Evidence map›Paper›PMID 36215509›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Blockade of the protease ADAM17 ameliorates experimental pancreatitis.

Mohamed I Saad, Teresa Weng, Joanne Lundy, Linden J Gearing, Alison C West, Christopher M Harpur, Mohammad Alanazi, Christopher Hodges, Daniel Croagh, Beena Kumar and 3 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  8. Targeted therapeutics for pancreatitis.Frontiers in physiology · 2026
    Review
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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

13 authors at 5 institutions in 3 countries.

Mohamed I SaadDepartment of Molecular and Translational Science, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, VIC 3800, Australia.ORCID 0000-0002-4855-2360
Teresa WengDepartment of Molecular and Translational Science, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, VIC 3800, Australia.ORCID 0000-0003-2262-7587
Joanne LundyDepartment of Molecular and Translational Science, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, VIC 3800, Australia.
Linden J GearingDepartment of Molecular and Translational Science, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, VIC 3800, Australia.
Alison C WestDepartment of Molecular and Translational Science, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, VIC 3800, Australia.
Christopher M HarpurDepartment of Molecular and Translational Science, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, VIC 3800, Australia.
Mohammad AlanaziDepartment of Molecular and Translational Science, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, VIC 3800, Australia.
Christopher HodgesDepartment of Molecular and Translational Science, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, VIC 3800, Australia.
Daniel CroaghDepartment of Surgery, School of Clinical Sciences, Monash University, VIC 3168, Australia.
Beena KumarDepartment of Anatomical Pathology, Monash Health, Clayton, VIC 3168, Australia.
Irit SagiDepartment of Biological Regulation, Weizmann Institute of Science, Rehovot 7610001, Israel.ORCID 0000-0001-5595-5515
Stefan Rose-JohnInstitute of Biochemistry, Christian-Albrechts-University, Kiel 24118, Germany.ORCID 0000-0002-7519-3279
Brendan J JenkinsDepartment of Molecular and Translational Science, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, VIC 3800, Australia.
Hudson Institute of Medical Research · AUChristian-Albrechts-Universität zu Kiel · DEMonash Health · AUMonash University · AUWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acute and chronic pancreatitis, the latter associated with fibrosis, are multifactorial inflammatory disorders and leading causes of gastrointestinal disease-related hospitalization. Despite the global health burden of pancreatitis, currently, there are no effective therapeutic agents. In this regard, the protease A Disintegrin And Metalloproteinase 17 (ADAM17) mediates inflammatory responses through shedding of bioactive inflammatory cytokines and mediators, including tumor necrosis factor α (TNFα) and the soluble interleukin (IL)-6 receptor (sIL-6R), the latter of which drives proinflammatory IL-6 trans-signaling. However, the role of ADAM17 in pancreatitis is unclear. To address this,

Indexed as

NitrosaminesPancreatitisAcute DiseaseADAM17 ProteinAnimalsCarcinogensCeruletideCytokinesDisintegrinsEndopeptidasesFibrosisInterleukin-6KetonesMiceNicotinePeptide HydrolasesADAM17 ProteinAdam17 protein, mouseCarcinogensCeruletideCytokinesDisintegrinsEndopeptidasesInterleukin-6KetonesNicotineNitrosaminesPeptide HydrolasesTumor Necrosis Factor-alphaADAM17ADAM17 prodomain inhibitorapoptosisinflammationpancreatitis

Identifiers

PMID36215509
PMCPMC9586293
OpenAlexW4304099399

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.