Results 301 to 310 of about 125,351 (338)
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Current Protocols in Molecular Biology, 2008
AbstractT4 RNA ligase 1 catalyzes the ATP‐dependent covalent joining of single‐stranded 5′‐phosphoryl termini of DNA or RNA to single‐stranded 3′‐hydroxyl termini of DNA or RNA. T4 RNA ligase 2 also catalyzes the joining of a 3′‐hydroxyl terminus of RNA to a 5′‐phosphorylated RNA or DNA; unlike T4 RNA ligase 1, this enzyme prefers double‐stranded ...
Nicole M, Nichols +2 more
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AbstractT4 RNA ligase 1 catalyzes the ATP‐dependent covalent joining of single‐stranded 5′‐phosphoryl termini of DNA or RNA to single‐stranded 3′‐hydroxyl termini of DNA or RNA. T4 RNA ligase 2 also catalyzes the joining of a 3′‐hydroxyl terminus of RNA to a 5′‐phosphorylated RNA or DNA; unlike T4 RNA ligase 1, this enzyme prefers double‐stranded ...
Nicole M, Nichols +2 more
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European Journal of Medical Genetics, 2009
Ligase IV (LIG4) syndrome belongs to the group of hereditary disorders associated with impaired DNA damage response mechanisms. Subjects affected with this rare autosomal recessive disease exhibit microcephaly, unusual facial features, growth retardation, developmental delay, skin anomalies, and are typically pancytopenic.
Dimitry A, Chistiakov +2 more
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Ligase IV (LIG4) syndrome belongs to the group of hereditary disorders associated with impaired DNA damage response mechanisms. Subjects affected with this rare autosomal recessive disease exhibit microcephaly, unusual facial features, growth retardation, developmental delay, skin anomalies, and are typically pancytopenic.
Dimitry A, Chistiakov +2 more
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Mutation Research/DNA Repair, 1990
Recent studies on eukaryotic DNA ligases are briefly reviewed. The two distinguishable enzymes from mammalian cells, DNA ligase I and DNA ligase II, have been purified to homogeneity and characterized biochemically. Two distinct DNA ligases have also been identified in Drosophila melanogaster embryos.
D D, Lasko, A E, Tomkinson, T, Lindahl
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Recent studies on eukaryotic DNA ligases are briefly reviewed. The two distinguishable enzymes from mammalian cells, DNA ligase I and DNA ligase II, have been purified to homogeneity and characterized biochemically. Two distinct DNA ligases have also been identified in Drosophila melanogaster embryos.
D D, Lasko, A E, Tomkinson, T, Lindahl
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Current Protocols in Molecular Biology, 2011
AbstractThe DNA ligase enzyme family catalyzes the formation of a phosphodiester bond between juxtaposed 5′‐phosphate and 3′‐hydroxyl termini in duplex DNA. This activity can seal nicks in duplex DNA or join double‐stranded DNA fragments having either blunt or cohesive ends.
Gregory J S, Lohman +2 more
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AbstractThe DNA ligase enzyme family catalyzes the formation of a phosphodiester bond between juxtaposed 5′‐phosphate and 3′‐hydroxyl termini in duplex DNA. This activity can seal nicks in duplex DNA or join double‐stranded DNA fragments having either blunt or cohesive ends.
Gregory J S, Lohman +2 more
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BioEssays, 1997
AbstractDNA joining enzymes play an essential role in the maintenance of genomic integrity and stability. Three mammalian genes encoding DNA ligases, LIG1, LIG3 and LIG4, have been identified. Since DNA ligase II appears to be derived from DNA ligase III by a proteolytic mechanism, the three LIG genes can account for the four biochemically distinct DNA
A E, Tomkinson, D S, Levin
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AbstractDNA joining enzymes play an essential role in the maintenance of genomic integrity and stability. Three mammalian genes encoding DNA ligases, LIG1, LIG3 and LIG4, have been identified. Since DNA ligase II appears to be derived from DNA ligase III by a proteolytic mechanism, the three LIG genes can account for the four biochemically distinct DNA
A E, Tomkinson, D S, Levin
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Essays in Biochemistry, 2005
The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds).
Helen C, Ardley, Philip A, Robinson
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The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds).
Helen C, Ardley, Philip A, Robinson
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Current Protocols in Molecular Biology, 1989
AbstractDNA ligases catalyze the formation of phosphodiester bonds between juxtaposed 5' phosphate and a 3'‐hydroxyl terminus in duplex DNA. This activity can repair single‐stranded nicks in duplex DNA and join duplex DNA restriction fragments having either blunt ends or homologous cohesive ends. Two ligases are used for nucleic acid research and their
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AbstractDNA ligases catalyze the formation of phosphodiester bonds between juxtaposed 5' phosphate and a 3'‐hydroxyl terminus in duplex DNA. This activity can repair single‐stranded nicks in duplex DNA and join duplex DNA restriction fragments having either blunt ends or homologous cohesive ends. Two ligases are used for nucleic acid research and their
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2000
Ligase chain reaction (LCR), employing just oligonucleotide probes and Principle and DNA ligase, is capable of detecting approximately
G H, Shimer, K C, Backman
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Ligase chain reaction (LCR), employing just oligonucleotide probes and Principle and DNA ligase, is capable of detecting approximately
G H, Shimer, K C, Backman
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DNA ligases and ligase-based technologies
Clinical and Applied Immunology Reviews, 2001Abstract DNA ligases catalyze the strand joining reaction at a nick junction. The requirement of base-pair complementarity at the nick junction has been explored for development of ligase-based technologies for mutation detection. In oligonucleotide ligation assay (OLA), two DNA probes complementary to the target sequence are joined by DNA ligase ...
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Current Protocols in Molecular Biology, 1991
AbstractT4 RNA ligase, the product of the phage gene 63, is purified from phage‐infected cells. It catalyzes the ATP‐dependent covalent joining of single‐stranded 5'‐phosphoryl termini of DNA or RNA to single‐stranded 3'‐hydroxyl termini of DNA or RNA. This unit describes specific reaction conditions as well as applications such as radioactive labeling
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AbstractT4 RNA ligase, the product of the phage gene 63, is purified from phage‐infected cells. It catalyzes the ATP‐dependent covalent joining of single‐stranded 5'‐phosphoryl termini of DNA or RNA to single‐stranded 3'‐hydroxyl termini of DNA or RNA. This unit describes specific reaction conditions as well as applications such as radioactive labeling
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