Evidence map›Paper›PMID 28062577›Full record

ArticleThe Journal of biological chemistry2017

Overlapping Specificity of Duplicated Human Pancreatic Elastase 3 Isoforms and Archetypal Porcine Elastase 1 Provides Clues to Evolution of Digestive Enzymes.

Eszter Boros, András Szabó, Katalin Zboray, Dávid Héja, Gábor Pál, Miklós Sahin-Tóth

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
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  6. Homology-based identification and structural analysis ofComputational and structural biotechnology journal · 2024
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  10. Substrate specificity of human chymotrypsin-like protease (CTRL) characterized by phage display-selected small-protein inhibitors.Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.] · 2023
    Article
  11. Article
  12. Loss-of-function variant in chymotrypsin like elastase 3B (CELA3B) is associated with non-alcoholic chronic pancreatitis.Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.] · 2022
    Article
  13. Article
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  16. Detection of human elastase isoforms by the ScheBo Pancreatic Elastase 1 Test.American journal of physiology. Gastrointestinal and liver physiology · 2017
    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

6 authors at 2 institutions in 2 countries.

Eszter BorosFrom the Department of Biochemistry, Eötvös Loránd University, Budapest 1117, Hungary and.
András SzabóDepartment of Molecular and Cell Biology, Boston University Henry M. Goldman School of Dental Medicine, Boston, Massachusetts 02118.
Katalin ZborayFrom the Department of Biochemistry, Eötvös Loránd University, Budapest 1117, Hungary and.
Dávid HéjaFrom the Department of Biochemistry, Eötvös Loránd University, Budapest 1117, Hungary and.
Gábor PálFrom the Department of Biochemistry, Eötvös Loránd University, Budapest 1117, Hungary and gabor.pal@ttk.elte.hu.
Miklós Sahin-TóthDepartment of Molecular and Cell Biology, Boston University Henry M. Goldman School of Dental Medicine, Boston, Massachusetts 02118 miklos@bu.edu.ORCID 0000-0003-4513-9922
Eötvös Loránd University · HUBoston University · US

Funding

Chymotrypsin in pancreatitisR01DK082412 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SAHIN-TOTH, MIKLOS · 2009 to 2024
$5.8M
Molecular Pathomechanism of Hereditary PancreatitisR01DK058088 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SAHIN-TOTH, MIKLOS · 2001 to 2019
$5.3M
Pancreatic elastasesR01DK095753 · NIDDK · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SAHIN-TOTH, MIKLOS · 2013 to 2016
$1.4M
NIDDK NIH HHS R01 DK058088NIDDK NIH HHS R01 DK082412NIDDK NIH HHS R01 DK095753
6 · The paper itself

Abstract

Chymotrypsin-like elastases (CELAs) are pancreatic serine proteinases that digest dietary proteins. CELAs are typically expressed in multiple isoforms that can vary among different species. The human pancreas does not express CELA1 but secretes two CELA3 isoforms, CELA3A and CELA3B. The reasons for the CELA3 duplication and the substrate preferences of the duplicated isoforms are unclear. Here, we tested whether CELA3A and CELA3B evolved unique substrate specificities to compensate for the loss of CELA1. We constructed a phage library displaying variants of the substrate-like

Indexed as

Evolution, MolecularAmino Acid SequenceAnimalsBacteriophagesHumansInsect ProteinsIsoenzymesKineticsPancreatic ElastasePeptidesSubstrate SpecificitySwineInsect ProteinsIsoenzymesLOC126284306 protein, Schistocerca gregariaPancreatic ElastasePeptideschymotrypsinchymotrypsin Celastasepancreasphage displayprotease inhibitorserine protease

Identifiers

PMID28062577
PMCPMC5314167
OpenAlexW2569172367

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.