Evidence map›Paper›PMID 26738562›Full record

ArticleBMC evolutionary biology2016

Identification and classification of small molecule kinases: insights into substrate recognition and specificity.

Krishnadev Oruganty, Eric E Talevich, Andrew F Neuwald, Natarajan Kannan

Open access · goldAbstract read
In one paragraph

Article in BMC evolutionary biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. ACAD10 and ACAD11 enable mammalian 4-hydroxy acid lipid catabolism.Nature structural & molecular biology · 2025
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  4. Structural basis for FN3K-mediated protein deglycation.Structure (London, England : 1993) · 2024
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  6. Review
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  8. Metabolites · 2022
    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

4 authors at 3 institutions in 1 country.

Krishnadev OrugantyDepartment of Biochemistry & Molecular Biology, University of Georgia, Athens, GA, 30602, USA. okrishnadev@gmail.com.
Eric E TalevichDepartment of Pathology and Helen Diller Family Comprehensive Cancer Center, University of California, San Francisco, CA, 94158, USA. eric.talevich@gmail.com.
Andrew F NeuwaldInstitute for Genome Sciences and Department of Biochemistry & Molecular Biology, School of Medicine, University of Maryland, Baltimore, MD, 21201, USA. aneuwald@som.umaryland.edu.
Natarajan KannanDepartment of Biochemistry & Molecular Biology, University of Georgia, Athens, GA, 30602, USA. kannan@bmb.uga.edu.
University of Georgia · USUniversity of California, San Francisco · USUniversity of Maryland, Baltimore · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMany prokaryotic kinases that phosphorylate small molecule substrates, such as antibiotics, lipids and sugars, are evolutionarily related to Eukaryotic Protein Kinases (EPKs). These Eukaryotic-Like Kinases (ELKs) share the same overall structural fold as EPKs, but differ in their modes of regulation, substrate recognition and specificity-the sequence and structural determinants of which are poorly understood.

resultsTo better understand the basis for ELK specificity, we applied a Bayesian classification procedure designed to identify sequence determinants responsible for functional divergence. This reveals that a large and diverse family of aminoglycoside kinases, characterized members of which are involved in antibiotic resistance, fall into major sub-groups based on differences in putative substrate recognition motifs. Aminoglycoside kinase substrate specificity follows simple rules of alternating hydroxyl and amino groups that is strongly correlated with variations at the DFG + 1 position.

conclusionsSubstrate specificity determining features in small molecule kinases are mostly confined to the catalytic core and can be identified based on quantitative sequence and crystal structure comparisons.

Indexed as

Amino Acid SequenceBayes TheoremProtein KinasesProtein Structure, TertiarySubstrate SpecificityProtein Kinases

Identifiers

PMID26738562
PMCPMC4702295
OpenAlexW2231680986

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.