Evidence map›Paper›PMID 26501912›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2016

Rapid Identification of Protein Kinase Phosphorylation Site Motifs Using Combinatorial Peptide Libraries.

Chad J Miller, Benjamin E Turk

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
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  6. Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024
    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

2 authors.

Chad J MillerDepartment of Pharmacology, Yale University School of Medicine, 333 Cedar Street, 208066, New Haven, CT, 06520, USA.
Benjamin E TurkDepartment of Pharmacology, Yale University School of Medicine, 333 Cedar Street, 208066, New Haven, CT, 06520, USA. ben.turk@yale.edu.

Funding

INSTITUTIONAL NATIONAL RESEARCH SERVICE AWARDT32GM007324 · NIGMS · YALE UNIVERSITY · PI BENNETT, ANTON M · 1987 to 2022
$6.2M
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 GM104047NIGMS NIH HHS T32 GM007324
6 · The paper itself

Abstract

Eukaryotic protein kinases phosphorylate substrates at serine, threonine, and tyrosine residues that fall within the context of short sequence motifs. Knowing the phosphorylation site motif for a protein kinase facilitates designing substrates for kinase assays and mapping phosphorylation sites in protein substrates. Here, we describe an arrayed peptide library protocol for rapidly determining kinase phosphorylation consensus sequences. This method uses a set of peptide mixtures in which each of the 20 amino acid residues is systematically substituted at nine positions surrounding a central site of phosphorylation. Peptide mixtures are arrayed in multiwell plates and analyzed by radiolabel assay with the kinase of interest. The preferred sequence is determined from the relative rate of phosphorylation of each peptide in the array. Consensus peptides based on these sequences typically serve as efficient and specific kinase substrates for high-throughput screening or incorporation into biosensors.

Indexed as

Amino Acid MotifsProtein Processing, Post-TranslationalAmino Acid SequenceCombinatorial Chemistry TechniquesConsensus SequenceHumansImage Processing, Computer-AssistedIndicators and ReagentsPeptide LibraryPhosphorylationProtein KinasesSignal TransductionSpectrophotometry, UltravioletSubstrate SpecificityIndicators and ReagentsPeptide LibraryProtein KinasesEnzyme specificityKinase assayPeptide librariesProtein kinasesSignal transductionSubstrate profiling

Identifiers

PMID26501912
PMCPMC4784478

What OpenQuestion holds

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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.