Results 21 to 30 of about 1,611,597 (332)

Characterization of RNA polymerases from Rous sarcoma virus-induced mouse ascites sarcoma cells. [PDF]

open access: yes, 1979
RNA polymerase was extracted from the Schmidt-Ruppin strain of Rous sarcoma virus (SR-RSV)-induced C3H/He mouse ascites sarcoma cells (SR-C3H). RNA polymerase was separated into RNA polymerases I and II by DEAE-Sephadex chromatography.
Misumi, Hiromasa, Oda, Takuzo
core   +1 more source

A comparative study of DNA-dependent RNA polymerases from rat ascites hepatoma cell nuclei and from rat liver nuclei [PDF]

open access: yes, 1975
DNA-dependent RNA polymerases (EC 2.7.7.6) were extracted and partially purified form the nuclei of rat ascites hepatoma cells (AH-130) induced by 4-dimethylaminoazobenzene.
Misumi, Hiromasa
core   +1 more source

SnapShot: DNA Polymerases I Prokaryotes

open access: yesCell, 2010
The nucleus and mitochondria of eukaryote cells and the nucleoid of prokaryote cells contain remarkable enzymes, called DNA polymerases, which ensure the faithful duplication of genetic material. These enzymatic machines incorporate the building blocks of DNA, deoxyribonucleotide triphosphates (dNTPs), into growing polynucleotide chains. The error rate
Foti, James J., Walker, Graham C.
openaire   +3 more sources

Variable termination sites of DNA polymerases encountering a DNA-protein cross-link. [PDF]

open access: yesPLoS ONE, 2018
DNA-protein cross-links (DPCs) are important DNA lesions induced by endogenous crosslinking agents such as formaldehyde or acetaldehyde, as well as ionizing radiation, cancer chemotherapeutic drugs, and abortive action of some enzymes.
Anna V Yudkina   +2 more
doaj   +1 more source

RNase H enables efficient repair of R-loop induced DNA damage. [PDF]

open access: yes, 2016
R-loops, three-stranded structures that form when transcripts hybridize to chromosomal DNA, are potent agents of genome instability. This instability has been explained by the ability of R-loops to induce DNA damage. Here, we show that persistent R-loops
Amon, Jeremy D, Koshland, Douglas
core   +1 more source

Characterization of DNA Polymerase from Thermus thermophilus MAT72 Phage Tt72

open access: yesProceedings, 2020
Thermophilic phages are recognized as an untapped source of thermostable enzymes relevant in biotechnology; however, their biology is poorly explored. This has led us to start a project aimed at investigating thermophilic phages isolated from geothermal ...
Sebastian Dorawa   +6 more
doaj   +1 more source

Cloning of DNA Polymerase I Geobacillus thermoleovorans SGAir0734 from a Batu Kuwung Hot Spring in Escherichia coli

open access: yesInternational Journal of Technology, 2020
Access to biological engineering has become a critical point of modern science development through polymerase chain reaction (PCR). One of the main components in this process is DNA polymerase, which copies the main template DNA.
Kenny Lischer   +5 more
doaj   +1 more source

Topological impact of noncanonical DNA structures on Klenow fragment of DNA polymerase [PDF]

open access: yes, 2017
Noncanonical DNA structures that stall DNA replication can cause errors in genomic DNA. Here, we investigated how the noncanonical structures formed by sequences in genes associated with a number of diseases impacted DNA polymerization by the Klenow ...
Benabou   +11 more
core   +1 more source

A model for transition of 5 '-nuclease domain of DNA polymerase I from inert to active modes [PDF]

open access: yes, 2011
Bacteria contain DNA polymerase I (PolI), a single polypeptide chain consisting of similar to 930 residues, possessing DNA-dependent DNA polymerase, 3'-5' proofreading and 5'-3' exonuclease (also known as flap endonuclease) activities.
A Díaz   +50 more
core   +4 more sources

Domain exchange: chimeras of Thermus aquaticus DNA polymerase, Escherichia coli DNA polymerase I and Thermotoga neapolitana DNA polymerase [PDF]

open access: yesProtein Engineering, Design and Selection, 2000
The intervening domain of the thermostable Thermus aquaticus DNA polymerase (TAQ: polymerase), which has no catalytic activity, has been exchanged for the 3'-5' exonuclease domain of the homologous mesophile Escherichia coli DNA polymerase I (E.coli pol I) and the homologous thermostable Thermotoga neapolitana DNA polymerase (TNE: polymerase).
B, Villbrandt   +3 more
openaire   +2 more sources

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