Evidence map›Paper›PMID 31427437›Full record

ArticleThe Journal of biological chemistry2019

A two-component protease in

Ana M Martins, John A Latham, Paulo J Martel, Ian Barr, Anthony T Iavarone, Judith P Klinman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

13 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Microbial synthesis of pyrroloquinoline quinone.World journal of microbiology & biotechnology · 2023
    Review
  5. Characterization of the Pyrroloquinoline Quinone ProducingInternational journal of molecular sciences · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. 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 3 institutions in 2 countries.

Ana M MartinsCalifornia Institute for Quantitative Biosciences, University of California Berkeley, Berkeley, California 94720.
John A LathamDepartment of Chemistry and Biochemistry, University of Denver, Denver, Colorado 8020.ORCID 0000-0002-3034-1768
Paulo J MartelCentre for Biomedical Research, Faculty of Sciences and Technology, University of the Algarve, 8005-139 Faro, Portugal.
Ian BarrCalifornia Institute for Quantitative Biosciences, University of California Berkeley, Berkeley, California 94720.
Anthony T IavaroneCalifornia Institute for Quantitative Biosciences, University of California Berkeley, Berkeley, California 94720.
Judith P KlinmanCalifornia Institute for Quantitative Biosciences, University of California Berkeley, Berkeley, California 94720 klinman@berkeley.edu.ORCID 0000-0001-5734-2843
QB3 · USUniversity of Algarve · PTUniversity of Denver · US

Funding

Looking in New Directions for Origins and Cryptic Mechanisms of Enzyme CatalysisR35GM118117 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH P · 2016 to 2025
$7.5M
Elucidating the biosynthesis of mycofactocin, an unknown molecule essential for M. tuberculosisR01GM124002 · NIGMS · UNIVERSITY OF DENVER (COLORADO SEMINARY) · PI EATON, SANDRA S. · 2017 to 2021
$1.6M
High Definition Ion Mobility SpectrometerS10OD020062 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI WILLIAMS, EVAN R · 2015 to 2015
$590k
NIGMS NIH HHS R01 GM124002NIGMS NIH HHS R35 GM118117NIH HHS S10 OD020062
6 · The paper itself

Abstract

Pyrroloquinoline quinone is a prominent redox cofactor in many prokaryotes, produced from a ribosomally synthesized and post-translationally modified peptide PqqA via a pathway comprising four conserved proteins PqqB-E. These four proteins are now fairly well-characterized and span radical SAM activity (PqqE), aided by a peptide chaperone (PqqD), a dual hydroxylase (PqqB), and an eight-electron, eight-proton oxidase (PqqC). A full description of this pathway has been hampered by a lack of information regarding a protease/peptidase required for the excision of an early, cross-linked di-amino acid precursor to pyrroloquinoline quinone. Herein, we isolated and characterized a two-component heterodimer protein from the α-proteobacterium

Indexed as

AlphaproteobacteriaAmino Acid SequenceCoenzymesModels, MolecularOxidation-ReductionPeptide HydrolasesPQQ CofactorProtein BindingProtein MultimerizationProtein Processing, Post-TranslationalProtein Structure, QuaternaryCoenzymesPeptide HydrolasesPQQ Cofactorenzyme catalysisheterodimerM16B proteasepeptidesPQQproteaseserinezinc

Identifiers

PMID31427437
PMCPMC6791305
OpenAlexW2969583714

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.