Evidence map›Paper›PMID 29544874›Full record

ReviewTrends in biochemical sciences2018

Homing in: Mechanisms of Substrate Targeting by Protein Kinases.

Chad J Miller, Benjamin E Turk

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
–field-weighted citation impact
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

121 citing papers in PubMed.

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61 more citing papers are in PubMed but not listed here.

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

2 authors.

Chad J MillerDepartment of Pharmacology, Yale School of Medicine, New Haven, CT 06520, USA.
Benjamin E TurkDepartment of Pharmacology, Yale School of Medicine, New Haven, CT 06520, USA. Electronic address: ben.turk@yale.edu.

Funding

Translational CoreP01DK057751 · NIDDK · YALE UNIVERSITY · PI YANG, XIAOYONG · 2001 to 2020
$25.6M
Structure-directed investigations into the regulation of Ste20 kinasesR01GM102262 · NIGMS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON · 2012 to 2025
$4.2M
Modeling human phosphorylation networks through kinome-wide profilingR01GM104047 · NIGMS · YALE UNIVERSITY · PI TURK, BENJAMIN E, YAFFE, MICHAEL B · 2013 to 2017
$2.4M
NIGMS NIH HHS R01 GM102262NIGMS NIH HHS R01 GM104047
6 · The paper itself

Abstract

Protein phosphorylation is the most common reversible post-translational modification in eukaryotes. Humans have over 500 protein kinases, of which more than a dozen are established targets for anticancer drugs. All kinases share a structurally similar catalytic domain, yet each one is uniquely positioned within signaling networks controlling essentially all aspects of cell behavior. Kinases are distinguished from one another based on their modes of regulation and their substrate repertoires. Coupling specific inputs to the proper signaling outputs requires that kinases phosphorylate a limited number of sites to the exclusion of hundreds of thousands of off-target phosphorylation sites. Here, we review recent progress in understanding mechanisms of kinase substrate specificity and how they function to shape cellular signaling networks.

Indexed as

HumansPhosphorylationProtein KinasesSignal TransductionSubstrate SpecificityProtein Kinasesenzyme specificitylinear sequence motifprotein interactionsprotein kinaseprotein phosphorylation

Identifiers

PMID29544874
PMCPMC5923429

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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.