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

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

8.0K
Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
8.0K
The Proteasome Structure01:17

The Proteasome Structure

1.5K
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
1.5K
The Proteasome02:18

The Proteasome

9.9K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
9.9K
The Proteasome01:13

The Proteasome

1.5K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.5K
Peptide Bonds02:43

Peptide Bonds

81.5K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
81.5K
Proteomics01:33

Proteomics

9.1K
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...
9.1K

You might also read

Related Articles

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

Sort by
Same author

[Age-related dynamics of SLC6A4 serotonin transporter gene expression and serotonin synthesis in ovaries.]

Advances in gerontology = Uspekhi gerontologii·2025
Same author

[KE peptide regulates SIRT1, PARP1, PARP2 gene expression and protein synthesis in human mesenchymal stem cells aging.]

Advances in gerontology = Uspekhi gerontologii·2023
Same author

[Chondrocytes secretory phenotype associated with aging: role in the pathogenesis of osteoarthritis and prospects for peptide bioregulation.]

Advances in gerontology = Uspekhi gerontologii·2023
Same author

[The influence of peptides on the chondrogenic differentiation of human mesenchymal stem cells during replicative aging.]

Advances in gerontology = Uspekhi gerontologii·2023
Same author

[Predictive role of erythrocytes in assessment of COVID-19 outcomes].

Voprosy virusologii·2023
Same author

[Peptides prevent the forming of secretory phenotype of chondrocytes associated with the aging.]

Advances in gerontology = Uspekhi gerontologii·2023

Related Experiment Video

Updated: Dec 25, 2025

Sample Preparation for Endopeptidomic Analysis in Human Cerebrospinal Fluid
10:23

Sample Preparation for Endopeptidomic Analysis in Human Cerebrospinal Fluid

Published on: December 4, 2017

9.3K

Peptide KE in Human Proteome.

A Yu Terekhov1, D Yu Kormilets2, N S Linkova3,4

  • 1Department of Normal Physiology, Moscow, Russia.

Bulletin of Experimental Biology and Medicine
|April 5, 2020
PubMed
Summary

The bioregulatory peptide KE, known for its protective and anti-cancer effects, is most abundant in nuclear and cytoplasmic proteins. This suggests a role in regulating gene expression through DNA binding.

Keywords:
gene expressionhuman proteomenuclear proteinspeptide KE

More Related Videos

Sampling Human Indigenous Saliva Peptidome Using a Lollipop-Like Ultrafiltration Probe: Simplify and Enhance Peptide Detection for Clinical Mass Spectrometry
08:37

Sampling Human Indigenous Saliva Peptidome Using a Lollipop-Like Ultrafiltration Probe: Simplify and Enhance Peptide Detection for Clinical Mass Spectrometry

Published on: August 7, 2012

11.8K
Two-dimensional Gel Electrophoresis Coupled with Mass Spectrometry Methods for an Analysis of Human Pituitary Adenoma Tissue Proteome
12:34

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

Published on: April 2, 2018

13.9K

Related Experiment Videos

Last Updated: Dec 25, 2025

Sample Preparation for Endopeptidomic Analysis in Human Cerebrospinal Fluid
10:23

Sample Preparation for Endopeptidomic Analysis in Human Cerebrospinal Fluid

Published on: December 4, 2017

9.3K
Sampling Human Indigenous Saliva Peptidome Using a Lollipop-Like Ultrafiltration Probe: Simplify and Enhance Peptide Detection for Clinical Mass Spectrometry
08:37

Sampling Human Indigenous Saliva Peptidome Using a Lollipop-Like Ultrafiltration Probe: Simplify and Enhance Peptide Detection for Clinical Mass Spectrometry

Published on: August 7, 2012

11.8K
Two-dimensional Gel Electrophoresis Coupled with Mass Spectrometry Methods for an Analysis of Human Pituitary Adenoma Tissue Proteome
12:34

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

Published on: April 2, 2018

13.9K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Peptide KE demonstrates immunoprotective, geroprotective, and oncostatic activities.
  • The KE motif is found in cytokines and peptide hormones, but its prevalence across the human proteome is understudied.

Purpose of the Study:

  • To investigate the incidence of the bioregulatory peptide KE motif in various functional groups of the human proteome.
  • To understand the relationship between KE motif presence and protein function.

Main Methods:

  • Analysis of the human proteome data from the UniProt portal, including 20,417 proteins.
  • Quantification of KE motif levels across different protein functional groups.

Main Results:

  • KE motifs were most abundant in cytoplasmic and nuclear proteins.
  • KE motifs were least prevalent in membrane and other protein categories.
  • KE peptide molecules from nuclear proteins can bind DNA and regulate gene expression via limited proteolysis.

Conclusions:

  • The distribution of the KE motif suggests a significant role for nuclear and cytoplasmic proteins in its biological functions.
  • The findings highlight a potential mechanism for gene expression regulation involving KE peptides released from nuclear proteins.