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DNA polymerase μ (Pol μ) is the only template-dependent human DNA polymerase capable of repairing double-strand DNA breaks (DSBs) with unpaired 3′ ends in nonhomologous end joining (NHEJ).
Its preserved exonuclease activity indicates that it can bind DNA and suggests that the ... codon deletion in POLD1 affecting the polymerase active site causes a markedly different phenotype ...
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AZoLifeSciences on MSNStudy Reveals RNA Polymerase I Stalling Mechanism at Abasic DNA Damage SitesNew study shows RNA polymerase I halts at abasic DNA damage, helping prevent faulty rRNA production and exposing lesions for ...
Biology lectures teach students that when a cell’s replication machinery comes together, DNA polymerase takes off down the double-helix like a car on a highway ...
This observation is critical to understanding how the initial RNA-primed template is handed off from the primase active site in one subunit (where RNA synthesis occurs) to the DNA polymerase ...
RNA Polymerase Active Site Cavity Deforms the DNA Building Blocks To understand how RNA polymerases avoid using DNA building blocks, a research team from the University of Turku headed by ...
When TV shows like CSI: Crime Scene Investigation portray DNA processing in the forensic lab, the results appear instantly with a DNA match wrapping up the case in hours. However, the ...
During this process, DNA polymerase “reads” the existing DNA strands to create two new strands that match the existing ones. DNA Polymerase enzyme syntheses labeled educational vector ...
Taq polymerase is the heat-stable (thermostable) DNA polymerase extracted from the ... Consequently, the Taq polymerase only becomes active after the temperature destroys the monoclonal antibody ...
At the heart of this method lies the Bst DNA polymerase, whose enzymatic properties—such as strand displacement activity, thermostability, and catalytic efficiency—are critical to the success ...
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