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

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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 form...
Leaky Scanning02:28

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...

You might also read

Related Articles

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

Sort by
Same author

Comprehensive Engineering of Ionizable Lipid Nanoparticles and mRNA Elements for Next-Generation Vaccines.

ACS nano·2026
Same author

Conserved stromal EMT program controls regenerative capacity of mesenchymal stromal cells across multiple tissues.

Science advances·2026
Same author

MARCH2-mediated Lys63-linked polyubiquitination promotes metastasis by modulating the catalytic activity of TGF-β type I receptor.

Cell death & disease·2025
Same author

Meso-macroporous hydrogel for direct litre-scale isolation of extracellular vesicles.

Nature nanotechnology·2025
Same author

ATE1 promotes breast cancer progression via arginylation-dependent regulation of MAPK-MYC signaling.

Cell communication and signaling : CCS·2025
Same author

Tracing the mark of arginine.

Nature chemical biology·2025
Same journal

Demonstration of a quantum C-NOT gate in a time-multiplexed fully reconfigurable photonic processor.

Nature communications·2026
Same journal

Nonlinear quantum light source with van der Waals ferroelectric NbOX<sub>2</sub> (X = Br, I).

Nature communications·2026
Same journal

Antagonistic histone H2A variants and autonomous heterochromatin formation shape epigenomic patterns in Arabidopsis.

Nature communications·2026
Same journal

The long tail of nitrate pollution in groundwater challenges governance of global water quality.

Nature communications·2026
Same journal

Select microbial metabolites promote tau aggregation in a murine tauopathy model.

Nature communications·2026
Same journal

Warming climate has lengthened global intense tropical cyclone seasons.

Nature communications·2026
See all related articles

Related Experiment Video

Updated: Jun 10, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

9.9K

Implementing N-terminomics and machine learning to probe Nt-arginylation.

Shinyeong Ju1, Laxman Nawale2,3, Seonjeong Lee1

  • 1Chemical and Biological Integrative Research Center, Korea Institute of Science and Technology, Seoul, Republic of Korea.

Nature Communications
|December 9, 2025
PubMed
Summary
This summary is machine-generated.

Researchers developed a new method to detect N-terminal arginylation (Nt-arginylation), a key protein modification involved in cellular processes. This technique identifies new sites, aiding in the discovery of potential biomarkers and drug targets.

More Related Videos

A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis
09:40

A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis

Published on: April 28, 2022

2.9K
A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues
09:16

A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues

Published on: May 4, 2022

2.6K

Related Experiment Videos

Last Updated: Jun 10, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

9.9K
A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis
09:40

A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis

Published on: April 28, 2022

2.9K
A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues
09:16

A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues

Published on: May 4, 2022

2.6K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • N-terminal arginylation (Nt-arginylation) is a crucial post-translational modification (PTM) impacting protein quality control, organelle homeostasis, and stress signaling.
  • Previous studies of Nt-arginylation were hindered by significant technical challenges.

Purpose of the Study:

  • To develop an integrated approach for identifying N-terminal arginylation sites in cells.
  • To overcome technical limitations in studying this important PTM.

Main Methods:

  • Combined N-terminomics with machine learning-based filtering to detect Nt-arginylation in cellulo.
  • Utilized Arg-starting missed cleavage peptides as proxies for ATE1-mediated arginylation.
  • Trained a transfer learning model to predict mass spectra and retention times, followed by statistical filtering.

Main Results:

  • Identified 134 novel Nt-arginylation sites in thapsigargin-treated HeLa cells.
  • Found arginylation enrichment in proteins involved in various organelles, particularly at caspase cleavage and signal peptide processing sites.
  • Validated interactions of eight tested proteins with the p62 ZZ domain and observed temporal changes in arginylation post-stress.

Conclusions:

  • The developed approach enables sensitive detection of rare N-terminal modifications.
  • This method holds potential for discovering novel biomarkers and drug targets related to Nt-arginylation.
  • Provides new insights into the roles of Nt-arginylation in cellular stress responses.