Evidence map›Paper›PMID 31155057›Full record

ArticleMethods in enzymology2019

Design and synthesis of fluorescent activity probes for protein phosphatases.

Garrett R Casey, Jon R Beck, Cliff I Stains

Abstract read
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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

3 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  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

3 authors at 2 institutions in 1 country.

Garrett R CaseyDepartment of Chemistry and Nebraska Center for Integrated Biomolecular Communication, University of Nebraska-Lincoln, Lincoln, NE, United States.
Jon R BeckDepartment of Chemistry and Nebraska Center for Integrated Biomolecular Communication, University of Nebraska-Lincoln, Lincoln, NE, United States.
Cliff I StainsDepartment of Chemistry and Nebraska Center for Integrated Biomolecular Communication, University of Nebraska-Lincoln, Lincoln, NE, United States; Cancer Genes and Molecular Recognition Program, Fred & Pamela Buffet Cancer Center, University of Nebraska Medical Center, Omaha, NE, United States. Electronic address: cstains2@unl.edu.
University of Nebraska–Lincoln · USUniversity of Nebraska Medical Center · US

Funding

Chemical Approaches for Interrogating Fundamental Biomedical ProcessesR35GM119751 · NIGMS · UNIVERSITY OF VIRGINIA · PI STAINS, CLIFF I · 2016 to 2020
$1.8M
NIGMS NIH HHS R35 GM119751
6 · The paper itself

Abstract

Protein phosphatases act in concert with protein kinases to regulate and maintain the phosphoproteome. However, the catalog of chemical tools to directly monitor the enzymatic activity of phosphatases has lagged behind their kinase counterparts. In this chapter, we provide protocols for repurposing the phosphorylation-sensitive sulfonamido-oxine fluorophore known as Sox to afford direct activity probes for phosphatases. With validated activity probes in-hand, inhibitor screens can be conducted with recombinant enzyme and the role of phosphatases in cell signaling can be investigated in unfractionated cell lysates.

Indexed as

AnimalsBiosensing TechniquesChemistry Techniques, SyntheticEnzyme AssaysFluorescent DyesHumansOxyquinolinePhosphoprotein PhosphatasesPhosphorylationSignal TransductionSpectrometry, FluorescenceSulfonamidesFluorescent DyesOxyquinolinePhosphoprotein PhosphatasesSulfonamidesBiosensorCell signalingFluorescent probesPhosphataseSensor

Identifiers

PMID31155057
PMCPMC6567983
OpenAlexW2921727096

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.