Evidence map›Paper›PMID 22365604›Full record

ArticleChemistry & biology2012

Interrogating signaling nodes involved in cellular transformations using kinase activity probes.

Cliff I Stains, Nathan C Tedford, Traci C Walkup, Elvedin Luković, Brenda N Goguen, Linda G Griffith, Douglas A Lauffenburger, Barbara Imperiali

Open access · bronzeAbstract read
In one paragraph

Article in Chemistry & biology, 2012. 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
3.1field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. A Constellation of Fluorescent Biosensors to Illuminate the Galaxy of Protein Kinases.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Quantification of Cell Signaling Networks Using Kinase Activity Chemosensors.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Differential sensing of MAP kinases using SOX-peptides.Angewandte Chemie (International ed. in English) · 2014
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Profile of Barbara Imperiali.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  20. 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.

Cliff I StainsDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Nathan C Tedford
Traci C Walkup
Elvedin Luković
Brenda N Goguen
Linda G Griffith
Douglas A Lauffenburger
Barbara Imperiali
Massachusetts Institute of Technology · US

Funding

STRUCTUREU54GM064346 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI IMPERIALI, BARBARA · 2001 to 2010
$74.9M
Tumor Cell Networks CenterU54CA112967 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LAUFFENBURGER, DOUGLAS A · 2004 to 2015
$26.2M
Design, Synthesis, and Application of a Real-Time MAPK Activity SensorF32GM085909 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI STAINS, CLIFF I · 2008 to 2010
$138k
NCI NIH HHS U54 CA112967NCI NIH HHS U54-CA112967NIGMS NIH HHS F32 GM085909NIGMS NIH HHS F32GM085909NIGMS NIH HHS GM064346NIGMS NIH HHS U54 GM064346
6 · The paper itself

Abstract

Protein kinases catalyze protein phosphorylation and thereby control the flow of information through signaling cascades. Currently available methods for concomitant assessment of the enzymatic activities of multiple kinases in complex biological samples rely on indirect proxies for enzymatic activity, such as posttranslational modifications to protein kinases. Our laboratories have recently described a method for directly quantifying the enzymatic activity of kinases in unfractionated cell lysates using substrates containing a phosphorylation-sensitive unnatural amino acid termed CSox, which can be monitored using fluorescence. Here, we demonstrate the utility of this method using a probe set encompassing p38α, MK2, ERK1/2, Akt, and PKA. This panel of chemosensors provides activity measurements of individual kinases in a model of skeletal muscle differentiation and can be readily used to generate individualized kinase activity profiles for tissue samples from clinical cancer patients.

Indexed as

AnimalsCell DifferentiationCell LineHeLa CellsHep G2 CellsHT29 CellsHumansHydroxyquinolinesKineticsMiceMuscle, SkeletalNeoplasmsPhosphorylationProtein KinasesSignal TransductionSubstrate SpecificityHydroxyquinolinesProtein KinasesSulfonamides

Identifiers

PMID22365604
PMCPMC3307342
OpenAlexW1993315330

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.