Zobrazeno 1 - 10
of 13
pro vyhledávání: '"R. M. A. Knegtel"'
Autor:
R. Niessen, J. Kroeze, K. Spreeuwenberg, J. J. Kok, R. M. A. Knegtel, S. V. Roosmalen-Vos, A. N. Vermeulen, D. Schaap, C. M. Kuiper, G. Arts, N. V. D. Beek-Verhoeven
Publikováno v:
Parasitology. 128:603-616
AnEimeria acervulinaprotein fraction was identified which conferred partial protection against anE. acervulinachallenge infection. From this fraction a 37 kDa protein was purified and its corresponding cDNA was cloned and shown to encode a lactate de
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
Autor:
Rolf Boelens, Geerten W. Vuister, Robert Kaptein, R. M. A. Knegtel, André Padilla, Gerard J. Kleywegt
Publikováno v:
Journal of Magnetic Resonance, Series B. 102:166-176
Computer-assisted assignment of homonuclear 3D NMR spectra of proteins. Application to Pike Parvalbumin III
Autor:
Robert Kaptein, Maria Luisa Ganadu, R. M. A. Knegtel, A. V. E. George, Rolf Boelens, P.T. Vandersaag
Publikováno v:
Biochemical and Biophysical Research Communications. 192:492-498
The two zinc fingers of the DNA binding domain of the human retinoic acid receptor-β were labelled with 113 Cd. Two- and three-dimensional heteronuclear nuclear magnetic resonance (NMR) experiments show that the first eight conserved cysteine residu
Autor:
Robert Kaptein, Manfred Schnarr, Michèle Granger-Schnarr, Pascal Dumoulin, Richard H. Ebright, R. M. A. Knegtel
Publikováno v:
Biochemistry. 35(14)
The structure of the complex of full-length Escherichia coli LexA repressor with a consensus operator DNA fragment has been probed by affinity photo-cross-linking and affinity cleavage. These methods allow the determination of approximate intermolecu
Autor:
Robert Kaptein, R. M. A. Knegtel, J.A.C. Rullmann, Rolf Boelens, V. P. Chuprina, Monique Slijper
Publikováno v:
NMR as a Structural Tool for Macromolecules ISBN: 9781461380290
An essential step in the regulation of gene expression is the binding of a regulatory protein to a specific DNA sequence in the promotor region of the gene. The understanding of protein-DNA recognition is, therefore, a major theme in structural biolo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::09a0ff5d1795cb803a6411cd01b9d9f3
https://doi.org/10.1007/978-1-4613-0387-9_14
https://doi.org/10.1007/978-1-4613-0387-9_14
Publikováno v:
Interface between Chemistry and Biochemistry ISBN: 9783034898898
This chapter presents an overview of the application of modern NMR methods in structural studies of the DNA binding domains (DBDs) of nuclear hormone receptors. The DBDs studied so far comprise those of the glucocorticoid, estrogen, retinoic acid and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9559824066a6e8e165c11ddcc86798bc
https://doi.org/10.1007/978-3-0348-9061-8_13
https://doi.org/10.1007/978-3-0348-9061-8_13
Monte Carlo docking of protein-DNA complexes: incorporation of DNA flexibility and experimental data
Publikováno v:
Protein engineering. 7(6)
A Monte Carlo simulation program (MONTY) has been developed to dock proteins onto DNA. Protein and DNA interact via square-well potentials for hydrogen bond and van der Waals interactions. The effect of the inclusion of DNA flexibility and experiment
Publikováno v:
Journal of molecular biology. 235(1)
A Monte Carlo method is described for automated docking of proteins on DNA. The simulation program MONTY keeps the entire DNA and the protein backbone and core fixed while protein surface side-chains are allowed to rotate freely. The entire protein i
Autor:
Douglas Eib, Johannes G. Schilthuis, Paul T. van der Saag, Robert Kaptein, Masato Katahira, R. M. A. Knegtel, Rolf Boelens
Publikováno v:
New Developments in Lipid-Protein Interactions and Receptor Function ISBN: 9781461362395
All-trans-retinoic acid (RA), a vitamin A derivative, plays a crucial role in vertebrate development and differentiation (Thaller & Eichele, 1987). Retinoic acid acts through binding to nuclear retinoic acid receptors (RARs). RARs are members of a su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ba2609a43ecc27d17915ecc9a04ba7db
https://doi.org/10.1007/978-1-4615-2860-9_15
https://doi.org/10.1007/978-1-4615-2860-9_15