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Related Concept Videos

Proteomics01:33

Proteomics

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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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Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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Ribosome Profiling02:24

Ribosome Profiling

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Ribosome profiling or ribo-sequencing is a deep sequencing technique that produces a snapshot of active translation in a cell. It selectively sequences the mRNAs protected by ribosomes to get an insight into a cell’s translation landscape at any given point in time.
Applications of ribosome profiling
Ribosome profiling has many applications, including in vivo monitoring of translation inside a particular organ or tissue type and quantifying new protein synthesis levels.
The technique...
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Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

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Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
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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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Related Experiment Video

Updated: Jan 8, 2026

Mass Spectrometry-Based Proteomics Analyses Using the OpenProt Database to Unveil Novel Proteins Translated from Non-Canonical Open Reading Frames
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Mass Spectrometry-Based Proteomics Analyses Using the OpenProt Database to Unveil Novel Proteins Translated from Non-Canonical Open Reading Frames

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Decoding the Cryptic Proteome Between Antigens and Novel Functional Proteins.

Emma G Bawden1, Sebastian Amigorena1, Yago A Arribas1

  • 1Inserm U932 Immunity and Cancer, Institut Curie, PSL University, Paris, 75005, France.

European Journal of Immunology
|December 19, 2025
PubMed
Summary
This summary is machine-generated.

The human proteome complexity increases with cryptic proteins from the non-coding genome. These proteins offer a source of antigens for immune surveillance and expand functional protein diversity for evolution.

Keywords:
DRiPsantigen presentationcryptic proteomeimmunopeptidomicsribosome profiling

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Area of Science:

  • Genomics
  • Proteomics
  • Immunology

Background:

  • The human genome contains a vast non-coding region, previously considered non-functional.
  • Recent discoveries show translation of cryptic proteins from non-coding DNA, expanding proteome complexity.
  • These proteins are often expressed at low levels, rapidly degraded, and presented on MHC-I.

Purpose of the Study:

  • To propose a model explaining the role of cryptic proteins in human proteome evolution and immune surveillance.
  • To investigate how cryptic proteins contribute to functional protein diversity.
  • To understand the source of antigens for immunosurveillance.

Main Methods:

  • Theoretical modeling of cryptic protein translation and its evolutionary implications.
  • Analysis of protein expression, degradation, and MHC-I presentation pathways.
  • Review of existing literature on non-coding genome translation and immunology.

Main Results:

  • Cryptic proteins increase the diversity of functional proteins available for evolutionary selection.
  • A subset of cryptic proteins can be stable and functional, integrating into the proteome.
  • Cryptic proteins serve as a source of antigens for the immune system's surveillance.

Conclusions:

  • The translation of cryptic proteins is a significant factor in proteome expansion and evolution.
  • Cryptic proteins play a dual role: expanding functional diversity and providing antigens for immunosurveillance.
  • This process highlights the dynamic interplay between the non-coding genome, protein evolution, and immune response.