Evidence map›Paper›PMID 17881302›Full record

ReviewBiochimica et biophysica acta2008

Peptide-based fluorescent sensors of protein kinase activity: design and applications.

Vyas Sharma, Qunzhao Wang, David S Lawrence

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  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. Review
  4. Review
  5. Kinase Signaling in Dendritic Development and Disease.Frontiers in cellular neuroscience · 2021
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. A fluorescent reporter of the phosphorylation status of the substrate protein STAT3.Angewandte Chemie (International ed. in English) · 2011
    Article
  13. Measuring enzyme activity in single cells.Trends in biotechnology · 2011
    Review
  14. Article
  15. Visualizing tyrosine kinase activity with bipartite tetracysteine display.Chembiochem : a European journal of chemical biology · 2010
    Article
  16. Development of pH-responsive fluorescent false neurotransmitters.Journal of the American Chemical Society · 2010
    Article
  17. Review
  18. The chemical biology of protein phosphorylation.Annual review of biochemistry · 2009
    Review
  19. Uber-responsive peptide-based sensors of signaling proteins.Angewandte Chemie (International ed. in English) · 2009
    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

3 authors.

Vyas SharmaDepartment of Biochemistry, The Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Qunzhao Wang
David S Lawrence

Funding

SYNTHETIC REGULATORS OF TYROSINE PROTEIN KINASESR01CA079954 · NCI · YESHIVA UNIVERSITY · PI LAWRENCE, DAVID S. · 1999 to 2016
$4.2M
Spatiotemporal Dynamics of Protein Kinase C ActivityR01CA095019 · NCI · YESHIVA UNIVERSITY · PI LAWRENCE, DAVID S. · 2002 to 2006
$1.8M
Chemical Tools for Assessing Intracellular PKA ActivityR01GM067198 · NIGMS · YESHIVA UNIVERSITY · PI LAWRENCE, DAVID S. · 2003 to 2006
$1.5M
Intracellular Probes for Studying PKG ActivityR01NS048406 · NINDS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LAWRENCE, DAVID S. · 2005 to 2008
$1.3M
PROBES OF PROTEIN KINASE SPECIFICITYR01GM045989 · NIGMS · YESHIVA UNIVERSITY · PI LAWRENCE, DAVID S. · 1991 to 2001
$700k
NCI NIH HHS R01 CA079954NCI NIH HHS R01 CA095019NIGMS NIH HHS R01 GM045989NIGMS NIH HHS R01 GM067198NINDS NIH HHS R01 NS048406
6 · The paper itself

Abstract

Protein kinases control the flow of information through cell-signaling pathways. A detailed analysis of their behavior enhances our ability to understand normal cellular states and to devise therapeutic interventions for diseases. The design and application of "Environmentally-Sensitive", "Deep-Quench" and "Self-Reporting" sensor systems for studying protein kinase activity are described. These sensors allow real-time activity measurements in a continuous manner for a wide variety of kinases. As these sensors can be adapted from an in vitro screen to imaging kinase activity in living cells, they support both preliminary and later stages of drug discovery.

Indexed as

Microscopy, FluorescenceMolecular Probe TechniquesAnimalsFluorescent DyesHumansPeptidesPhosphorylationProtein KinasesFluorescent DyesPeptidesProtein Kinases

Identifiers

PMID17881302
PMCPMC2684651

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.