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Helicases and human diseases [PDF]
Frontiers in Genetics, 2015 Recent progress in pharmaceutical sciences has made it possible for us to live longer and longer. For example, antibiotics and vaccines have been developed that were successfully administered to patients with infectious diseases. A number of effective drugs for specific diseases could be purified from natural resources or created by chemical synthesis,
Yasuhiro Furuichi +2 more
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Switching roles for a helicase [PDF]
Cell Cycle, 2013 Helicases are widespread enzymes that share a core RecA fold and characteristic amino acid motifs which together form an ATP binding/hydrolysis site.1 For the classical helicases (i.e., those which conform to the family name), ATP-binding provides energy to drive the separation of polynucleotide duplexes into single strands. There are also many enzymes
Seidel, Ralf, Szczelkun, Mark D
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Mechanisms of hexameric helicases [PDF]
Critical Reviews in Biochemistry and Molecular Biology, 2021 Ring-shaped hexameric helicases are essential motor proteins that separate duplex nucleic acid strands for DNA replication, recombination, and transcriptional regulation. Two evolutionarily distinct lineages of these enzymes, predicated on RecA and AAA+ ATPase folds, have been identified and characterized to date.
Amy J. Fernandez, James M. Berger
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Viruses, 2017 West Nile virus (WNV) is a neurotropic flavivirus that can cause encephalitis in mammalian and avian hosts. In America, the virulent WNV strain (NY99) is causing yearly outbreaks of encephalitis in humans and horses, while in Australia the less virulent ...
Yin Xiang Setoh +5 more
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Frontiers in Bioscience, 2013 Superfamily 1 helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along, and concomitant unwinding of, DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and, accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination and ...
Gilhooly, Neville Surain +2 more
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Structural basis for DEAH-helicase activation by G-patch proteins
Proceedings of the National Academy of Sciences of the United States of America, 2020 Significance RNA helicases exert mechanical force that changes RNA configurations in many essential cellular pathways, e.g., during mRNA maturation or assembly of ribosomes.
M. Studer +4 more
semanticscholar +1 more source
Opening of DNA double strands by helicases. Active versus passive opening [PDF]
, 2002 Helicase opening of double-stranded nucleic acids may be "active" (the helicase directly destabilizes the dsNA to promote opening) or "passive" (the helicase binds ssNA available due to a thermal fluctuation which opens part of the dsNA).
A. W. Hunter +14 more
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G-quadruplexes and helicases [PDF]
Nucleic Acids Research, 2016 Guanine-rich DNA strands can fold in vitro into non-canonical DNA structures called G-quadruplexes. These structures may be very stable under physiological conditions. Evidence suggests that G-quadruplex structures may act as 'knots' within genomic DNA, and it has been hypothesized that proteins may have evolved to remove these structures.
Anne Bourdoncle +7 more
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Microorganisms, 2020 Brucellosis is still a global health issue, and surveillance and control of this zoonotic disease in livestock remains a challenge. Human outbreaks are mainly linked to the consumption of unpasteurized dairy products.
Michaela Projahn +3 more
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Archives of medical science : AMS, 2020 Introduction The extreme health and economic problems in the world due to the SARS-CoV-2 infection have led to an urgent need to identify potential drug targets for treating coronavirus disease 2019 (COVID-19).
J. Borgio +8 more
semanticscholar +1 more source