Publications by authors named "G T Kozlov"
Article Synopsis
- LARPs are RNA-binding proteins with a conserved La motif domain, and LARP1 specifically regulates ribosomal protein synthesis and mRNA stability without a standard RNA binding domain.
- The study found that LARP1 shows a unique preference for recognizing singly guanylated poly(A) sequences, without increased affinity for multiple guanines.
- High-resolution crystal structures and isothermal titration measurements revealed that LARP1 also binds cyclic di-nucleotides with strong affinity, suggesting its role in stabilizing poly(A) tails influenced by guanylation.
Down syndrome is the most frequently occurring genetic condition, with a substantial escalation in risk associated with advanced maternal age. The syndrome is characterized by a diverse range of phenotypes, affecting to some extent all levels of organization, and its progeroid nature - early manifestation of aspects of the senile phenotype. Despite extensive investigations, many aspects and mechanisms of the disease remain unexplored.
View Article and Find Full Text PDFCandidate molecular targets uncovered in mouse lifespan extension studies.
Expert Opin Ther Targets
June 2024
Introduction: Multiple interventions have demonstrated an increase in mouse lifespan. However, non-standardized controls, sex or strain-specific factors, and insufficient focus on targets, hinder the translation of these findings into clinical applications.
Areas Covered: We examined the effects of genetic and drug-based interventions on mice from databases DrugAge, GenAge, the Mouse Phenome Database, and publications from PubMed that led to a lifespan extension of more than 10%, identifying specific molecular targets that were manipulated to achieve the maximum lifespan in mice.
Article Synopsis
- Cystathionine- -synthase (CBS)-pair domain transporters (CNNMs) are important for regulating magnesium levels in the body by transporting magnesium ions and affecting a specific ion channel (TRPM7).
- The study presents the crystal structure of the extracellular part of tapeworm CNNM4, revealing it forms a dimer with specific molecular structures and sites for sugar molecules.
- Mutations in the extracellular domain of human CNNM4 hinder its dimerization, and a similar mutation in mouse CNNM2 negatively affects its ability to transport magnesium in cells.
Cystathionine-β-synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) are an evolutionarily conserved family of magnesium transporters. They promote efflux of Mg ions on their own and influx of divalent cations when expressed with the transient receptor potential ion channel subfamily M member 7 (TRPM7). Recently, ADP-ribosylation factor-like GTPase 15 (ARL15) has been identified as CNNM-binding partner and an inhibitor of divalent cation influx by TRPM7.
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