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

Phosphorylation01:02

Phosphorylation

54.9K
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...
54.9K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

15.3K
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...
15.3K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

4.6K
4.6K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

18.0K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
18.0K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

18.7K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
18.7K
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

10.6K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
10.6K

You might also read

Related Articles

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

Sort by
Same author

Parameter identifiability of linear-compartmental mammillary models.

Bulletin of mathematical biology·2025
Same author

Dynamics of ERK regulation in the processive limit.

Journal of mathematical biology·2021
Same author

Joining and decomposing reaction networks.

Journal of mathematical biology·2020
Same author

Isolating phyllotactic patterns embedded in the secondary growth of sweet cherry (<i>Prunus avium</i> L.) using magnetic resonance imaging.

Plant methods·2019
Same author

Algebraic signatures of convex and non-convex codes.

Journal of pure and applied algebra·2019
Same author

Oscillations and bistability in a model of ERK regulation.

Journal of mathematical biology·2019
Same journal

The hydra and hormetic effects in a single discrete-time overcompensation model.

Mathematical biosciences·2026
Same journal

Seasonal impacts on brucellosis transmission mediated by live sheep supply-demand dynamics.

Mathematical biosciences·2026
Same journal

Optimal controls and cost-effectiveness analysis on the transmission dynamics of early blight disease in tomatoes.

Mathematical biosciences·2026
Same journal

Temperature-dependent dynamics and allee effect thresholds mediate fourfold cusp stability in biological control of invasive vectors.

Mathematical biosciences·2026
Same journal

Dynamics of a stochastic tumor-immune interaction system with an Ornstein-Uhlenbeck process.

Mathematical biosciences·2026
Same journal

Post-peak dynamics and epidemic overshoot in SIR-type frameworks.

Mathematical biosciences·2026
See all related articles

Related Experiment Video

Updated: Feb 28, 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

19.4K

An all-encompassing global convergence result for processive multisite phosphorylation systems.

Mitchell Eithun1, Anne Shiu2

  • 1Department of Mathematical Sciences, Ripon College, Ripon, WI 54971, USA.

Mathematical Biosciences
|June 11, 2017
PubMed
Summary
This summary is machine-generated.

This study generalizes global stability findings for processive multisite phosphorylation networks. It shows that these networks remain globally stable even with irreversible reactions and product inhibition, expanding biological understanding.

Keywords:
Chemical reaction networkGlobal stabilityIntermediate complexMonotone systems theorySR-graph

More Related Videos

Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

24.7K
Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

8.9K

Related Experiment Videos

Last Updated: Feb 28, 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

19.4K
Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

24.7K
Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

8.9K

Area of Science:

  • Biochemistry
  • Systems Biology
  • Enzymology

Background:

  • Phosphorylation is a fundamental biological process involving enzyme-mediated phosphate group addition.
  • Multisite phosphorylation can occur via distributive or processive mechanisms.
  • Previous work established global stability for reversible processive phosphorylation but not for irreversible cases.

Purpose of the Study:

  • To generalize global convergence results for processive multisite phosphorylation networks.
  • To include irreversible reactions and product inhibition within the analysis of processive systems.
  • To investigate how network modifications affect global convergence properties.

Main Methods:

  • Defined an all-encompassing processive network model.
  • Applied monotone systems theory.
  • Utilized network and graph reductions by removing intermediate complexes.

Main Results:

  • Demonstrated global convergence for processive phosphorylation networks with irreversible reactions.
  • Showed that product inhibition does not disrupt global convergence.
  • Established that global convergence is preserved under specific network modifications.

Conclusions:

  • Processive multisite phosphorylation networks exhibit global stability under broader conditions than previously known.
  • The study provides a framework for analyzing network robustness in biochemical systems.
  • Findings contribute to understanding the stability principles governing complex biological networks.