Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Karen L. Menge"'
Autor:
Dominic Yurk, Karen L. Menge, Claudia Shin, Scott E. Fraser, Aditya Rajagopal, Gregory J. Tsongalis, Thomas A. Tombrello, Lucien Jacky
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-8 (2019)
Scientific Reports
Scientific Reports
The real time polymerase chain reaction (rtPCR) is an essential method for detecting nucleic acids that has a wide range of clinical and research applications. Current multiplexed rtPCR is capable of detecting four to six nucleic acid targets in a si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ee6ced1756cbfb277cfba9635c08c77
https://doi.org/10.1038/s41598-018-37732-y
https://doi.org/10.1038/s41598-018-37732-y
Autor:
Karen L. Menge, Floyd R. Bryant
Publikováno v:
Biochemistry. 31:5151-5157
The structurally related nucleoside triphosphates, adenosine triphosphate (ATP), purine riboside triphosphate (PTP), inosine triphosphate (ITP), and guanosine triphosphate (GTP), are all hydrolyzed by the recA protein with the same turnover number (1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e0039c513bb52c3d9207e00eee6efa3
https://doi.org/10.1021/bi00137a009
https://doi.org/10.1021/bi00137a009
Autor:
Soheil Rahmati, Karen L. Menge, Beverly R. Nodes, Geoffrey O. Hudson, Robert Almassy, Ellen W. Moomaw, Zdenek Hostomsky, Zuzana Hostomska
Publikováno v:
Biochemistry. 34(49)
The crystal structure of the catalytic domain of rat DNA polymerase beta revealed that Asp256 is located in proximity to the previously identified active site residues Asp190 and Asp192. We have prepared and kinetically characterized the nucleotidyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6a6aad5907d6e92119ca157ae92c6b0
https://pubmed.ncbi.nlm.nih.gov/8519750
https://pubmed.ncbi.nlm.nih.gov/8519750
Autor:
Karen L. Menge, Floyd R. Bryant
Publikováno v:
Biochemistry. 31(22)
We have examined the effects of the structurally related nucleoside triphosphates, adenosine triphosphate (ATP), purine riboside triphosphate (PTP), inosine triphosphate (ITP), and guanosine triphosphate (GTP), on the recA protein-promoted DNA renatu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8012312ba41b628f175c3ea106d6c5a4
https://pubmed.ncbi.nlm.nih.gov/1606139
https://pubmed.ncbi.nlm.nih.gov/1606139
Autor:
Karen L. Menge, Floyd R. Bryant
Publikováno v:
Biochemistry. 27:2635-2640
The cooperativity of the single-stranded DNA dependent nucleoside triphosphatase activity of the recA protein was investigated by examining the influence of a good substrate (ATP) on the hydrolysis of a poor substrate (GTP). At pH 7.5 and 37 degrees
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21174197a43ca7ecc2eac936988d0ae3
https://doi.org/10.1021/bi00407a055
https://doi.org/10.1021/bi00407a055
Publikováno v:
Biochemistry. 28(3)
Quantitative agarose gel assays reveal that the recA protein promoted renaturation of complementary DNA strands (phi X DNA) proceeds in two stages. The first stage results in the formation of unit-length duplex DNA as well as a distribution of other
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fd69bb1adb67882a8077bcbdf0c0bb9
https://pubmed.ncbi.nlm.nih.gov/2523733
https://pubmed.ncbi.nlm.nih.gov/2523733