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| http://dx.doi.org/10.4267/2042/45997 | DOI Listing |
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Structure guided modification of 2-chloro-5-(ethyl-phenyl-sulfamoyl)-N-[2-(2-oxo-pyrrolidin-1-yl)-phenyl]-benzamide to afford selective inhibitors of Cryptosporidium parvum N-myristoyltransferase.
Bioorg Med Chem Lett
January 2025
Department of Biochemistry, University of Washington, Seattle, WA 98195, United States. Electronic address:
Cryptosporidium parvum is a protozoan parasite that causes severe diarrheal illness in children and each year nearly 50,000 children under age 5 die due to the disease. Despite tremendous research efforts, there remains a lack of effective therapies and vaccines. Novel inhibitors against N-myristoyltransferase of C.
View Article and Find Full Text PDFTargeting n-myristoyltransferases promotes a pan-Mammarenavirus inhibition through the degradation of the Z matrix protein.
PLoS Pathog
December 2024
Unité de Biologie des Infections Virales Emergentes, Institut Pasteur, Université Paris Cité, Lyon, France.
Several Old World and New World Mammarenavirus are responsible for hemorrhagic fever in humans. These enveloped viruses have a bi-segmented ambisense RNA genome that encodes four proteins. All Mammarenavirus identified to date share a common dependency on myristoylation: the addition of the C14 myristic acid on the N-terminal G2 residue on two of their proteins.
View Article and Find Full Text PDFZelenirstat Inhibits N-Myristoyltransferases to Disrupt Src Family Kinase Signaling and Oxidative Phosphorylation, Killing Acute Myeloid Leukemia Cells.
Mol Cancer Ther
January 2025
Department of Cell Biology, Faculty of Medicine & Dentistry, University of Alberta, Edmonton, Canada.
Article Synopsis
- Acute myeloid leukemia (AML) is a serious blood cancer with few treatment options and a high chance of coming back after chemotherapy.
- Researchers studied N-myristoylation, a protein modification linked to cancer cell survival, and found that the level of N-myristoyltransferase 2 (NMT2) can indicate patient outcomes.
- They tested a drug called zelenirstat, which inhibits myristoylation, and found it caused cancer cell death and reduced leukemia in models, suggesting it could be an effective new treatment for AML patients with poor prognoses.
Cellular N-Myristoyl Transferases Are Required for Mammarenavirus Multiplication.
Viruses
August 2024
Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
The mammarenavirus matrix Z protein plays critical roles in virus assembly and cell egress. Meanwhile, heterotrimer complexes of a stable signal peptide (SSP) together with glycoprotein subunits GP1 and GP2, generated via co-and post-translational processing of the surface glycoprotein precursor GPC, form the spikes that decorate the virion surface and mediate virus cell entry via receptor-mediated endocytosis. The Z protein and the SSP undergo N-terminal myristoylation by host cell N-myristoyltransferases (NMT1 and NMT2), and G2A mutations that prevent myristoylation of Z or SSP have been shown to affect the Z-mediated virus budding and GP2-mediated fusion activity that is required to complete the virus cell entry process.
View Article and Find Full Text PDFVP0 Myristoylation Is Essential for Senecavirus A Replication.
Pathogens
July 2024
State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150069, China.
Article Synopsis
- Many picornaviruses, including Senecavirus A (SVA), depend on myristoylation of their capsid proteins for effective viral replication, which is facilitated by the enzyme N-myristoyltransferase (NMT).
- Research showed that inhibitors of NMT can effectively block SVA replication, and that knocking out NMT1 in specific cells led to reduced viral replication, while increasing its expression supported replication.
- The study established that myristoylation of SVA’s VP0 protein is crucial for its function and distribution within cells, with specific residues in the protein's structure playing key roles in its ability to replicate.
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