Evidence map›Paper›PMID 30541869›Full record

ArticleMolecular & cellular proteomics : MCP2019

High-throughput Identification of FLT3 Wild-type and Mutant Kinase Substrate Preferences and Application to Design of Sensitive

Minervo Perez, John Blankenhorn, Kevin J Murray, Laurie L Parker

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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.

Minervo PerezFrom the ‡University of Minnesota, Department of Biochemistry, Molecular Biology and Biophysics, 420 Washington Avenue SE, Minneapolis, Minnesota 55455.ORCID 0000-0002-2768-4954
John BlankenhornFrom the ‡University of Minnesota, Department of Biochemistry, Molecular Biology and Biophysics, 420 Washington Avenue SE, Minneapolis, Minnesota 55455.
Kevin J Murray¶University of Minnesota, Department of Veterinary Population Medicine, 319 15 Avenue South East, Minneapolis, Minnesota 55455.
Laurie L ParkerFrom the ‡University of Minnesota, Department of Biochemistry, Molecular Biology and Biophysics, 420 Washington Avenue SE, Minneapolis, Minnesota 55455; llparker@umn.edu.ORCID 0000-0002-6234-3346
University of Minnesota · US

Funding

Biosensor Assay to Screen for Signaling Pathway Inhibition in CancerR01CA182543 · NCI · UNIVERSITY OF MINNESOTA · PI PARKER, LAURIE L. · 2014 to 2018
$2.1M
Multiplexed Kinase Biosensor Technology to Detect Leukemia Signaling with Mass SpR33CA183671 · NCI · UNIVERSITY OF MINNESOTA · PI PARKER, LAURIE L. · 2014 to 2017
$1.1M
NCI NIH HHS R01 CA182543NCI NIH HHS R33 CA183671
6 · The paper itself

Abstract

Acute myeloid leukemia (AML) is an aggressive disease that is characterized by abnormal increase of immature myeloblasts in blood and bone marrow. The FLT3 receptor tyrosine kinase plays an integral role in hematopoiesis, and one third of AML diagnoses exhibit gain-of-function mutations in FLT3, with the juxtamembrane domain internal tandem duplication (ITD) and the kinase domain D835Y variants observed most frequently. Few FLT3 substrates or phosphorylation sites are known, which limits insight into FLT3's substrate preferences and makes assay design particularly challenging. We applied

Indexed as

MutationCell Line, Tumorfms-Like Tyrosine Kinase 3High-Throughput Screening AssaysHumansLeukemia, Myeloid, AcutePhosphorylationProtein DomainsProtein Interaction MapsProteomicsTandem Repeat SequencesFLT3 protein, humanfms-Like Tyrosine Kinase 3Acute Myeloid LeukemiaAssay developmentFLT3FLT3-ITDKinase Assay-Linked with PhosphoproteomicsKINATEST-IDMass SpectrometryPhosphorylationSubstrate identificationTyrosine Kinases*

Identifiers

PMID30541869
PMCPMC6398213
OpenAlexW2951709812

What OpenQuestion holds

Textmetadata
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.