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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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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
openaire +3 more sources
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
openaire +3 more sources
Duplex DNA from Sites of Helicase-Polymerase Uncoupling Links Non-B DNA Structure Formation to Replicative Stress [PDF]
, 2020 BACKGROUND: Replication impediments can produce helicase-polymerase uncoupling allowing lagging strand synthesis to continue for as much as 6 kb from the site of the impediment.
Abdelhamid, Mahmoud A S +9 more
core +2 more sources
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
openaire +4 more sources
Identification of Five Putative Yeast RNA Helicase Genes [PDF]
, 1990 The RNA helicase gene family encodes a group of eight homologous proteins that share regions of sequence similarity. This group of evolutionarily conserved proteins presumably all utilize ATP (or some other nucleoside triphosphate) as an energy source ...
Abelson, John +2 more
core +1 more source
European Journal of Biology, 2022 Objective: Coronavirus Disease 2019 (COVID19) is a viral disease caused by Severe Acute Respiratory Syndrome Coronavirus-2 (SARS CoV-2). The high mutation propensity of the SARS CoV-2 genome is one of the biggest threats to the long-term validity of ...
Ekrem Akbulut
doaj +1 more source
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
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
openaire +3 more sources
The Nuclease Activity of the Yeast Dna2 Protein, Which Is Related to the RecB-like Nucleases, Is Essential in Vivo [PDF]
, 2000 Saccharomyces cerevisiae Dna2 protein is required for DNA replication and repair and is associated with multiple biochemical activities: DNA-dependent ATPase, DNA helicase, and DNA nuclease.
Budd, Martin E. +2 more
core +1 more source