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

Oxidative modifications in nitrosative stress

J S Stamler, A Hausladen

    Nature Structural Biology
    |April 18, 1998
    PubMed
    Summary
    This summary is machine-generated.

    Understanding protein redox sensitivity requires examining cysteine residue modifications. These modifications are linked to both biological signaling and cellular stress responses.

    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

    Seasonal changes in antioxidants in red spruce (Picea rubens Sarg.) from three field sites in the northeastern United States.

    The New phytologist·2021
    Same author

    Seasonal changes in antioxidants in red spruce as affected by ozone.

    The New phytologist·2021
    Same author

    The antithrombotic effects of organic nitrates.

    Trends in cardiovascular medicine·2011
    Same author

    Inclusion of an S-nitrosylating agent in the insufflating gas does not alter gastric activity in rats following pneumoperitoneum.

    Surgical endoscopy·2006
    Same author

    Nitrosative stress: protection by glutathione-dependent formaldehyde dehydrogenase.

    Redox report : communications in free radical research·2001
    Same author

    Nitrosylation. the prototypic redox-based signaling mechanism.

    Cell·2001
    Same journal

    Fingering nucleic acids: the RNA did it.

    Nature structural biology·2003
    Same journal

    Histone H1.2 as a trigger for apoptosis.

    Nature structural biology·2003
    Same journal

    Tom40: more than just a channel.

    Nature structural biology·2003
    Same journal

    Announcing the worldwide Protein Data Bank.

    Nature structural biology·2003
    Same journal

    Small RNAs come of age.

    Nature structural biology·2003
    Same journal

    Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC.

    Nature structural biology·2003
    See all related articles

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cellular Signaling

    Background:

    • The molecular mechanisms underlying protein redox sensitivity remain largely unknown.
    • Cysteine residues are critical sites for post-translational modifications influenced by reactive oxygen and nitrogen species.

    Discussion:

    • This study explores the spectrum of nitric oxide (NO) and oxygen (O2)-related cysteine modifications.
    • These modifications represent a continuum, functioning as both vital biological signaling events and indicators of cellular stress.

    Key Insights:

    • Redox modifications of cysteine residues play a dual role in cellular function.
    • Distinguishing between signaling pathways and stress responses mediated by these modifications is crucial.

    Outlook:

    Related Experiment Videos

    • Further research is needed to elucidate the precise molecular basis of redox sensitivity.
    • Understanding these modifications can lead to insights into diseases associated with oxidative and nitrosative stress.