Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Kristi Wojtuszewski"'
Publikováno v:
Biochemistry. 45:5039-5047
The fluorescent adenosine analogue 4-amino-8-(2-deoxy-beta-d-ribofuranosyl)-5'-O-dimethoxytrityl-6-methyl-7(8H)-pteridone (6MAP) has been used to perform residue specific analyses of DNA A-tracts during the premelting transition. DNA A-tracts, which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98893bf20254a630ddee285c017e776b
https://doi.org/10.1021/bi0518343
https://doi.org/10.1021/bi0518343
Publikováno v:
Biophysical Journal. 86:1625-1631
The effects of HU, the histone-like protein from Escherichia coli, on the equilibrium cyclization of duplex DNAs have been observed as a function of protein concentration and DNA sequence. The results indicate that the presence of HU significantly en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3d4d2dedaf78355944f3f250b3ccec9
https://doi.org/10.1016/s0006-3495(04)74230-7
https://doi.org/10.1016/s0006-3495(04)74230-7
Publikováno v:
Journal of biomolecular structuredynamics. 17
UV resonance Raman (UVRR) spectroscopy has been used to investigate the three purine bases, adenine, guanine and inosine, as a function of pH. Excitation wavelengths of 260 and 210 nm were used to probe the in-plane ring stretching frequencies and th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e9c5bd377810c6cf32b6c37eb9c635c
https://pubmed.ncbi.nlm.nih.gov/22607441
https://pubmed.ncbi.nlm.nih.gov/22607441
Autor:
Jay R. Knutson, Aleksandr V. Smirnov, Frank M. Balis, Mary E. Hawkins, Kristi Wojtuszewski Poulin
Two different microenvironments in the DNA sequence 5′-act aGa gat ccc tca gac cct ttt agt cag tGt gga-3′ (in both single- and double-stranded forms) are explored using two similar fluorescent nucleoside analogues, 3MI and 6MI. Each probe was eva
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41f219f178e7211863fa3c20a15f0160
https://europepmc.org/articles/PMC3412956/
https://europepmc.org/articles/PMC3412956/
Autor:
Kristi Wojtuszewski, Ishita Mukerji
Publikováno v:
Protein science : a publication of the Protein Society. 13(9)
HU, a multifunctional DNA-binding protein, participates in several cellular functions including growth, recombination, replication and transposition (Drlica and Rouviere-Yaniv 1987). Originally identified as a histone-like protein (Rouviere-Yaniv and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a55eefb5b8dc856d1ae275145a0ca61
https://pubmed.ncbi.nlm.nih.gov/15322284
https://pubmed.ncbi.nlm.nih.gov/15322284
Autor:
Kristi Wojtuszewski, Ishita Mukerji
Publikováno v:
Biochemistry. 42(10)
HU, an architectural DNA-binding protein, either stabilizes DNA in a bent conformation or induces a bend upon binding to give other proteins access to the DNA. In this study, HU binding affinity for a bent DNA sequence relative to a linear sequence w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5c174d097153c40a97895db5a83888a
https://pubmed.ncbi.nlm.nih.gov/12627977
https://pubmed.ncbi.nlm.nih.gov/12627977
Autor:
Kristi Wojtuszewski, Matthew R. Trojan, Jennifer Cheek, Megan Kibbey, Ryan M. McGhan, Joan B. Broderick, Timothy F. Henshaw, Sheila R. Smith, Amy Kopf, William E. Broderick
Publikováno v:
Biochemical and biophysical research communications. 269(2)
Pyruvate formate-lyase-activating enzyme (PFL-AE) from Escherichia coli ( E. coli ) catalyzes the stereospecific abstraction of a hydrogen atom from Gly734 of pyruvate formate-lyase (PFL) in a reaction that is strictly dependent on the cosubstrate S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c9782ee902272c21d86cabe32b5bbf9
https://pubmed.ncbi.nlm.nih.gov/10708574
https://pubmed.ncbi.nlm.nih.gov/10708574
Autor:
Mary E. Hawkins, Kristi Wojtuszewski Poulin, Frank M. Balis, Jay R. Knutson, Aleksandr V. Smirnov
Publikováno v:
Biophysical Journal. 96:402a
We explored two different microenvironments in the sequence; 5′-actaGagatccctcagacccttttagtcagtGtgga -3′ in single and duplex form using two similar nucleoside analogs. 3MI and 6MI were each investigated in two different environments, one flanked
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3b2da7ba2dbc95872d67d2bf1fe5599
https://doi.org/10.1016/j.bpj.2008.12.2046
https://doi.org/10.1016/j.bpj.2008.12.2046
Autor:
Timothy F. Henshaw, Michael K. Johnson, Joan B. Broderick, Kristi Wojtuszewski, Randall E. Duderstadt, Daniel C. Fernandez
Publikováno v:
Journal of the American Chemical Society. 119:7396-7397
Only a few enzymes are known to utilize stable protein-based radicals as part of their catalytic cycles.1 Among these are both the aerobic and anaerobic ribonucleotide reductases and pyruvate formate-lyase from Escherichia coli. Aerobic and anaerobic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::079849bcdea1dca72ecc159e6805f892
https://doi.org/10.1021/ja9711425
https://doi.org/10.1021/ja9711425
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