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 Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

You might also read

Related Articles

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

Sort by
Same author

Extended Half-Life Factor Concentrates in Haemophilia Treatment.

Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie·2026
Same author

Thrombin generation to predict breakthrough bleeding in patients with acquired hemophilia A under emicizumab prophylaxis.

Haematologica·2025
Same author

Rare Congenital Bleeding Disorders - Challenges Remain.

Hamostaseologie·2025
Same author

Overview on Rare Congenital Bleeding Disorders and Epidemiological Data from the German Haemophilia Registry (DHR) and a Survey in Germany, Austria, and Switzerland.

Hamostaseologie·2025
Same author

Sustained survival benefit of emicizumab and postponed immunosuppression in acquired hemophilia A.

Blood advances·2025
Same author

Detection of Apple Proliferation Disease Using Hyperspectral Imaging and Machine Learning Techniques.

Sensors (Basel, Switzerland)·2024
Same journal

Slow Evolution Towards Generalism in a Model of Variable Dietary Range.

Bulletin of mathematical biology·2026
Same journal

CBINN: Cancer Biology-Informed Neural Network for Unknown Parameter Estimation and Missing Physics Identification.

Bulletin of mathematical biology·2026
Same journal

A Cost-Sensitive Behavioral Modeling Analysis of the Early Identification and Control of Infectious Diseases.

Bulletin of mathematical biology·2026
Same journal

Tracking Dynamics of Superspreading Through Contacts, Exposures, and Transmissions in Edge-Based Network Epidemics.

Bulletin of mathematical biology·2026
Same journal

The Exact Hypergeometric Posterior Method for Accurate Inference of Population Size from Mark-Recapture Data.

Bulletin of mathematical biology·2026
Same journal

Modeling, Analysis, and Optimal Control of Leukemic Cell Population Dynamics Under Therapy.

Bulletin of mathematical biology·2026
See all related articles

Related Experiment Video

Updated: May 7, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Multistationarity in sequential distributed multisite phosphorylation networks.

Katharina Holstein1, Dietrich Flockerzi, Carsten Conradi

  • 1Max-Planck-Institut Dynamik komplexer technischer Systeme, Sandtorstr. 1, 39106, Magdeburg, Germany, holstein@mpi-magdeburg.mpg.de.

Bulletin of Mathematical Biology
|September 20, 2013
PubMed
Summary
This summary is machine-generated.

This study identifies a necessary and sufficient sign condition for multistationarity in sequential protein phosphorylation networks. This finding enables explicit calculation of rate constants, allowing systematic exploration of parameter space for these crucial biological processes.

More Related Videos

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Related Experiment Videos

Last Updated: May 7, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Area of Science:

  • Biochemistry
  • Systems Biology
  • Molecular Biology

Background:

  • Multisite phosphorylation is critical for intracellular processes like signal transduction and cell-cycle control.
  • The phenomenon of multistationarity, characterized by multiple positive steady states in dynamical systems, is known to occur in these networks.
  • However, the specific rate constants governing multistationarity have remained largely uncharacterized.

Purpose of the Study:

  • To establish a necessary and sufficient sign condition for multistationarity in n-site sequential, distributive phosphorylation networks.
  • To provide a method for explicitly determining rate constants that permit multistationarity.
  • To enable a systematic exploration of the parameter space associated with multistationarity.

Main Methods:

  • Analysis of polynomial dynamical systems representing sequential, distributive phosphorylation.
  • Derivation of a sign condition for multistationarity.
  • Expression of the sign condition using linear systems.
  • Construction of feasible linear systems for n≥2 to prove the existence of multistationary conditions.

Main Results:

  • A precise sign condition for multistationarity in n-site sequential, distributive phosphorylation has been established.
  • This condition, expressed via linear systems, allows for the identification of rate constants enabling multistationarity.
  • For n≥2, feasible linear systems were constructed, providing an independent proof of multistationarity's possibility.
  • A direct consequence is that the ratio of kinase-substrate to phosphatase-substrate complexes is constant across steady states.

Conclusions:

  • The developed sign condition provides a fundamental understanding of multistationarity in complex phosphorylation networks.
  • This work facilitates the explicit calculation of rate constants, paving the way for systematic analysis of biological parameter spaces.
  • The findings offer new insights into the quantitative behavior of intracellular signaling pathways.