Evidence map›Paper›PMID 23063535›Full record

ArticleBiochimica et biophysica acta2013

Accessing the reproducibility and specificity of pepsin and other aspartic proteases.

Joomi Ahn, Min-Jie Cao, Ying Qing Yu, John R Engen

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

58 citing papers in PubMed, 154 citations in OpenAlex.

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  19. Review
  20. Fundamentals of HDX-MS.Essays in biochemistry · 2023
    Review
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

4 authors at 3 institutions in 2 countries.

Joomi AhnDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA 02115, USA.
Min-Jie Cao
Ying Qing Yu
John R Engen
Waters (United States) · USJimei University · CNNortheastern University · US

Funding

Protein conformational change upon membrane associationR01GM086507 · NIGMS · NORTHEASTERN UNIVERSITY · PI ENGEN, JOHN R · 2009 to 2012
$1.6M
Extending the applications of hydrogen exchange mass spectrometryR01GM101135 · NIGMS · NORTHEASTERN UNIVERSITY · PI ENGEN, JOHN R · 2012 to 2015
$1.2M
NIGMS NIH HHS GM086507NIGMS NIH HHS R01 GM086507NIGMS NIH HHS R01 GM101135
6 · The paper itself

Abstract

The aspartic protease pepsin is less specific than other endoproteinases. Because aspartic proteases like pepsin are active at low pH, they are utilized in hydrogen deuterium exchange mass spectrometry (HDX MS) experiments for digestion under hydrogen exchange quench conditions. We investigated the reproducibility, both qualitatively and quantitatively, of online and offline pepsin digestion to understand the compliment of reproducible pepsin fragments that can be expected during a typical pepsin digestion. The collection of reproducible peptides was identified from >30 replicate digestions of the same protein and it was found that the number of reproducible peptides produced during pepsin digestion becomes constant above 5-6 replicate digestions. We also investigated a new aspartic protease from the stomach of the rice field eel (Monopterus albus Zuiew) and compared digestion efficiency and specificity to porcine pepsin and aspergillopepsin. Unique cleavage specificity was found for rice field eel pepsin at arginine, asparagine, and glycine. Different peptides produced by the various proteases can enhance protein sequence coverage and improve the spatial resolution of HDX MS data. This article is part of a Special Issue entitled: Mass spectrometry in structural biology.

Indexed as

Amino Acid SequenceAnimalsArginineAsparagineAspartic Acid ProteasesDeuteriumDeuterium Exchange MeasurementEelsGlycineHorsesHydrogenMass SpectrometryMolecular Sequence DataPepsin APeptidesRabbitsArginineAsparagineAspartic Acid ProteasesDeuteriumGlycineHydrogenPepsin APeptides

Identifiers

PMID23063535
PMCPMC3553288
OpenAlexW2085981159

What OpenQuestion holds

Textmetadata
LicenceTDM
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.