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

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
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
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

3.5K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
3.5K
Translation01:31

Translation

17.4K
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
Proteins are...
17.4K
Translation01:31

Translation

154.7K
Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of...
154.7K
Alternative RNA Splicing02:18

Alternative RNA Splicing

24.5K
Alternative RNA splicing is the regulated splicing of exons and introns to produce different mature mRNAs from a single pre-mRNA. Unlike in constitutive splicing where a single gene produces a single type of mRNA, alternative splicing allows an organism to produce multiple proteins from a single gene and plays an important role in protein diversity.
There are five types of alternative RNA splicing that vary in the ways the pre-mRNA segments are removed or retained in the mature mRNA. The first...
24.5K

You might also read

Related Articles

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

Sort by
Same author

MLMarker: a machine learning framework for tissue inference and biomarker discovery.

Genome biology·2026
Same author

Multi-omics analysis of extracellular vesicle cargo in cancer.

Trends in cancer·2026
Same author

DiaReport: Reproducible workflow for differential expression analysis and interactive reporting in DIA-based proteomics.

Bioinformatics (Oxford, England)·2026
Same author

A living biobank of sarcoma patient-derived cell cultures reveals multi-omic and functional insights that capture disease heterogeneity.

Clinical and translational medicine·2026
Same author

A Combined Omics Approach to Elucidate the Molecular Interplay behind a Beneficial <i>Arabidopsis-Caulobacter</i> Interaction.

Journal of proteome research·2026
Same author

Author Correction: Community benchmarking and evaluation of human unannotated microprotein detection by mass spectrometry based proteomics.

Nature communications·2026
Same journal

Intrinsically disordered regions in eukaryotic mRNA decay pathways.

Trends in biochemical sciences·2026
Same journal

A unified mechanism of phosphate export across eukaryotes through EXS domain-containing proteins.

Trends in biochemical sciences·2026
Same journal

Drugging the proteome via large-scale chemoproteomics.

Trends in biochemical sciences·2026
Same journal

Peptideins: Navigating the gray zone of the proteome.

Trends in biochemical sciences·2026
Same journal

A metabolon channels nicotine biosynthesis.

Trends in biochemical sciences·2026
Same journal

Better call chaperone.

Trends in biochemical sciences·2026
See all related articles

Related Experiment Video

Updated: Dec 29, 2025

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
09:18

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Published on: September 7, 2021

3.2K

N-Terminal Proteoforms in Human Disease.

Annelies Bogaert1, Esperanza Fernandez1, Kris Gevaert1

  • 1VIB Center for Medical Biotechnology, VIB, B-9000 Ghent, Belgium; Department of Biomolecular Medicine, Ghent University, B-9000 Ghent, Belgium.

Trends in Biochemical Sciences
|February 1, 2020
PubMed
Summary
This summary is machine-generated.

Researchers review N-terminal proteoforms, which are protein variants differing at their N termini. These variants, arising from splicing and modifications, are linked to human diseases and may offer diagnostic and therapeutic potential.

Keywords:
N-terminal modificationsN-terminal proteoformsalternative splicingalternative translation initiationprotein N termini

More Related Videos

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

2.8K
Human Colonoid Monolayers to Study Interactions Between Pathogens, Commensals, and Host Intestinal Epithelium
07:20

Human Colonoid Monolayers to Study Interactions Between Pathogens, Commensals, and Host Intestinal Epithelium

Published on: April 9, 2019

9.6K

Related Experiment Videos

Last Updated: Dec 29, 2025

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
09:18

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Published on: September 7, 2021

3.2K
Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

2.8K
Human Colonoid Monolayers to Study Interactions Between Pathogens, Commensals, and Host Intestinal Epithelium
07:20

Human Colonoid Monolayers to Study Interactions Between Pathogens, Commensals, and Host Intestinal Epithelium

Published on: April 9, 2019

9.6K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genomics

Background:

  • The human genome encodes fewer genes than the number of distinct protein variants (proteoforms).
  • Alternative splicing and post-translational modifications are key drivers of proteoform diversity.
  • N-terminal variations in proteoforms are increasingly recognized for their disease relevance.

Purpose of the Study:

  • To review the mechanisms generating N-terminal proteoforms.
  • To highlight the link between N-terminal proteoforms and human diseases.
  • To explore the therapeutic and diagnostic potential of N-terminal proteoforms.

Main Methods:

  • Literature review focusing on N-terminal proteoform generation.
  • Analysis of splicing, translation initiation, and protein modification pathways.
  • Examination of disease associations and clinical implications.

Main Results:

  • Splicing, translation initiation, and protein modifications are primary mechanisms producing N-terminal proteoforms.
  • Specific N-terminal proteoforms are implicated in various human pathologies.
  • These proteoforms represent potential biomarkers and therapeutic targets.

Conclusions:

  • N-terminal proteoforms are significant contributors to human proteome complexity.
  • Understanding their generation is crucial for elucidating disease mechanisms.
  • N-terminal proteoforms hold promise for future medical diagnostics and treatments.