Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Protein kinase recognition sequence motifs.

B E Kemp1, R B Pearson

  • 1St Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.

Trends in Biochemical Sciences
|September 1, 1990
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Antimicrobial use practices, attitudes and responsibilities in UK farm animal veterinary surgeons.

Preventive veterinary medicine·2018
Same author

Understanding the culture of antimicrobial prescribing in agriculture: a qualitative study of UK pig veterinary surgeons.

The Journal of antimicrobial chemotherapy·2016
Same author

PR55α-containing protein phosphatase 2A complexes promote cancer cell migration and invasion through regulation of AP-1 transcriptional activity.

Oncogene·2015
Same author

Understanding antimicrobial use and prescribing behaviours by pig veterinary surgeons and farmers: a qualitative study.

The Veterinary record·2014
Same author

PR55α-containing protein phosphatase 2A complexes promote cancer cell migration and invasion through regulation of AP-1 transcriptional activity.

Oncogene·2014
Same author

Leptin stimulation of COXIV is impaired in obese skeletal muscle myotubes.

Obesity research & clinical practice·2013
Same journal

Peptideins: Navigating the gray zone of the proteome.

Trends in biochemical sciences·2026
Same journal

A metabolon channels nicotine biosynthesis.

Trends in biochemical sciences·2026
Same journal

Better call chaperone.

Trends in biochemical sciences·2026
Same journal

Biochemistry at scale: Seeing both the forest and the trees.

Trends in biochemical sciences·2026
Same journal

Voices across Asia and Oceania: Biochemistry across borders.

Trends in biochemical sciences·2026
Same journal

Metabolic control of RNA splicing by polyamines.

Trends in biochemical sciences·2026
See all related articles

Protein kinases regulate cellular processes by phosphorylating proteins. Understanding phosphorylation sites helps identify new targets and design specific inhibitors.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Signaling

Background:

  • Protein kinases are essential enzymes regulating cellular functions through phosphorylation.
  • Phosphorylation involves adding phosphate groups to serine, threonine, or tyrosine residues on target proteins.
  • Identifying kinase substrate sequences is key to understanding enzyme specificity.

Purpose of the Study:

  • To elucidate the mechanisms by which protein kinases recognize their substrate proteins.
  • To leverage knowledge of phosphorylation sites for identifying new potential phosphorylation targets.
  • To enable the design of specific model substrates and inhibitors for protein kinases.

Main Methods:

  • Analysis of identified phosphorylation site sequences.

Related Experiment Videos

  • Studies utilizing model peptides representing phosphorylation sites.
  • Bioinformatic approaches for identifying potential phosphorylation sites in novel protein sequences.

    • Main Results:

    • Characterization of consensus sequences recognized by protein kinases.
    • Development of predictive models for substrate recognition.
    • Validation of model peptides in mimicking kinase-substrate interactions.

    Conclusions:

    • Knowledge of phosphorylation site sequences provides critical insights into protein kinase substrate specificity.
    • This understanding facilitates the identification of novel phosphorylation sites in newly sequenced proteins.
    • The findings support the rational design of specific kinase inhibitors and model substrates for research.