Zobrazeno 1 - 10
of 56
pro vyhledávání: '"Vince J, LiCata"'
Autor:
Vince J. LiCata, Yanling Yang
Publikováno v:
Biochemical and biophysical research communications. 497(1)
Klenow and Klentaq are the large fragment domains of the Pol I DNA polymerases from Escherichia coli and Thermus aquaticus, respectively. Herein, we show that both polymerases can significantly stimulate complementary intermolecular end-joining ligat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b679546f3ebdc9654be70863516d384
https://pubmed.ncbi.nlm.nih.gov/29409896
https://pubmed.ncbi.nlm.nih.gov/29409896
Autor:
Vince J. LiCata, Chin Chi Liu
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 82:785-793
The thermal stability of Taq DNA polymerase is well known, and is the basis for its use in PCR. A comparative thermodynamic characterization of the large fragment domains of Taq (Klentaq) and E. coli (Klenow) DNA polymerases has been performed by obt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e95a11b54b81442c210aa22bfbe3c76f
https://doi.org/10.1002/prot.24458
https://doi.org/10.1002/prot.24458
Autor:
Vince J. LiCata, Yanling Yang
Publikováno v:
Biophysical Chemistry. 159:188-193
Different DNA polymerases partition differently between replication and repair pathways. In this study we examine if two Pol I family polymerases from evolutionarily distant organisms also differ in their preferences for replication versus repair sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bc4537619054dbba8830d0743317dcc
https://doi.org/10.1016/j.bpc.2011.06.008
https://doi.org/10.1016/j.bpc.2011.06.008
Publikováno v:
Journal of Molecular Biology. 401:223-238
The significant enhancing effect of glutamate on DNA binding by Escherichia coli nucleic acid binding proteins has been extensively documented. Glutamate has also often been observed to reduce the apparent linked ion release (Deltan(ions)) upon DNA b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79c150532d1892228d01535cba33ff85
https://doi.org/10.1016/j.jmb.2010.06.009
https://doi.org/10.1016/j.jmb.2010.06.009
Publikováno v:
Polymer Reviews. 48:653-673
The Teaching Craft for Macromolecular Creativity project at Louisiana State University is an experiment in graduate polymer education. With support from the National Science Foundation's Division of Graduate Education, in the form of an IGERT grant,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7f36d9b0eb284d2acc2db12793eb5d47
https://doi.org/10.1080/15583720802445623
https://doi.org/10.1080/15583720802445623
Autor:
Jaycob D. Warfel, Vince J. LiCata
Publikováno v:
DNA repair. 31
Deinococcus radiodurans (Dr) has a significantly more robust DNA repair response than Escherichia coli (Ec), which helps it survive extremely high doses of ionizing radiation and prolonged periods of desiccation. DrRecA protein plays an essential par
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::556b5e94be74765e91421a570911ece5
https://pubmed.ncbi.nlm.nih.gov/26021744
https://pubmed.ncbi.nlm.nih.gov/26021744
Publikováno v:
Biophysical Journal. 90:1739-1751
DNA binding of Klenow polymerase has been characterized with respect to temperature to delineate the thermodynamic driving forces involved in the interaction of this polymerase with primed-template DNA. The temperature dependence of the binding affin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::987ef20fe77c46c77e490f46014355cc
https://doi.org/10.1529/biophysj.105.071837
https://doi.org/10.1529/biophysj.105.071837
Autor:
Allyn J. Schoeffler, Allison M. Joubert, Chin Chi Liu, Fenggang Peng, Farheen Khan, Vince J. LiCata
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 54:616-621
We have examined the chemical denaturations of the Klentaq and Klenow large-fragment domains of the Type 1 DNA polymerases from Thermus aquaticus (Klentaq) and Escherichia coli (Klenow) under identical solution conditions in order to directly compare
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01281c2166644026539e5aeb2dc75537
https://doi.org/10.1002/prot.10641
https://doi.org/10.1002/prot.10641
Autor:
Kausiki Datta, Vince J. LiCata
Publikováno v:
Nucleic Acids Research. 31:5590-5597
DNA binding of the Type 1 DNA polymerase from Thermus aquaticus (Taq polymerase) and its Klentaq large fragment domain have been studied as a function of temperature. Equilibrium binding assays were performed from 5 to 70 degrees C using a fluorescen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c03a6f5cb0669e681001f3560f3293ca
https://doi.org/10.1093/nar/gkg774
https://doi.org/10.1093/nar/gkg774
Publikováno v:
Biochemical Journal. 374:785-792
Thermal denaturations of the type 1 DNA polymerases from Thermus aquaticus (Taq polymerase) and Escherichia coli (Pol 1) have been examined using differential scanning calorimetry and CD spectroscopy. The full-length proteins are single-polypeptide c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::248a5429b7eb27b00ff4a5136e81184b
https://doi.org/10.1042/bj20030323
https://doi.org/10.1042/bj20030323