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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.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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...
Overview of Skeletal Muscle01:15

Overview of Skeletal Muscle

Skeletal muscles are composed of a bundle of muscle fibers and are attached to bones through tendons. Each skeletal muscle fiber is a single muscle cell. The sarcolemma, the plasma membrane of a skeletal muscle cell, consists of a lipid bilayer and glycocalyx that supports muscle fibers. The sarcolemma extends into the muscle cells to form tubular structures called transverse or T-tubules. Each side of the T-tubules consists of a membrane-bound structure called the sarcoplasmic reticulum,...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...

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Related Experiment Video

Updated: Jun 5, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

The Musite open-source framework for phosphorylation-site prediction.

Jianjiong Gao1, Dong Xu

  • 1Department of Computer Science, C.S. Bond Life Sciences Center, University of Missouri, Columbia, Missouri 65211, USA.

BMC Bioinformatics
|January 8, 2011
PubMed
Summary
This summary is machine-generated.

Musite is a new open-source framework for phosphorylation-site prediction. This machine learning tool offers an extensible platform for integrating biological evidence, aiding researchers in phosphoproteomics data analysis.

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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
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Last Updated: Jun 5, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

Area of Science:

  • Biochemistry
  • Bioinformatics
  • Computational Biology

Background:

  • Phosphorylation-site prediction is crucial due to increasing phosphoproteomics data.
  • Numerous prediction tools exist, but a dedicated open-source framework was lacking.
  • Musite addresses this gap as a specialized open-source solution.

Purpose of the Study:

  • To introduce Musite, an open-source framework for machine learning-based phosphorylation-site prediction.
  • To provide a flexible and extensible platform for developing predictive applications.

Main Methods:

  • Implementation of Musite using six loosely coupled modules.
  • Development of a Java application programming interface (API) for extensibility.
  • Facilitation of integration with diverse biological evidence sources.

Main Results:

  • Musite provides a modular and extensible framework.
  • The Java API allows for easy integration of various biological data.
  • Enables the development of advanced phosphorylation-site prediction applications.

Conclusions:

  • Musite is an open-source, extensible framework for phosphorylation-site prediction.
  • It is released under the GNU GPL license.
  • Source code and software are available for community use and development.