Evidence map›Paper›PMID 35625613›Full record

ReviewBiomolecules2022

Kinases on Double Duty: A Review of UniProtKB Annotated Bifunctionality within the Kinome.

Aziz M Rangwala, Victoria R Mingione, George Georghiou, Markus A Seeliger

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 53% 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

3 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

4 authors at 1 institution in 1 country.

Aziz M RangwalaDepartment of Pharmacological Sciences, Renaissance School of Medicine, Stony Brook University, Stony Brook, NY 11794, USA.ORCID 0000-0003-3556-7931
Victoria R MingioneDepartment of Pharmacological Sciences, Renaissance School of Medicine, Stony Brook University, Stony Brook, NY 11794, USA.ORCID 0000-0001-9367-6082
George GeorghiouDepartment of Pharmacological Sciences, Renaissance School of Medicine, Stony Brook University, Stony Brook, NY 11794, USA.ORCID 0000-0001-5067-3199
Markus A SeeligerDepartment of Pharmacological Sciences, Renaissance School of Medicine, Stony Brook University, Stony Brook, NY 11794, USA.ORCID 0000-0003-0990-1756
Stony Brook School · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM008444 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI FROHMAN, MICHAEL A. · 1992 to 2024
$12.6M
Dynamics of Ligand Binding and Protein Kinase Regulation_RenewalR35GM119437 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI Markus A Seeliger · 2016 to 2026
$6.5M
Scholars in BioMedical Sciences (SBMS) Training ProgramT32GM127253 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI TSIRKA, STYLIANI-ANNA (STELLA) E · 2018 to 2022
$689k
Elucidating the Role of Binding Kinetics in the Development of Abl Kinase Drug ResistanceF30CA260771 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI RANGWALA, AZIZ MOHAMMEDI · 2021 to 2024
$184k
NIH HHS F30 CA260771NIH HHS R35 GM119437NIH HHS T32 GM008444NIH HHS T32 GM127253
6 · The paper itself

Abstract

Phosphorylation facilitates the regulation of all fundamental biological processes, which has triggered extensive research of protein kinases and their roles in human health and disease. In addition to their phosphotransferase activity, certain kinases have evolved to adopt additional catalytic functions, while others have completely lost all catalytic activity. We searched the Universal Protein Resource Knowledgebase (UniProtKB) database for bifunctional protein kinases and focused on kinases that are critical for bacterial and human cellular homeostasis. These kinases engage in diverse functional roles, ranging from environmental sensing and metabolic regulation to immune-host defense and cell cycle control. Herein, we describe their dual catalytic activities and how they contribute to disease pathogenesis.

Indexed as

Knowledge BasesProtein KinasesHumansPhosphorylationProtein Kinasescancerinflammationkinasemetabolismphosphorylationsignal transduction

Identifiers

PMID35625613
PMCPMC9138534
OpenAlexW4280644273

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.