Evidence map›Paper›PMID 26490465›Full record

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

Analysis of Protein Tyrosine Kinase Specificity Using Positional Scanning Peptide Microarrays.

Yang Deng, Benjamin E Turk

Abstract read
PubMed Full text at PMC Publisher
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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  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

2 authors.

Yang DengDepartment of Biomedical Engineering, Yale University, New Haven, CT, USA.
Benjamin E TurkDepartment of Pharmacology, Yale University School of Medicine, SHM B395e, 333 Cedar Street, New Haven, CT, 06520, USA. ben.turk@yale.edu.

Funding

Modeling human phosphorylation networks through kinome-wide profilingR01GM104047 · NIGMS · YALE UNIVERSITY · PI TURK, BENJAMIN E, YAFFE, MICHAEL B · 2013 to 2017
$2.4M
Phosphorylation networks regulated by energy stress in yeastR01GM105947 · NIGMS · YALE UNIVERSITY · PI TURK, BENJAMIN E · 2013 to 2016
$1.3M
Global peptide microarray profiling of tyrosine kinases deregulated in cancerR21CA147993 · NCI · YALE UNIVERSITY · PI TURK, BENJAMIN E · 2010 to 2011
$349k
NCI NIH HHS R21 CA147993NIGMS NIH HHS R01 GM104047NIGMS NIH HHS R01 GM105947
6 · The paper itself

Abstract

Protein tyrosine kinases phosphorylate their substrates within the context of specific consensus sequences surrounding the site of modification. We describe a peptide microarray approach to rapidly determine tyrosine kinase phosphorylation site motifs. This method uses a peptide library that systematically substitutes each of the amino acid residues at multiple positions surrounding a central tyrosine residue. Peptide substrates are synthesized as biotin conjugates for immobilization on avidin-coated slides. Following incubation of the slide with protein kinase and radiolabeled ATP, the relative extent of phosphorylation of each of the peptides is quantified by phosphor imaging. This method allows small quantities of kinase to be analyzed rapidly in parallel, facilitating analysis of large numbers of kinases.

Indexed as

AvidinPrintingProtein Array AnalysisProtein-Tyrosine KinasesSubstrate SpecificityAvidinProtein-Tyrosine KinasesEnzyme specificityKinase assayPeptide microarraysProtein tyrosine kinase sSignal transductionSubstrate profiling

Identifiers

PMID26490465
PMCPMC4814292

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.