Evidence map›Paper›PMID 37179332›Full record

ArticleNature communications2023

Prenylcysteine oxidase 1 like protein is required for neutrophil bactericidal activities.

Anastasiia Petenkova, Shelby A Auger, Jeffrey Lamb, Daisy Quellier, Cody Carter, On Tak To, Jelena Milosevic, Rana Barghout, Abirami Kugadas, Xiaoxiao Lu and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. With a little help from a friend - a new partner for acid-sensitive channels.Pflugers Archiv : European journal of physiology · 2026
    Article
  3. ACS chemical biology · 2025
    Article
  4. Article
  5. Article
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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

15 authors at 5 institutions in 2 countries.

Anastasiia PetenkovaDepartment of Medicine, Division of Infectious Diseases, Mass General Brigham, Harvard Medical School, Boston, MA, 02115, USA.ORCID 0000-0002-7253-623X
Shelby A AugerDepartment of Chemistry, University of Minnesota, Minneapolis, MN, 55455, USA.ORCID 0000-0003-2873-2580
Jeffrey LambDepartment of Medicine, Division of Infectious Diseases, Mass General Brigham, Harvard Medical School, Boston, MA, 02115, USA.
Daisy QuellierDepartment of Medicine, Division of Infectious Diseases, Mass General Brigham, Harvard Medical School, Boston, MA, 02115, USA.
Cody CarterDepartment of Medicine, Division of Infectious Diseases, Mass General Brigham, Harvard Medical School, Boston, MA, 02115, USA.
On Tak ToDepartment of Medicine, Division of Infectious Diseases, Mass General Brigham, Harvard Medical School, Boston, MA, 02115, USA.
Jelena MilosevicCenter for Regenerative Medicine, Massachusetts General Hospital, Boston, MA, 02114, USA.
Rana BarghoutCenter for Regenerative Medicine, Massachusetts General Hospital, Boston, MA, 02114, USA.
Abirami KugadasDepartment of Medicine, Division of Infectious Diseases, Mass General Brigham, Harvard Medical School, Boston, MA, 02115, USA.
Xiaoxiao LuDepartment of Medicine, Division of Infectious Diseases, Mass General Brigham, Harvard Medical School, Boston, MA, 02115, USA.
Jennifer Geddes-McAlisterMolecular and Cellular Biology Department, University of Guelph, Guelph, ON, N1G 2W1, Canada.ORCID 0000-0002-4257-2096
Raina FichorovaDepartment of Obstetrics, Gynecology, and Reproductive Biology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, 02115, USA.
David B SykesCenter for Regenerative Medicine, Massachusetts General Hospital, Boston, MA, 02114, USA.ORCID 0000-0002-9788-0221
Mark D DistefanoDepartment of Chemistry, University of Minnesota, Minneapolis, MN, 55455, USA.ORCID 0000-0002-2872-0259
Mihaela GadjevaDepartment of Medicine, Division of Infectious Diseases, Mass General Brigham, Harvard Medical School, Boston, MA, 02115, USA. mgadjeva@fas.harvard.edu.ORCID 0000-0002-9014-386X
Harvard University · USMassachusetts General Hospital · USUniversity of Minnesota · USBrigham and Women's Hospital · USUniversity of Guelph · CA

Funding

Women's CancerP30CA077598 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI Timothy C. Hallstrom · 1998 to 2026
$100.4M
Training Grant: Functional Proteomics of AgingT32AG029796 · NIA · UNIVERSITY OF MINNESOTA · PI EDGAR A ARRIAGA, Douglas G Mashek · 2008 to 2026
$6.6M
Novel treatment strategies to regulate inflammation during P.aeruginosa keratitisR01EY022054 · NEI · BRIGHAM AND WOMEN'S HOSPITAL · PI GADJEVA, MIHAELA GUEORGUIEVA · 2012 to 2020
$4.0M
Training the Next Generation of Chemical BiologistsT32GM132029 · NIGMS · UNIVERSITY OF MINNESOTA · PI Erin Elizabeth Carlson, William Charles Krause Pomerantz · 2019 to 2026
$2.7M
Chemical Approaches for Exploring Protein Prenylation in Living CellsR35GM141853 · NIGMS · UNIVERSITY OF MINNESOTA · PI MARK D DISTEFANO · 2021 to 2026
$2.4M
Developing differentiation therapy for the treatment of patients with acute myeloid leukemiaK08CA201640 · NCI · MASSACHUSETTS GENERAL HOSPITAL · PI SYKES, DAVID B · 2017 to 2020
$677k
NCI NIH HHS K08 CA201640NCI NIH HHS P30 CA077598NEI NIH HHS R01 EY022054NIA NIH HHS T32 AG029796NIGMS NIH HHS R35 GM141853NIGMS NIH HHS T32 GM132029
6 · The paper itself

Abstract

The bactericidal function of neutrophils is dependent on a myriad of intrinsic and extrinsic stimuli. Using systems immunology approaches we identify microbiome- and infection-induced changes in neutrophils. We focus on investigating the Prenylcysteine oxidase 1 like (Pcyox1l) protein function. Murine and human Pcyox1l proteins share ninety four percent aminoacid homology revealing significant evolutionary conservation and implicating Pcyox1l in mediating important biological functions. Here we show that the loss of Pcyox1l protein results in significant reductions in the mevalonate pathway impacting autophagy and cellular viability under homeostatic conditions. Concurrently, Pcyox1l CRISPRed-out neutrophils exhibit deficient bactericidal properties. Pcyox1l knock-out mice demonstrate significant susceptibility to infection with the gram-negative pathogen Psuedomonas aeruginosa exemplified through increased neutrophil infiltrates, hemorrhaging, and reduced bactericidal functionality. Cumulatively, we ascribe a function to Pcyox1l protein in modulation of the prenylation pathway and suggest connections beween metabolic responses and neutrophil functionality.

Indexed as

NeutrophilsProteinsAnimalsCarbon-Sulfur LyasesCysteineHumansMiceMice, KnockoutOxidoreductasesCarbon-Sulfur LyasesCysteineOxidoreductasesPcyox1 protein, mouseprenylcysteineProteins

Identifiers

PMID37179332
PMCPMC10182992
OpenAlexW4376612764

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.