Evidence map›Paper›PMID 27998975›Full record

ArticleThe Journal of biological chemistry2017

The Major Protein Arginine Methyltransferase in

Lucie Kafková, Erik W Debler, John C Fisk, Kanishk Jain, Steven G Clarke, Laurie K Read

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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  6. Emerging functions of pseudoenzymes.The Biochemical journal · 2023
    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

6 authors at 2 institutions in 1 country.

Lucie KafkováFrom the Department of Microbiology and Immunology, Witebsky Center for Microbial Pathogenesis and Immunology, and Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, Buffalo, New York 14214.
Erik W Deblerthe Laboratory of Cell Biology, The Rockefeller University, New York, New York 10065, and.
John C FiskFrom the Department of Microbiology and Immunology, Witebsky Center for Microbial Pathogenesis and Immunology, and Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, Buffalo, New York 14214.
Kanishk Jainthe Department of Chemistry and Biochemistry and The Molecular Biology Institute, UCLA, Los Angeles, California 90095.
Steven G Clarkethe Department of Chemistry and Biochemistry and The Molecular Biology Institute, UCLA, Los Angeles, California 90095.
Laurie K ReadFrom the Department of Microbiology and Immunology, Witebsky Center for Microbial Pathogenesis and Immunology, and Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, Buffalo, New York 14214, lread@buffalo.edu.
University at Buffalo, State University of New York · USRockefeller University · US

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
Protein Arginine Methylation in TrypanosomesR01AI060260 · NIAID · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI READ, LAURIE K. · 2003 to 2014
$3.3M
Regulation of RNA editing in Trypansoma bruceiR01AI061580 · NIAID · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI READ, LAURIE K. · 2006 to 2015
$3.0M
CONTROL OF EUKARYOTIC MEMBRANE FUNCTION BY METHYLATIONR01GM026020 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CLARKE, STEVEN G · 1985 to 2013
$2.1M
NIAID NIH HHS R01 AI060260NIAID NIH HHS R01 AI061580NIGMS NIH HHS R01 GM026020NIGMS NIH HHS T32 GM007185
6 · The paper itself

Abstract

Prozymes are catalytically inactive enzyme paralogs that dramatically stimulate the function of weakly active enzymes through complex formation. The two prozymes described to date reside in the polyamine biosynthesis pathway of the human parasite

Indexed as

Amino Acid SequenceBiopolymersCatalytic DomainCell LineEnzyme StabilityProtein-Arginine N-MethyltransferasesProtein BindingProtein Processing, Post-TranslationalProtozoan ProteinsSequence Homology, Amino AcidTrypanosoma brucei bruceiBiopolymersProtein-Arginine N-MethyltransferasesProtozoan Proteinsallosteric regulationarginine methylationpost-translational modification (PTM)PRMTprotein methylationprozymeTrypanosoma bruceitrypanosome

Identifiers

PMID27998975
PMCPMC5313084
OpenAlexW2566458819

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.