Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Families02:47

Protein Families

16.4K
Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
16.4K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

13.7K
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...
13.7K
Protein Networks02:26

Protein Networks

4.4K
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,...
4.4K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Defect-Suppressed Molecular Passivation Film Endure the Trade-Off: Scalable Co-Passivation for Copper That Withstands Harsh Alkaline Attack.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same author

Knowledge, attitude, and practice toward medical nutritional therapy among patients with chronic kidney disease.

Frontiers in nutrition·2026
Same author

<sup>18</sup>F-FDG PET biomarker of individual cerebral metabolic connectivity in focal epilepsy subtypes and association with prognosis.

Frontiers in medicine·2026
Same author

Ï€-SeqOmics: A Sequential Workflow for Genomic, Transcriptomic, Proteomic, and Phosphoproteomic Profiling From Biopsy-Scale Samples.

Molecular & cellular proteomics : MCP·2026
Same author

Integration of habitat radiomics and 2.5D deep features from <sup>18</sup>F-FDG PET/CT for noninvasive prediction of PD-L1 TPS ≥ 50% in non-small cell lung cancer.

European journal of radiology·2026
Same author

AI-enhanced virtual laboratories improve learning outcomes and student engagement in food microbiology education.

Scientific reports·2026

Related Experiment Video

Updated: Dec 1, 2025

Mass Spectrometry-Based Proteomics Analyses Using the OpenProt Database to Unveil Novel Proteins Translated from Non-Canonical Open Reading Frames
07:38

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

Published on: April 11, 2019

13.1K

Open-pFind Verified Four Missing Proteins from Multi-Tissues.

Shujia Wu1,2, Jinshuai Sun2,3, Xi Wang4

  • 1School of Basic Medical Science, Key Laboratory of Combinational Biosynthesis and Drug Discovery of Ministry of Education, School of Basic Medical Sciences, Wuhan University, Wuhan 430072, China.

Journal of Proteome Research
|November 11, 2020
PubMed
Summary

The Chromosome-Centric Human Proteome Project identified four new missing proteins (MPs) using advanced mass spectrometry on human tissues. This research advances our understanding of the complete human proteome by confirming protein expression for previously unannotated proteins.

Keywords:
Chromosome-Centric Human Proteome Projectmissing proteinsmultiple tissuesopen-pFind

More Related Videos

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

278
An Optimized Quantitative Pull-Down Analysis of RNA-Binding Proteins Using Short Biotinylated RNA
07:55

An Optimized Quantitative Pull-Down Analysis of RNA-Binding Proteins Using Short Biotinylated RNA

Published on: February 17, 2023

4.7K

Related Experiment Videos

Last Updated: Dec 1, 2025

Mass Spectrometry-Based Proteomics Analyses Using the OpenProt Database to Unveil Novel Proteins Translated from Non-Canonical Open Reading Frames
07:38

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

Published on: April 11, 2019

13.1K
Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

278
An Optimized Quantitative Pull-Down Analysis of RNA-Binding Proteins Using Short Biotinylated RNA
07:55

An Optimized Quantitative Pull-Down Analysis of RNA-Binding Proteins Using Short Biotinylated RNA

Published on: February 17, 2023

4.7K

Area of Science:

  • Proteomics
  • Human Proteome Project
  • Mass Spectrometry

Background:

  • The Chromosome-Centric Human Proteome Project (C-HPP) aimed to identify all human proteins.
  • Significant progress reduced the number of missing proteins (MPs) from 5511 to 1899.
  • Remaining MPs are challenging due to low abundance, specificity, and complex characteristics.

Purpose of the Study:

  • To identify and validate previously uncharacterized missing proteins (MPs) at the protein level.
  • To leverage advanced mass spectrometry and multi-tissue proteomics to detect low-abundance proteins.
  • To contribute to the completion of the human proteome annotation.

Main Methods:

  • Utilized open-pFind software for analyzing mass spectrometry data from 20 healthy human tissue pairs.
  • Integrated a large-scale testis dataset digested with three enzymes (Glu-C, Lys-C, trypsin).
  • Performed rigorous screening, manual checks, peptide synthesis, and database matching for validation.

Main Results:

  • Mapped over 1.5 million peptides to 14,279 protein entries with a <1% false discovery rate.
  • Identified 103 MP candidates, with 86 showing improved unique peptide counts compared to single-tissue data.
  • Validated four specific missing proteins (P0C7T8, Q8WWZ4, Q8IV35, O14921) in distinct human tissues.

Conclusions:

  • Successfully validated four missing proteins, providing crucial protein-level evidence for their existence.
  • Demonstrated the effectiveness of high-resolution mass spectrometry and multi-enzyme digestion for MP discovery.
  • This work significantly contributes to the ongoing effort to achieve a complete human proteome map.