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Biochemical characterization and mutational analysis of lysophosphatidic acid acyltransferases of Escherichia coli highlighting their involvement in the generation of membrane phospholipid diversity.
J Biochem
December 2024
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Article Synopsis
- Lysophosphatidic acid acyltransferase (LPAAT) is an important enzyme in phospholipid biosynthesis, converting lysophosphatidic acid to phosphatidic acid, with two types identified in E. coli: EcPlsC and EcYihG.
- The study established a method to purify both EcPlsC and EcYihG in their active forms, revealing that EcPlsC prefers unsaturated fatty acyl-CoAs at optimal conditions of pH 8.0 and 37 °C, while EcYihG favors saturated acyl-CoAs at pH 7.5 and 30 °C.
- Mutational analysis using
CCDC69 maintains genome integrity by regulating KIF2C/MCAK depolymerase activity and the stability of the chromosomal passenger complex.
Sci Rep
December 2024
CRBM CNRS UMR 5237, Equipe Cycle Cellulaire, Université de Montpellier, 1919 Route de Mende, 34293, Montpellier, France.
Accurate genome inheritance during cell division relies on a complex chromosome segregation mechanism. This process occurs once all the kinetochores of sister chromatids are attached to microtubules emanating from the opposite poles of the mitotic spindle. To control the precision of this mechanism, the Chromosome Passenger Complex (CPC) actively identifies and corrects improper microtubule attachments.
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 PDFC. elegans PPEF-type phosphatase (Retinal degeneration C ortholog) functions in diverse classes of cilia to regulate nematode behaviors.
Sci Rep
November 2024
Department of Molecular Biology and Biochemistry, Simon Fraser University, 8888 University Drive, Burnaby, BC, V5A 1S6, Canada.
Primary (non-motile) cilia represent structurally and functionally diverse organelles whose roles as specialized cellular antenna are central to animal cell signaling pathways, sensory physiology and development. An ever-growing number of ciliary proteins, including those found in vertebrate photoreceptors, have been uncovered and linked to human disorders termed ciliopathies. Here, we demonstrate that an evolutionarily-conserved PPEF-family serine-threonine phosphatase, not functionally linked to cilia in any organism but associated with rhabdomeric (non-ciliary) photoreceptor degeneration in the Drosophila rdgC (retinal degeneration C) mutant, is a bona fide ciliary protein in C.
View Article and Find Full Text PDFClinical Pharmacology of Asciminib: A Review.
Clin Pharmacokinet
November 2024
Novartis Biomedical Research, Fabrikstrasse 2, 4056, Basel, Switzerland.
Asciminib is a first-in-class allosteric inhibitor of the kinase activity of BCR::ABL1, specifically targeting the ABL myristoyl pocket (STAMP). This review focuses on the pharmacokinetic (PK) and pharmacodynamic data of asciminib, which is approved at a total daily dose of 80 mg for the treatment of adult patients with chronic myeloid leukemia in chronic phase who are either resistant or intolerant to ≥ 2 tyrosine kinase inhibitors or those harboring the T315I mutation (at a dose of 200 mg twice daily). Asciminib is predicted to be almost completely absorbed from the gut, with an absolute bioavailability (F) of approximately 73%.
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