Zobrazeno 1 - 10
of 11
pro vyhledávání: '"William M. Lindstrom"'
Autor:
Lisa J. Storrie-Lombardi, Mark Bowman, Daniel R. Harbeck, Brian Haworth, Annie Kirby, William M. Lindstrom, Curtis McCully, Jon Nation, Rachel A. Street, Nikolaus H. Volgenau
Publikováno v:
Observatory Operations: Strategies, Processes, and Systems IX.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b1f525cbdf5a232b875fff2f9e7e9282
https://doi.org/10.1117/12.2630470
https://doi.org/10.1117/12.2630470
Autor:
Samuel L. Schlagman, Victor V. Zinoviev, William M. Lindstrom, A. A. Evdokimov, Stanley Hattman, Norbert O. Reich, Ernst G. Malygin
Publikováno v:
Journal of Biological Chemistry. 278:41749-41755
We compared the (pre)steady-state and single turnover methylation kinetics of bacteriophage T4Dam (DNA-(adenine-N6)-methyltransferase)-mediated methyl group transfer from S-adenosyl-l-methionine (AdoMet) to oligodeoxynucleotide duplexes containing a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89575fbd182e01c6250b63a40aff030c
https://doi.org/10.1074/jbc.m306397200
https://doi.org/10.1074/jbc.m306397200
Publikováno v:
Journal of Molecular Biology. 325:711-720
We show that the kinetic mechanism of the DNA (cytosine-N4-)-methyltransferase M.BamHI, which modifies the underlined cytosine ( GGAT C C ), differs from cytosine C5 methyltransferases, and is similar to that observed with adenine N6 methyltransferas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afc70e9c9110925a259f2117d10c6cee
https://doi.org/10.1016/s0022-2836(02)01282-2
https://doi.org/10.1016/s0022-2836(02)01282-2
Autor:
William M. Lindstrom, Stanley Hattman, Norbert O. Reich, Ovechkina Lg, Victor V. Zinoviev, Ernst G. Malygin, Samuel L. Schlagman, A. A. Evdokimov
Publikováno v:
Nucleic Acids Research. 29:2361-2369
The fluorescence of 2-aminopurine ((2)A)-substituted duplexes (contained in the GATC target site) was investigated by titration with T4 Dam DNA-(N6-adenine)-methyltransferase. With an unmethylated target ((2)A/A duplex) or its methylated derivative (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb848004184f7ffc406dfc5d090ebfd8
https://doi.org/10.1093/nar/29.11.2361
https://doi.org/10.1093/nar/29.11.2361
Autor:
Samuel L. Schlagman, Stanley Hattman, William M. Lindstrom, Norbert O. Reich, Ernst G. Malygin
Publikováno v:
Nucleic Acids Research. 28:4207-4211
The DNA methyltransferase of bacteriophage T4 (T4 Dam MTase) recognizes the palindromic sequence GATC, and catalyzes transfer of the methyl group from S:-adenosyl-L-methionine (AdoMet) to the N(6)-position of adenine [generating N(6)-methyladenine an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::623fbe07f1c69b7ae273d2d8b11057ad
https://doi.org/10.1093/nar/28.21.4207
https://doi.org/10.1093/nar/28.21.4207
Publikováno v:
Journal of Biological Chemistry. 273:2368-2373
DNA methyltransferases are excellent prototypes for investigating DNA distortion and enzyme specificity because catalysis requires the extrahelical stabilization of the target base within the enzyme active site. The energetics and kinetics of base fl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f6bf939233028e943382b08d866be49
https://doi.org/10.1074/jbc.273.4.2368
https://doi.org/10.1074/jbc.273.4.2368
Autor:
Arthur J. Olson, Lily S. Cheng, Rommie E. Amaro, Wilfred W. Li, William M. Lindstrom, David D. L. Minh, J. Andrew McCammon, Jung-Hsin Lin
Publikováno v:
Journal of the American Chemical Society. 129(25)
The emergence and continuing global spread of the highly virulent avian influenza H5N1 has raised concerns of a possible human pandemic. Several approved anti-influenza drugs effectively target the neuraminidase (NA), a surface glycoprotein that clea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5750ad14f46c4bd45143ade4ec801805
https://pubmed.ncbi.nlm.nih.gov/17539643
https://pubmed.ncbi.nlm.nih.gov/17539643
Autor:
Ernst G, Malygin, William M, Lindstrom, Victor V, Zinoviev, Alexey A, Evdokimov, Samuel L, Schlagman, Norbert O, Reich, Stanley, Hattman
Publikováno v:
The Journal of biological chemistry. 278(43)
We compared the (pre)steady-state and single turnover methylation kinetics of bacteriophage T4Dam (DNA-(adenine-N6)-methyltransferase)-mediated methyl group transfer from S-adenosyl-l-methionine (AdoMet) to oligodeoxynucleotide duplexes containing a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1b061a1bd9b73ff035a3fe32216a1178
https://pubmed.ncbi.nlm.nih.gov/12893823
https://pubmed.ncbi.nlm.nih.gov/12893823
Autor:
Ernst G, Malygin, Victor V, Zinoviev, Alexey A, Evdokimov, William M, Lindstrom, Norbert O, Reich, Stanley, Hattman
Publikováno v:
The Journal of biological chemistry. 278(18)
We studied the kinetics of methyl group transfer by the BamHI DNA-(cytosine-N(4)-)-methyltransferase (MTase) from Bacillus amyloliquefaciens to a 20-mer oligodeoxynucleotide duplex containing the palindromic recognition site GGATCC. Under steady stat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b01bcafcb2c1659389ad1e35dbacedee
https://pubmed.ncbi.nlm.nih.gov/12598537
https://pubmed.ncbi.nlm.nih.gov/12598537
Publikováno v:
The Journal of biological chemistry. 275(7)
Pre-steady state partitioning analysis of theHhaI DNA methyltransferase directly demonstrates the catalytic competence of the enzyme·DNA complex and the lack of catalytic competence of the enzyme·S-adenosyl-l-methionine (AdoMet) complex. The enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5c1d7740badedf6a469eb53488a9181
https://pubmed.ncbi.nlm.nih.gov/10671528
https://pubmed.ncbi.nlm.nih.gov/10671528