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

Serpins: finely balanced conformational traps.

Robert N Pike1, Stephen P Bottomley, James A Irving

  • 1Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria, Australia. rob.pike@med.monash.edu.au

IUBMB Life
|October 22, 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

BMN 349, a small molecule inhibitor of Z alpha-1 antitrypsin polymerization, increases secretion and reduces intrahepatic inclusions in a mouse model of disease.

Hepatology (Baltimore, Md.)·2026
Same author

<i>Helicobacter pylori</i> induces the production of interleukin-37 to promote broad immunosuppression and enhance colonization.

Gut microbes·2026
Same author

Characteristics of T-Cells Expressing IL-37 and Its Receptors in Inflammatory Bowel Disease.

International journal of molecular sciences·2026
Same author

Structural basis for uPAR binding to an antibody developed for targeted cancer therapy. Mechanistic insights into flexibility, ligand recognition, and molecular imaging.

Protein science : a publication of the Protein Society·2026
Same author

The mechanism of pathogenic α<sub>1</sub>-antitrypsin aggregation in the human liver.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Susceptibility of alpha-1 antitrypsin deficiency variants to polymer-blocking therapy.

JCI insight·2025
Same journal

ALKBH4 Promotes Osteogenesis via Epigenetic Regulation of BMP2-Wnt/β-Catenin Signaling in Cervical Spine OPLL.

IUBMB life·2026
Same journal

Single-Sequence Deep Learning Delivers Crystal-Quality Models of Covalent K-Ras G12 Hotspot Complexes.

IUBMB life·2026
Same journal

Mechanism of PCSK9-Mediated Macrophage Activation via the CAP1/NF-κB Pathway in CAWS-Induced Kawasaki Disease Vasculitis.

IUBMB life·2026
Same journal

Hormesis and the Golden Ratio: Toward a Universal Estimator of Adaptive Capacity.

IUBMB life·2026
Same journal

MicroRNAs in HPV-Associated Carcinogenesis: Potential Biomarkers in Oropharyngeal and Cervical Cancers.

IUBMB life·2026
Same journal

PGAM1 Orchestrates Cell Cycle Progression, Glycolytic Reprogramming, and Immunosuppressive Microenvironment in Triple-Negative Breast Cancer.

IUBMB life·2026
See all related articles

Serine protease inhibitors (serpins) are crucial for physiological balance, regulating proteases through unique conformational changes. Mutations in serpins can disrupt this balance, leading to various diseases.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • Serine protease inhibitors (serpins) are vital proteins involved in numerous physiological systems.
  • Their inhibitory function relies on unique conformational changes, essential for protease regulation.
  • Serpins play roles in both extracellular (e.g., coagulation) and intracellular processes (e.g., immune cell protection).

Purpose of the Study:

  • To elucidate the critical roles of serpins in maintaining physiological homeostasis.
  • To understand the mechanism of serpin-mediated protease inhibition.
  • To explore the consequences of mutations on serpin structure and function.

Main Methods:

  • Structural analysis of serpin conformational changes.
  • Investigation of serpin function in proteolytic cascades like coagulation.

Related Experiment Videos

  • Examination of intracellular serpin roles, including immune cell protection.
  • Analysis of disease-associated serpin mutations.

    • Main Results:

    • Serpins utilize conformational dynamics to inhibit target proteases effectively.
    • Modulators fine-tune serpin activity, particularly in proteolytic cascades.
    • Intracellular serpins protect cells from self-inflicted protease damage.
    • Mutations in critical serpin positions lead to disease, underscoring their importance in health.

    Conclusions:

    • Serpins are essential regulators of protease activity, critical for physiological health.
    • The delicate balance of serpin function is susceptible to disruptive mutations.
    • Understanding serpin mechanisms and mutations is key to comprehending and treating associated diseases.