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 Experiment Videos

Structural features of prions explored by sequence analysis I. Sequence data.

J P Mornon1, K Prat, F Dupuis

  • 1Systèmes Moléculaires & Biologie Structurale, LMCP, CNRS UMR 7590, Universités Paris 6 et Paris 7, France. mornon@lmcp.jussieu.fr

Cellular and Molecular Life Sciences : CMLS
|October 5, 2002
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Group-based exercice training programs for military members presenting musculoskeletal disorders - protocol for a pragmatic randomized controlled trial.

BMC musculoskeletal disorders·2022
Same author

Publisher Correction: SLX4 interacts with RTEL1 to prevent transcription-mediated DNA replication perturbations.

Nature structural & molecular biology·2020
Same author

Author Correction: SLX4 interacts with RTEL1 to prevent transcription-mediated DNA replication perturbations.

Nature structural & molecular biology·2020
Same author

SLX4 interacts with RTEL1 to prevent transcription-mediated DNA replication perturbations.

Nature structural & molecular biology·2020
Same author

mySinusitisCoach: patient empowerment in chronic rhinosinusitis using mobile technology.

Rhinology·2018
Same author

MP29-02 reduces nasal hyperreactivity and nasal mediators in patients with house dust mite-allergic rhinitis.

Allergy·2017
Same journal

PHLDA1 knockdown exacerbates emphysema in COPD by attenuating proliferation of alveolar type II cells via modulating GLI1 nuclear translocation.

Cellular and molecular life sciences : CMLS·2026
Same journal

Single-Cell dissection of fibrodysplasia ossificans progressiva identifies SPP1 as a mediator of macrophage-fibroadipogenic progenitors crosstalk.

Cellular and molecular life sciences : CMLS·2026
Same journal

Ablation of the renal tubular gluconeogenic enzyme PCK1 drives AKI-to-CKD transition by negatively regulating the TGF-β/Smad3 signaling pathway.

Cellular and molecular life sciences : CMLS·2026
Same journal

LncRNA modulates Dpp-mediated wing development to influence flight in Aedes aegypti.

Cellular and molecular life sciences : CMLS·2026
Same journal

TROP2 promotes bone metastasis of colorectal cancer through interaction with the fibronectin-integrin axis.

Cellular and molecular life sciences : CMLS·2026
Same journal

PRMT5-Cacna1d axis maintains calcium homeostasis to regulate postnatal motor development in mice.

Cellular and molecular life sciences : CMLS·2026
See all related articles

Sequence analysis reveals novel prion protein (PrP) relationships. Findings suggest a prion-like domain in foamy retroviruses and structural links to interferon-inducible proteins and TATA-box-binding protein.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Virology

Background:

  • Animal prion proteins (PrPs) exhibit high sequence homogeneity, limiting comparative analysis.
  • Understanding PrP structure and function is crucial for neurodegenerative disease research.

Purpose of the Study:

  • To identify proteins structurally or functionally related to prions using sequence analysis.
  • To explore potential origins and mechanisms of prion protein misfolding.

Main Methods:

  • Utilized a suite of sequence analysis tools to compare PrP sequences with other protein families.
  • Focused on identifying conserved domains and structural similarities.

Main Results:

  • Identified a putative prion-like domain in the envelope of foamy retroviruses.

Related Experiment Videos

  • Detected similarities between prions and an interferon-inducible membrane protein.
  • Proposed TATA-box-binding protein as a structural scaffold involved in PrP(C) to PrP(Sc) conversion.

    • Conclusions:

    • Sequence analysis can reveal distant relationships for homogenous protein families like prions.
    • Foamy retroviruses and interferon-inducible proteins may share evolutionary or functional links with prions.
    • The TATA-box-binding protein's role as a scaffold offers insights into prion pathogenesis.