Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Sandra L. Shaner"'
Autor:
Sandra L. Shaner, Orlando H. Gumbs
Publikováno v:
Biochemistry. 37:11692-11706
The Escherichia coli RecA protein promotes DNA strand exchange in homologous recombination and recombinational DNA repair. Stopped-flow kinetics and fluorescence resonance energy transfer (FRET) were used to study RecA-mediated strand exchange betwee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad79494bcf6aa7880678806358920e0e
https://doi.org/10.1021/bi980646s
https://doi.org/10.1021/bi980646s
Publikováno v:
Journal of Molecular Recognition. 9:468-473
Equilibrium binding of Escherichia coli LexA repressor to the recA operator was studied by the polyacrylamide gel mobility shift assay as a function of solution conditions. In the presence of NaCl at 20 degrees C, there was a significant salt depende
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ebe2200ffdb10e88f65bac7b1140e29e
https://doi.org/10.1002/(sici)1099-1352(199634/12)9:5/6<468::aid-jmr284>3.0.co
https://doi.org/10.1002/(sici)1099-1352(199634/12)9:5/6<468::aid-jmr284>3.0.co
Autor:
A. Madan Kumar, Chad Messer, Julie . Choi, Ge Zhang, Connie M. Drysdale, Vincent P. Schulz, Krishnan Nandabalan, Ruhong Jiang, Min Seob Lee, Beena Koshy, Gualberto Ruaño, Debra A. Tanguay, Anne Chew, Theodore S. Kalbfleisch, J. Claiborne Stephens, Kevin M. Arnold, Tara Acharya, Julie A. Schneider, Jin-Hua Han, Chuanbo Xu, Scott E. Stanley, Jicheng Duan, Sandra L. Shaner, Richard S. Judson, Gerald F. Vovis, William R. Newell, Janet L. Carr, Andreas Windemuth
Publikováno v:
Science (New York, N.Y.). 293(5529)
Variation within genes has important implications for all biological traits. We identified 3899 single nucleotide polymorphisms (SNPs) that were present within 313 genes from 82 unrelated individuals of diverse ancestry, and we organized the SNPs int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::484bcbf1384ad38d88a9bf64c49fe5ae
https://pubmed.ncbi.nlm.nih.gov/11452081
https://pubmed.ncbi.nlm.nih.gov/11452081
Autor:
Sandra L Shaner
Publikováno v:
eLS
Nonspecific protein–DNA complexes are those that form with identical affinity to any site on a DNA molecule without regard for the sequence or structure of the DNA. Typically, the thermodynamic driving force for forming these complexes is electrost
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::68c507a712f320970e21e0146dcc20d8
https://doi.org/10.1038/npg.els.0001358
https://doi.org/10.1038/npg.els.0001358
Publikováno v:
Biochemistry. 36(5)
The binding of Escherichia coli LexA repressor to the recA operator was examined as a function of the concentration of NaCl, KCl, NaF, and MgCl2 at pH 7.5, 21 degrees C. The effects of pH at 100 mM NaCl were also examined. Changes both in the qualita
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6e88baec9cc641aa0e5b2fbb7bef2cc
https://pubmed.ncbi.nlm.nih.gov/9033397
https://pubmed.ncbi.nlm.nih.gov/9033397
Publikováno v:
Analytical biochemistry. 242(2)
Quantitative zonal DNA affinity chromatography may be used to determine accurate equilibrium constants for the binding of proteins nonspecifically to DNA. Zonal quantitative affinity chromatography has not previously been applied to the determination
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::473ba6f8f76e6d96ba74ab103dc8f663
https://pubmed.ncbi.nlm.nih.gov/8937566
https://pubmed.ncbi.nlm.nih.gov/8937566
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 81(9)
Secondary structure in single-stranded DNA impedes the presynaptic association of recA protein and consequently blocks the formation of joint molecules as evidenced by effects of temperature, nucleotide sequence, and ionic conditions. Escherichia col
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15354aeaba8b2edf300e6dbe9917d1bf
https://pubmed.ncbi.nlm.nih.gov/6326142
https://pubmed.ncbi.nlm.nih.gov/6326142