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pro vyhledávání: '"W Guschlbauer"'
Autor:
W. Guschlbauer
This volume contains the texts of the nineteen lectures presented at the NATO-ASI - FEBS Course on'DNA - ligand interactions: from drugs to proteins.'The Advanced Study Institute (ASIl was held from August 30th to September 11th. 1986 in the Abbey of
Autor:
W. Guschlbauer
Teaching a course on nucleic acid structure is a hazardous undertaking, especially if one has no continuous teaching obligations. I still have done it on several occasions in various French universities, when colleagues, suffering from admin istrat
Autor:
Stéphane Marzabal, Ramon Eritja, Vera Thielking, Stephen DuBois, W. Guschlbauer, Angeles Cano
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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8 pages, 6 figuras, 2 tables.-- PMID: 7478992 [PubMed].-- PMCID: PMC307261.
We have measured steady-state kinetics of the N6-adenine methyltransferase Dam Mtase using as substrates non-selfcomplementary tetradecamer duplexs (d[GCCGGATCTAGACG]-d[
We have measured steady-state kinetics of the N6-adenine methyltransferase Dam Mtase using as substrates non-selfcomplementary tetradecamer duplexs (d[GCCGGATCTAGACG]-d[
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e464764b8a0e569682e13522c2ec2dd1
https://doi.org/10.1093/nar/23.18.3648
https://doi.org/10.1093/nar/23.18.3648
Publikováno v:
Biochemical and Biophysical Research Communications. 198:885-890
The cleavage of a 14 base pair DNA duplex containing one EcoRII recognition site by EcoRII restriction endonuclease (R.EcoRII) was studied in single turnover experiments with varying enzyme concentrations in the micromolar range. The reaction rate in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e44e8080b074b429369a19f637ec6f14
https://doi.org/10.1006/bbrc.1994.1126
https://doi.org/10.1006/bbrc.1994.1126
Publikováno v:
Proceedings of the National Academy of Sciences. 88:6394-6397
Adenine methylation of GATC sequences in DNA is carried out by the DNA adenine methyltransferase with the methyl group source being the cofactor S-adenosylmethionine. We report 3H NMR studies on the interaction of DNA adenine methyltransferase with S
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https://doi.org/10.1073/pnas.88.15.6394
https://doi.org/10.1073/pnas.88.15.6394
Autor:
A. Guy, W. Guschlbauer, J. Gabarro-Arpa, M. Le Bret, Yves Boulard, Robert Teoule, J.A.H. Cognet, G. V. Fazakerley
Publikováno v:
Nucleic Acids Research. 19:5159-5167
We have determined by two-dimensional nuclear magnetic resonance studies and molecular mechanics calculations the three-dimensional solution structure of a 21 residue oligonucleotide capable of forming a hairpin structure with a loop of three thymidi
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https://doi.org/10.1093/nar/19.19.5159
https://doi.org/10.1093/nar/19.19.5159
Publikováno v:
Nucleic Acids Research. 19:1753-1758
Adenine residues in DNA are oxidized under the action of ionizing radiation at the C-8 position to give 7,8-dihydro-8-oxoadenine. The formation of this lesion can be considered a cause of mutations and carcinogenesis. Oligodeoxyribonucleotides 39 and
Externí odkaz:
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https://doi.org/10.1093/nar/19.8.1753
https://doi.org/10.1093/nar/19.8.1753
Publikováno v:
Journal of Molecular Biology. 213:303-314
An abasic site in DNA creates a strong block to DNA polymerase and is a mutagenic base lesion. In this study, we present structural and dynamic properties of duplex oligodeoxynucleotides containing G, C and T opposite a model abasic site studied by o
Externí odkaz:
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https://doi.org/10.1016/s0022-2836(05)80192-5
https://doi.org/10.1016/s0022-2836(05)80192-5
Autor:
W. Guschlbauer
Publikováno v:
Landolt-Börnstein-Group VII Biophysics ISBN: 3540194282
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1daad78c5fd07f630a14dee6676584bb
https://doi.org/10.1007/10361369_10
https://doi.org/10.1007/10361369_10
Autor:
W. Guschlbauer
Publikováno v:
Landolt-Börnstein-Group VII Biophysics ISBN: 3540194282
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d09c967d18e3dda80ed82b6b9d1a3b18
https://doi.org/10.1007/10361369_13
https://doi.org/10.1007/10361369_13