Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Keith J. M. Moore"'
Autor:
Keith J. M. Moore, Jeremy Cahill, Guy Aidelberg, Rachel Aronoff, Ali Bektaş, Daniela Bezdan, Daniel J. Butler, Sridar V. Chittur, Martin Codyre, Fernan Federici, Nathan A. Tanner, Scott W. Tighe, Randy True, Sarah B. Ware, Anne L. Wyllie, Evan E. Afshin, Andres Bendesky, Connie B. Chang, Richard Dela Rosa, Eran Elhaik, David Erickson, Andrew S. Goldsborough, George Grills, Kathrin Hadasch, Andrew Hayden, Seong-Young Her, Julie A. Karl, Chang Hee Kim, Alison J. Kriegel, Thomas Kunstman, Zeph Landau, Kevin Land, Bradley W. Langhorst, Ariel B. Lindner, Benjamin E. Mayer, Lee A. McLaughlin, Matthew T. McLaughlin, Jenny Molloy, Christopher Mozsary, Jerry L. Nadler, Melinee D'Silva, David Ng, David H. O'Connor, Jerry E. Ongerth, Olayinka Osuolale, Ana Pinharanda, Dennis Plenker, Ravi Ranjan, Michael Rosbash, Assaf Rotem, Jacob Segarra, Stephan Schürer, Scott Sherrill-Mix, Helena Solo-Gabriele, Shaina To, Merly C. Vogt, Albert D. Yu, Christopher E. Mason
Publikováno v:
J Biomol Tech
As the second year of the COVID-19 pandemic begins, it remains clear that a massive increase in the ability to test for SARS-CoV-2 infections in a myriad of settings is critical to controlling the pandemic and to preparing for future outbreaks. The c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcc7049220c378abd20bf95f74cd84ab
https://pubmed.ncbi.nlm.nih.gov/35136384
https://pubmed.ncbi.nlm.nih.gov/35136384
Autor:
Marie J. Y. Reolo, Carlos S. R. Eleazar, Joseph P. Sonio, Ryonne T. Solon, Janika L. B. Villamor, Alexandra K. Loedin, Keith J. M. Moore
Publikováno v:
J Biomol Tech
The demand for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) molecular diagnostics that are faster, cheaper, and simpler to run than nasopharyngeal-based reverse transcription quantitative PCR (RT-qPCR) tests remains unmet in many part
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::354ae99880918592e9008067c7bed2f6
https://pubmed.ncbi.nlm.nih.gov/35027876
https://pubmed.ncbi.nlm.nih.gov/35027876
Publikováno v:
Journal of Molecular Biology. 288:255-274
Escherichia coli Rep helicase catalyzes the unwinding of duplex DNA in reactions that are coupled to ATP binding and hydrolysis. We have investigated the kinetic mechanism of ATP binding and hydrolysis by a proposed intermediate in Rep-catalyzed DNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3e9b65d8833e5b306bddd24ed6b02b5
https://doi.org/10.1006/jmbi.1999.2666
https://doi.org/10.1006/jmbi.1999.2666
Publikováno v:
Biochemistry. 35:2268-2282
The monomeric Escherichia coli Rep protein undergoes a DNA-induced dimerization upon binding either single-stranded (ss) or duplex DNA with the dimer being the active form of the Rep helicase. Using stopped-flow fluorescence, we have determined a min
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d89ade13f834dc47026a74d062b5186
https://doi.org/10.1021/bi9522763
https://doi.org/10.1021/bi9522763
Publikováno v:
Biochemistry. 35:5726-5734
The Escherichia coli Rep helicase catalyzes the unwinding of duplex DNA using the energy derived from ATP binding and hydrolysis. Rep functions as a dimer but assembles to its active dimeric form only on binding DNA. Each promoter of a dimer contains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9828a2702e6852665e9ed7aee694906
https://doi.org/10.1021/bi952959i
https://doi.org/10.1021/bi952959i
Autor:
Timothy M. Lohman, Keith J. M. Moore
Publikováno v:
Biochemistry. 33:14565-14578
The Escherichia coli Rep protein is a DNA helicase that functions as a homodimer to catalyze the unwinding of duplex DNA during DNA replication in a reaction that is coupled to the binding and hydrolysis of ATP. As a first step toward a molecular und
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e35f3f987166df258b5cb9eb60865b0
https://doi.org/10.1021/bi00252a024
https://doi.org/10.1021/bi00252a024
Autor:
Keith J. M. Moore, Timothy M. Lohman
Publikováno v:
Biochemistry. 33:14550-14564
The Escherichia coli Rep helicase catalyzes the unwinding of duplex DNA in a reaction that is coupled to ATP binding and hydrolysis. The Rep protein is a stable monomer in the absence of DNA but dimerizes upon binding either single-stranded or duplex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b0791f3c8b48d5d7dda94b70f446a6f
https://doi.org/10.1021/bi00252a023
https://doi.org/10.1021/bi00252a023
Publikováno v:
Biochemistry. 33:14306-14316
We describe a fluorescence assay that can be used to monitor helicase-catalyzed unwinding of duplex DNA continuously in real time. The assay is based on the observation that fluorescence resonance energy transfer (FRET) occurs between donor (fluoresc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5e14f43c9365185adbd882b089f6822
https://doi.org/10.1021/bi00251a044
https://doi.org/10.1021/bi00251a044
Publikováno v:
Biochemistry. 32:13575-13583
The solution dynamics of normal and transforming p21ras proteins in both the GTP- and GDP-bound forms were examined with time-resolved fluorescence spectroscopy. The fluorescent 2'(3')-O-(N-methylanthraniloyl) derivatives (mant derivatives) of GTP, d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84031b97797f7bd2922c95f55a4af225
https://doi.org/10.1021/bi00212a025
https://doi.org/10.1021/bi00212a025
Publikováno v:
Journal of Biological Chemistry. 268:10914-10919
Ras GTPase activating proteins (GAPs) contain an invariant motif, -FLR-, within the most conserved region of their catalytic domains. Certain mutations in this motif have greatly reduced activity (Skinner, R. H., Bradley, S., Brown, A. L., Johnson, N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a0a92fbed272a0a08448d9a595198c3
https://doi.org/10.1016/s0021-9258(18)82072-5
https://doi.org/10.1016/s0021-9258(18)82072-5