borotto, Clemente Capasso, John R Engen

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The FEBS journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.5field-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

12 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Gas-Phase Hydrogen/Deuterium Scrambling in Negative-Ion Mode Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019
    Article
  7. Article
  8. Analytical Aspects of Hydrogen Exchange Mass Spectrometry.Annual review of analytical chemistry (Palo Alto, Calif.) · 2015
    Review
  9. Article
  10. Article
  11. Hydrogen exchange mass spectrometry: are we out of the quicksand?Journal of the American Society for Mass Spectrometry · 2012
    Review
  12. 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

9 authors at 2 institutions in 2 countries.

Sébastien BrierDepartment of Chemistry & Chemical Biology and The Barnett Institute for Chemical & Biological Analysis, Northeastern University, Boston, MA, USA.
Giovanna Maria
Vincenzo Carginale
Antonio Capasso
Yan Wu
Robert M Taylor
Nicholas B Borotto
Clemente Capasso
John R Engen
Northeastern University · USInstitute of Protein Biochemistry · IT

Funding

Structural Dynamics of Src-Family Kinase ActivationR01GM070590 · NIGMS · UNIVERSITY OF NEW MEXICO · PI ENGEN, JOHN R · 2004 to 2008
$1.5M
NIGMS NIH HHS GM070590NIGMS NIH HHS R01 GM070590
6 · The paper itself

Abstract

The Antarctic notothenioid Trematomus bernacchii (rock cod) lives at a constant mean temperature of -1.9 degrees C. Gastric digestion under these conditions relies on the proteolytic activity of aspartic proteases such as pepsin. To understand the molecular mechanisms of Antarctic fish pepsins, T. bernacchii pepsins A1 and A2 were cloned, overexpressed in Escherichia coli, purified and characterized with a number of biochemical and biophysical methods. The properties of these two Antarctic isoenzymes were compared to those of porcine pepsin and found to be unique in a number of ways. Fish pepsins were found to be more temperature sensitive, generally less active at lower pH and more sensitive to inhibition by pepstatin than their mesophilic counterparts. The specificity of Antarctic fish pepsins was similar but not identical to that of pig pepsin, probably owing to changes in the sequence of fish enzymes near the active site. Gene duplication of Antarctic rock cod pepsins is the likely mechanism for adaptation to the harsh temperature environment in which these enzymes must function.

Indexed as

Amino Acid SequenceAnimalsAntarctic RegionsBinding SitesCloning, MolecularEnzyme PrecursorsEnzyme StabilityEscherichia coliGastric MucosaHydrogen-Ion ConcentrationInclusion BodiesIsoenzymesKineticsModels, MolecularMolecular Sequence DataMolecular WeightEnzyme PrecursorsIsoenzymesPepsin ApepstatinPepstatinsProtease InhibitorsRecombinant Proteins

Identifiers

PMID17976195
PMCPMC2533623
OpenAlexW1494136800

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.