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The formation of histamine in food is influenced by temperature, and histamine growth can be inhibited by maintaining a cold chain. However, simply relying on temperature control is insufficient, as certain bacteria can produce the enzyme histidine decarboxylase even at temperatures below 5°C. To address this issue, various methods, such as modified atmosphere packaging, high hydrostatic pressure, and irradiation, have been developed to control histamine in fishery products.

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We report the reversible redox-controlled DNA condensation using a simple dicationic diphenylalanine derivative which contains a disulfide unit as linker. Despite the conventional belief that DNA condensing agents require a charge of +3 or higher, this dicationic molecule functions below its critical aggregation concentration, representing a non-canonical DNA condensing agent. The interaction with DNA of the studied compound combines electrostatic effects with hydrophobic/stacking interactions provided with the diphenylalanine moiety.

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Chromatin remodeling, which involves the histone-to-protamine exchange process during spermiogenesis, is crucial for sperm nuclear condensation and male fertility. However, the key regulators and underlying molecular mechanisms involved in this process remain largely unexplored. In this study, we discovered that deficiency in the family with sequence similarity 170 member A (Fam170a) led to abnormal sperm nuclear morphology and male infertility in mice, mirroring the observation of very low Fam170a transcription levels in sperm of infertile men with teratozoospermia.

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Virtual screening of potential inhibitors of the ATPase site in Acinetobacter baumannii DNA Gyrase.

Comput Biol Med

January 2025

Laboratorio de Fisicoquímica Analítica, Unidad de Investigación Multidisciplinaria, Facultad de Estudios Superiores Cuautitlán, Universidad Nacional Autónoma de México, Cuautitlán Izcalli, Estado de México, 54714, Mexico. Electronic address:

Bacterial resistance is a global public health problem because of the ineffectiveness of conventional antibiotics against super pathogens. To counter this situation, the search for or design of new molecules is essential to inhibit the key proteins involved in several stages of bacterial infection. One of these key proteins is DNA gyrase, which is responsible for packaging and unfolding of DNA chains during replication.

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Six novel phages belonging to the family were isolated using as a host. Phages MuffinTheCat, Badulia, DesireeRose, Bee17, SCoupsA, and LuzDeMundo were purified from environmental samples by students participating in the Science Education Alliance Phage Hunters Advancing Genomics and Evolutionary Science (SEA-PHAGES) program at Alliance University, New York. The phages have linear dsDNA genomes 15,438-15,636 bp with 112-120 bp inverted terminal repeats.

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