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

Leaky Scanning02:28

Leaky Scanning

5.8K
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...
5.8K
Initiation of Translation02:33

Initiation of Translation

39.9K
Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
39.9K
Eukaryotic Transcription Inhibitors01:52

Eukaryotic Transcription Inhibitors

11.2K
Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells.
Eukaryotic transcription inhibitors usually contain two distinct domains, a...
11.2K
Regulation of Expression Occurs at Multiple Steps02:24

Regulation of Expression Occurs at Multiple Steps

26.8K
Gene expression can be regulated at almost every step from gene to protein. Transcription is the step that is most commonly regulated. This involves the binding of proteins to short regulatory sequences on the DNA. This association can either promote or inhibit the transcription of a gene associated with the respective sequence.
Transcription results in the generation of precursor (pre-mRNA) that consists of both exons and introns, which needs further processing before being translated to a...
26.8K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

3.4K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
3.4K
Regulation of Expression at Multiple Steps01:23

Regulation of Expression at Multiple Steps

1.5K
The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the...
1.5K

You might also read

Related Articles

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

Sort by
Same author

Appendiceal endometriosis mimicking acute appendicitis in a young woman: A case report.

Case reports in women's health·2026
Same author

Comment on "Comparison of ChatGPT-3.5, ChatGPT-4.0 and DeepSeek in generating dietary plans for patients with chronic kidney disease: A focus on nutritional accuracy and dietary inflammation".

Nutrition (Burbank, Los Angeles County, Calif.)·2026
Same author

Genome Amplification and Altered Transcriptome Aid in Survival and Enhanced Protein Secretion in Tunicamycin-Resistant CHOK1 Cells.

Biotechnology journal·2025
Same author

Salutary Effects of Overexpression of Rsm22, an Assembly Factor for the Mitochondrial Ribosome, on Frataxin/Yfh1 Depletion Phenotypes in <i>Saccharomyces cerevisiae</i>.

Biomolecules·2025
Same author

DTBA-net: Drug-Target Binding Affinity prediction using feature selection in hybrid CNN model.

Journal of computer-aided molecular design·2025
Same author

Assessment of knowledge of breast cancer risk factors and practice of breast self-examination among students at CSJM university, Kanpur.

Journal of the National Medical Association·2025

Related Experiment Video

Updated: Mar 13, 2026

Development of a Hepatitis B Virus Reporter System to Monitor the Early Stages of the Replication Cycle
09:35

Development of a Hepatitis B Virus Reporter System to Monitor the Early Stages of the Replication Cycle

Published on: February 1, 2017

14.1K

Modulation of HCV replication and translation by ErbB3 binding protein1 isoforms.

Priya Mishra1, Updesh Dixit1, Ashutosh K Pandey1

  • 1Department of Microbiology, Biochemistry, and Molecular Genetics, Rutgers New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, NJ 07103, USA.

Virology
|October 23, 2016
PubMed
Summary

ErbB3 binding protein 1 (Ebp-1) has two isoforms that differentially regulate Hepatitis C virus (HCV) replication. The p48 isoform promotes viral replication, while p42 inhibits it by modulating PKR activity.

Keywords:
Ebp1isoformsErbB3 binding protein1HCV replicationPKR activation

More Related Videos

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors
16:49

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors

Published on: July 16, 2012

12.1K
A Protocol for Analyzing Hepatitis C Virus Replication
13:04

A Protocol for Analyzing Hepatitis C Virus Replication

Published on: June 26, 2014

24.8K

Related Experiment Videos

Last Updated: Mar 13, 2026

Development of a Hepatitis B Virus Reporter System to Monitor the Early Stages of the Replication Cycle
09:35

Development of a Hepatitis B Virus Reporter System to Monitor the Early Stages of the Replication Cycle

Published on: February 1, 2017

14.1K
Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors
16:49

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors

Published on: July 16, 2012

12.1K
A Protocol for Analyzing Hepatitis C Virus Replication
13:04

A Protocol for Analyzing Hepatitis C Virus Replication

Published on: June 26, 2014

24.8K

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • Hepatitis C virus (HCV) replication relies on host cell factors.
  • ErbB3 binding protein 1 (Ebp-1) is a newly identified host factor interacting with HCV RNA.
  • Ebp-1 exists in two isoforms, p48 and p42, generated by alternative splicing.

Purpose of the Study:

  • To investigate the distinct roles of Ebp-1 isoforms in HCV replication.
  • To elucidate the mechanism by which Ebp-1 isoforms modulate HCV replication and host immune response.

Main Methods:

  • Identifying and characterizing Ebp-1 isoforms.
  • Analyzing the interaction of Ebp-1 isoforms with HCV proteins (NS5A, NS5B) and host factor PKR.
  • Assessing the impact of Ebp-1 isoforms on HCV replication using transient expression in knockdown cells.
  • Measuring the effect of Ebp-1 isoforms on PKR autophosphorylation.

Main Results:

  • Both Ebp-1 p48 and p42 isoforms interact with HCV NS5A, NS5B, and PKR.
  • Ebp-1 p48 isoform promotes HCV replication and localizes in cytoplasm and nuclei.
  • Ebp-1 p42 isoform inhibits HCV replication and localizes exclusively in the cytoplasm.
  • Ebp-1 p42 enhances PKR autophosphorylation, while Ebp-1 p48 inhibits it.

Conclusions:

  • Ebp-1 isoforms play opposing roles in regulating HCV replication.
  • The differential modulation of PKR by Ebp-1 isoforms is a key mechanism for HCV replication.
  • HCV may evade innate antiviral immunity by utilizing the p48 isoform to inhibit p42-mediated PKR activation and subsequent viral replication inhibition.