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Related Concept Videos

Proteomics01:33

Proteomics

9.9K
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...
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Role of Proteins in the Human Body01:28

Role of Proteins in the Human Body

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Proteins are the building block of life. They are also  the most abundant macromolecules with as many diverse roles in the body. They are part of many structural components that provide unique shapes and structures to animal cells, tissues, and organs. In addition, they also act as biological catalysts and carry out several anabolic and catabolic reactions. Notably, some proteins are chemical messengers and regulate many critical processes, such as metabolism, growth, and development. They...
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Tissues01:18

Tissues

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Cells with similar structure and function are grouped into tissues. A group of tissues with a specialized function is called an organ. There are four main types of tissue in vertebrates: epithelial, connective, muscle, and nervous.
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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
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Related Experiment Video

Updated: Feb 12, 2026

Quantitative Proteomics Workflow using Multiple Reaction Monitoring Based Detection of Proteins from Human Brain Tissue
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Quantitative Proteomics Workflow using Multiple Reaction Monitoring Based Detection of Proteins from Human Brain Tissue

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Mining the Human Tissue Proteome for Protein Citrullination.

Chien-Yun Lee1,2,3, Dongxue Wang1, Mathias Wilhelm1

  • 1From the ‡Chair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.

Molecular & Cellular Proteomics : MCP
|April 4, 2018
PubMed
Summary

This study identified 375 new citrullination sites on 209 human proteins using mass spectrometry. The findings advance understanding of protein citrullination, a modification linked to diseases like rheumatoid arthritis and cancer.

Keywords:
Data evaluationOmicsPost-translational modifications*Tandem Mass SpectrometryTissues*citrullinationhuman proteomepeptidylarginine deiminasesynthetic peptides

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Two-dimensional Gel Electrophoresis Coupled with Mass Spectrometry Methods for an Analysis of Human Pituitary Adenoma Tissue Proteome
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Area of Science:

  • Biochemistry
  • Proteomics
  • Post-translational Modifications

Background:

  • Citrullination, catalyzed by peptidylarginine deiminases (PADs), alters protein function but its roles are unclear due to methodological limitations.
  • Few citrullination sites have been confidently identified on human proteins.
  • Understanding citrullination is crucial for diseases like rheumatoid arthritis and cancer.

Purpose of the Study:

  • To identify citrullination sites on endogenous human proteins using deep proteomic profiling.
  • To establish a robust methodology for detecting and validating protein citrullination.
  • To expand the known landscape of protein citrullination in human tissues.

Main Methods:

  • Mass-spectrometry-based deep proteomic profiling of 30 human tissues.
  • Database searching of millions of tandem mass spectra.
  • Spectrum quality metrics and neutral loss detection for citrullinated peptides.
  • Creation of a reference spectral library using synthesized citrullinated and deamidated peptides.

Main Results:

  • Validated 375 citrullination sites on 209 human proteins, with >80% being novel.
  • Detected citrullination for the first time in 56% of the identified proteins.
  • Identified sequence motifs favoring Asp and Gly residues around citrullination sites.
  • Found highest citrullination levels in brain and lung tissues.
  • Observed no strong correlation between citrullination levels and PAD enzyme expression.

Conclusions:

  • This study represents the largest survey of protein citrullination to date, significantly expanding the number of identified sites.
  • The findings highlight the prevalence of citrullination across various human tissues.
  • Further development of enrichment methods is needed to study low-abundance proteins and the full scope of citrullination.