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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: Jun 16, 2026

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
08:12

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Systems-wide proteomic characterization of combinatorial post-translational modification patterns.

Nicolas L Young1, Mariana D Plazas-Mayorca, Benjamin A Garcia

  • 1Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.

Expert Review of Proteomics
|February 4, 2010
PubMed
Summary

Combinatorial protein post-translational modifications (PTMs) are increasingly identified, revealing complex biological patterns. Mass spectrometry advances enable the study of these intricate PTM networks and their cellular functions.

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Related Experiment Videos

Last Updated: Jun 16, 2026

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
08:12

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 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

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations
10:26

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Published on: November 7, 2019

Area of Science:

  • Molecular Biology
  • Proteomics
  • Biochemistry

Background:

  • Protein post-translational modifications (PTMs) regulate crucial cellular processes, including signaling, localization, and protein interactions.
  • Mass spectrometry (MS) is a primary technology for identifying and quantifying PTMs at the proteome-wide scale.
  • Emerging large-scale proteomic datasets facilitate the discovery of complex, combinatorial PTM patterns.

Purpose of the Study:

  • To review and highlight examples of combinatorial PTMs in biological systems.
  • To discuss mass spectrometry-based techniques employed in the investigation of these complex PTM patterns.
  • To underscore the emerging understanding of the biological significance of combinatorial PTMs.

Main Methods:

  • Literature review of recent studies on combinatorial PTMs.
  • Analysis of mass spectrometry-based approaches for PTM identification and quantification.
  • Examination of data from proteome-wide studies.

Main Results:

  • Many proteins are subject to multiple PTMs, often occurring in sequential or hierarchical patterns.
  • Combinatorial PTMs play significant roles in modulating protein function and cellular outcomes.
  • Advancements in mass spectrometry are critical for elucidating these complex modification landscapes.

Conclusions:

  • The study of combinatorial PTMs is a rapidly advancing field with profound biological implications.
  • Mass spectrometry techniques are essential for unraveling the complexity of PTM patterns.
  • Further research is needed to fully understand the biology governed by these intricate protein modifications.