Evidence map›Paper›PMID 31606083›Full record

ArticleMethods in enzymology2019

Assays for tyrosine phosphorylation in human cells.

Monica Kruk, Naomi Widstrom, Sampreeti Jena, Nicole L Wolter, John F Blankenhorn, Ibrahim Abdalla, Tzu-Yi Yang, Laurie L Parker

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.2field-weighted citation impact, top 18% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

8 authors at 1 institution in 1 country.

Monica KrukDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, United States.
Naomi WidstromDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, United States.
Sampreeti JenaDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, United States.
Nicole L WolterDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, United States.
John F BlankenhornDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, United States.
Ibrahim AbdallaDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, United States.
Tzu-Yi YangDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, United States.
Laurie L ParkerDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, United States. Electronic address: llparker@umn.edu.
University of Minnesota · US

Funding

TRAINING GRANT IN MICROBIOLOGY/CANCER RESEARCHT32CA009138 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI Scott M. Dehm · 1985 to 2026
$11.3M
Project 2: Cell Migration in Mechanically Complex MicroenvironmentsU54CA210190 · NCI · UNIVERSITY OF MINNESOTA · PI LARGAESPADA, DAVID ANDREW, ODDE, DAVID J. · 2016 to 2020
$10.0M
Biosensor Assay to Screen for Signaling Pathway Inhibition in CancerR01CA182543 · NCI · UNIVERSITY OF MINNESOTA · PI PARKER, LAURIE L. · 2014 to 2018
$2.1M
Fluorescence lifetime-based single fluorophore biosensors of post-translational modification enzyme activityR33CA217780 · NCI · UNIVERSITY OF MINNESOTA · PI PARKER, LAURIE L. · 2017 to 2019
$1.3M
NCI NIH HHS R01 CA182543NCI NIH HHS R33 CA217780NCI NIH HHS T32 CA009138NCI NIH HHS U54 CA210190
6 · The paper itself

Abstract

Tyrosine kinases are important for many cellular processes and disruption of their regulation is a factor in diseases like cancer, therefore they are a major target of anticancer drugs. There are many ways to measure tyrosine kinase activity in cells by monitoring endogenous substrate phosphorylation, or by using peptide substrates and incubating them with cell lysates containing active kinases. However, most of these strategies rely on antibodies and/or are limited in how accurately they model the intracellular environment. In cases in which activity needs to be measured in cells, but endogenous substrates are not known and/or suitable phosphospecific antibodies are not available, cell-deliverable peptide substrates can be an alternative and can provide information on activation and inhibition of kinases in intact, live cells. In this chapter, we review this methodology and provide a protocol for measuring Abl kinase activity in human cells using enzyme-linked immunosorbent assay (ELISA) with a generic antiphosphotyrosine antibody for detection.

Indexed as

Enzyme-Linked Immunosorbent AssayHumansK562 CellsPhosphorylationProto-Oncogene Proteins c-ablSubstrate SpecificityTyrosineProto-Oncogene Proteins c-ablTyrosineAbl kinaseCell penetrating peptideK562 cellsKinase substrateTyrosine kinase assay

Identifiers

PMID31606083
PMCPMC7379381
OpenAlexW2962921168

What OpenQuestion holds

Textmetadata
LicenceTDM
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.