Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Translation

Translation

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 Life

Translation

Translation

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 Life

Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...

Huntington Disease l: Introduction

Huntington Disease l: Introduction

Huntington disease or HD is a progressive, fatal neurodegenerative disorder inherited in an autosomal dominant pattern.PathophysiologyIt is caused by expansion of the CAG trinucleotide repeat in the HTT gene on chromosome 4 (4p16.3), producing an abnormal huntingtin protein with an expanded polyglutamine tract. This misfolded protein disrupts cellular function, leading to neuronal death. Normal alleles have ≤26 repeats, 27–35 are intermediate (risk of expansion), 36–39 show reduced penetrance,...

Lysosomal Hydrolases

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...

Leaky Scanning

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

Impaired motor activity in a CRISPR SCA5 L253P knock-in mouse is associated with selective β-III-spectrin subcellular redistribution in the cerebellum.

bioRxiv : the preprint server for biology·2026

Same author

Neural basis for mutant ATAXIN-1 induced respiratory dysfunction in mouse models of spinocerebellar ataxia type 1.

Neurobiology of disease·2026

Same author

Repeat-associated non-AUG translation as a common mechanism for the polyGln ataxias.

Cell reports·2025

Same author

Striatal pathology in Spinocerebellar Ataxia Type 1 mice: A comparative study with Huntington's disease.

bioRxiv : the preprint server for biology·2025

Same author

An expanded polyglutamine in ATAXIN1 results in a loss-of-function that exacerbates severity of Multiple Sclerosis in an EAE mouse model.

Research square·2025

Same author

An expanded polyglutamine in ATAXIN1 results in a loss-of-function that exacerbates severity of Multiple Sclerosis in an EAE mouse model.

Journal of neuroinflammation·2025

Search research articles

Related Experiment Video

Updated: Jun 2, 2026

Measuring RAN Peptide Toxicity in C. elegans

Measuring RAN Peptide Toxicity in C. elegans

Published on: April 30, 2020

Are polyglutamine diseases expanding?

¹Institute for Translational Neuroscience, Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis, MN 55455, USA. orrxx002@umn.edu

|May 11, 2011

Summary

This summary is machine-generated.

In Huntington's disease like-2 (HDL2), the exact cause is debated. New research shows the polyglutamine peptide, not RNA, drives HDL2 disease progression in a mouse model.

More Related Videos

Growth Assays to Assess Polyglutamine Toxicity in Yeast

Growth Assays to Assess Polyglutamine Toxicity in Yeast

Published on: March 5, 2012

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

Related Experiment Videos

Last Updated: Jun 2, 2026

Measuring RAN Peptide Toxicity in C. elegans

Measuring RAN Peptide Toxicity in C. elegans

Published on: April 30, 2020

Growth Assays to Assess Polyglutamine Toxicity in Yeast

Growth Assays to Assess Polyglutamine Toxicity in Yeast

Published on: March 5, 2012

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

Area of Science:

Neuroscience
Genetics
Molecular Biology

Background:

Huntington's disease like-2 (HDL2) is a neurodegenerative disorder with an unknown primary pathogenic mechanism.
Two potential culprits in HDL2 pathogenesis are CUG-containing RNA and CAG-encoding polyglutamine peptides.

Discussion:

This study investigates the role of polyglutamine peptides versus RNA in HDL2 pathogenesis using a mouse model.
The findings pinpoint the polyglutamine peptide as the key driver of disease progression in HDL2.

Key Insights:

The polyglutamine peptide, not the RNA, is identified as the pathogenic moiety in HDL2.
This research clarifies a long-standing question regarding the molecular basis of HDL2.

Outlook:

Further research can explore therapeutic strategies targeting the polyglutamine peptide in HDL2.
Understanding the precise role of the polyglutamine peptide may offer insights into other polyglutamine diseases.