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Related Concept Videos

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.
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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 the...
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Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
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Introduction to Enzyme Kinetics01:19

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Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
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Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
10:54

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Shared kinase fluctuations between two enzymatic reactions.

G Viswanathan1, C Jayaprakash, S C Sealfon

  • 1Department of Neurology and Center for Translational Systems Biology, Mount Sinai School of Medicine, Box 1137, New York, NY 10029, USA.

Physical Biology
|November 11, 2008
PubMed
Summary
This summary is machine-generated.

Cellular signaling noise from shared kinases distributes unevenly between pathways. The steady-state response dictates the extent of these fluctuations, impacting cellular function.

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Identification of Kinase-substrate Pairs Using High Throughput Screening
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Related Experiment Videos

Last Updated: Jun 28, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
10:54

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Area of Science:

  • Biochemistry
  • Cell Biology
  • Systems Biology

Background:

  • Kinases are essential enzymes in cellular signaling pathways, regulating information transfer.
  • Phosphorylation of multiple targets by a single kinase creates branching points in signaling networks.
  • Cellular responses exhibit significant cell-to-cell variation, influenced by kinase activity and noise.

Purpose of the Study:

  • To investigate how noise, arising from kinase fluctuations and intrinsic cellular processes, is distributed between two distinct signaling pathways.
  • To develop a theoretical framework for analyzing noise distribution in branched signaling systems.
  • To explore the impact of biological parameters on fluctuation dynamics and system responses.

Main Methods:

  • Development of a mathematical formalism to model noise propagation in branched signaling pathways.
  • Analysis of fluctuations around a steady state in a system with a shared kinase and two substrates.
  • Simulation using realistic biological constants to examine system behavior.

Main Results:

  • The steady-state response of the system is a key determinant of the magnitude and range of phosphorylated substrate fluctuations.
  • Noise distribution between the two pathways is sensitive to the chosen operating point (enzyme concentration).
  • Fluctuations and relaxation times to steady state exhibit distinct characteristics influenced by system parameters.

Conclusions:

  • Shared kinase noise distribution is not uniform and can be modulated by system parameters.
  • Understanding noise propagation is critical for comprehending cell-to-cell variability in signaling responses.
  • The operating point of a signaling network can be tuned to control how noise impacts downstream pathways.