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Structural Insights into Salinosporamide a Mediated Inhibition of the Human 20S Proteasome

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F25%3A00618755" target="_blank" >RIV/61388963:_____/25:00618755 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:90127/25:00143937

  • Result on the web

    <a href="https://doi.org/10.3390/molecules30061386" target="_blank" >https://doi.org/10.3390/molecules30061386</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/molecules30061386" target="_blank" >10.3390/molecules30061386</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structural Insights into Salinosporamide a Mediated Inhibition of the Human 20S Proteasome

  • Original language description

    The 20S proteasome, a critical component of the ubiquitin-proteasome system, plays a central role in regulating protein degradation in eukaryotic cells. Marizomib (MZB), also known as salinosporamide A, is a natural gamma-lactam-beta-lactone compound derived from Salinispora tropica and is a potent 20S proteasome covalent inhibitor with demonstrated anticancer properties. Its broad-spectrum inhibition of all three proteasome subunits and its ability to cross the blood-brain barrier has made it a promising therapeutic candidate for glioblastoma. In addition to this, MZB also demonstrates significant inhibition against the 20S proteasome of Trichomonas vaginalis (Tv20S), a protozoan parasite, suggesting its potential for parasitic treatments. Here, we present the cryo-EM structure of the human 20S proteasome in complex with MZB at 2.55 & Aring, resolution. This structure reveals the binding mode of MZB to all six catalytic subunits within the two beta-rings of the 20S proteasome, providing a detailed molecular understanding of its irreversible inhibitory mechanism. These findings enhance the therapeutic potential of MZB for both cancer and parasitic diseases at the molecular level and highlight marine-derived natural products in targeting the proteasome for therapeutic applications.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/LX22NPO5103" target="_blank" >LX22NPO5103: National Institute of Virology and Bacteriology</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2025

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Molecules

  • ISSN

    1420-3049

  • e-ISSN

    1420-3049

  • Volume of the periodical

    30

  • Issue of the periodical within the volume

    6

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    12

  • Pages from-to

    1386

  • UT code for WoS article

    001452896100001

  • EID of the result in the Scopus database

    2-s2.0-105001140522