Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Manfred Schnarr"'
Autor:
Jean-Claude Maurizot, Manfred Schnarr
Publikováno v:
European Journal of Biochemistry. 128:515-520
The secondary structure of the short tryptic headpiece of the lac repressor has been investigated by the analysis of its infrared and circular dichroic spectra. For the latter we used the method of Provencher and Glockner [Biochemistry (1981) 20, 33
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::761ad8e68d9e004cbfeaf704f39ceded
https://doi.org/10.1111/j.1432-1033.1982.tb06995.x
https://doi.org/10.1111/j.1432-1033.1982.tb06995.x
Autor:
Philippe Georgel, Jean-Marc Reichhart, Pascale Oertel-Buchheit, Manfred Schnarr, Isabelle Gross
Publikováno v:
Gene. 228:233-242
The Drosophila transcription factor Dorsal, a member of the Rel/NF-kappaB family of proteins, plays a key role in the establishment of dorsoventral polarity in the early embryo and is also involved in the immune response. Here, we present evidence th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b87f037f8ac99d3364bb520cad4c8aa8
https://doi.org/10.1016/s0378-1119(98)00595-2
https://doi.org/10.1016/s0378-1119(98)00595-2
Publikováno v:
Protein Science. 7:512-515
The LexA protein is part of a large family of prokaryotic transcriptional repressors that contain an amino-terminal DNA binding domain and a carboxy-terminal dimerization domain. These domains are separated by a linker or hinge region, which is gener
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7bd20d4b7e94a980ed2e810ea85ccadc
https://doi.org/10.1002/pro.5560070234
https://doi.org/10.1002/pro.5560070234
Autor:
G Younès-Cauet, Michèle Granger-Schnarr, Pascale Oertel-Buchheit, Dominique Porte, Manfred Schnarr, M Dmitrova
Publikováno v:
Molecular and General Genetics MGG. 257:205-212
Interactions between proteins affect a wide variety of biological processes, such as signal transduction and control of gene expression. In order to facilitate the study of protein-protein interactions we have developed a new method for specifically
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a006028f14255ed61e9a5710dc82b81e
https://doi.org/10.1007/s004380050640
https://doi.org/10.1007/s004380050640
Publikováno v:
Nucleic Acids Research. 25:3026-3033
The mammalian Fos and Fos-related proteins are unable to form homodimers and to bind DNA in the absence of a second protein, like c-Jun for example. In order to study the implications of hydrophobic point mutations in the c-Fox leucine zipper on DNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::137917820302f8f648da2c010cd72c07
https://doi.org/10.1093/nar/25.15.3026
https://doi.org/10.1093/nar/25.15.3026
Publikováno v:
Nucleic Acids Research. 24:4751-4758
cAMP-responsive-element (CRE)-binding factors interaction with nucleosomal DNA has been investigated in vitro on the human c-fos promoter. Analysis of nucleosome reconstitution of this promoter shows a preferential nucleosome positioning on the proxi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65e7a371bd997842e160b5d6c7c68da6
https://doi.org/10.1093/nar/24.23.4751
https://doi.org/10.1093/nar/24.23.4751
Autor:
Rolf Boelens, R. M. A. Knegtel, Rasmus H. Fogh, Heinz Rüterjans, G. Ottleben, Pascal Dumoulin, Manfred Schnarr, Robert Kaptein
Publikováno v:
Proteins: Structure, Function, and Genetics. 21:226-236
A structural model for the interaction of the LexA repressor DNA binding domain (DBD) with operator DNA is derived by means of Monte Carlo docking. Protein–DNA complexes were generated by docking the LexA repressor DBD NMR solution structure onto b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8819fca36f45078b48bd1bdc30eb088
https://doi.org/10.1002/prot.340210305
https://doi.org/10.1002/prot.340210305
Autor:
Florence Larminat, M. Defais, Christophe Cazaux, Neil P. Johnson, Giuseppe Villani, Manfred Schnarr
Publikováno v:
Journal of Biological Chemistry. 269:8246-8254
Escherichia coli RecA protein plays a central role both in DNA repair and in recombination. We report biochemical properties of three new RecA proteins mutated at positions 199 (RecA694), 207 (RecA659), and 211 (RecA611) in the putative DNA binding s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffe358de35ce2e0b90598077960c46c7
https://doi.org/10.1016/s0021-9258(17)37186-7
https://doi.org/10.1016/s0021-9258(17)37186-7
Autor:
Heinz Rüterjans, Rolf Boelens, Manfred Schnarr, Chris Sander, Rasmus H. Fogh, Liisa Holm, Robert Kaptein
Publikováno v:
"Protein Engineering, Design and Selection". 7:1449-1453
Comparison of structures can reveal surprising connections between protein families and provide new insights into the relationship between sequence, structure and function. The solution structure of LexA repressor from Escherichia coli reveals an une
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7c07d046c6741a8c25490e2e83d62e7
https://doi.org/10.1093/protein/7.12.1449
https://doi.org/10.1093/protein/7.12.1449
Publikováno v:
Nucleic Acids Research. 21:2363-2367
The LexA repressor from Escherichia coli induces DNA bending upon interaction with the two overlapping operators which regulate the transcription of the colicin A encoding gene caa. Both caa operators harbor T-tracts adjacent to their recognition mot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb3f3b231c2eb99a88d10c616fae16cd
https://doi.org/10.1093/nar/21.10.2363
https://doi.org/10.1093/nar/21.10.2363