Rolf Boelens
TitelGeciteerd doorJaar
HADDOCK: a protein− protein docking approach based on biochemical or biophysical information
C Dominguez, R Boelens, AMJJ Bonvin
Journal of the American Chemical Society 125 (7), 1731-1737, 2003
21812003
Dynamic readers for 5-(hydroxy) methylcytosine and its oxidized derivatives
CG Spruijt, F Gnerlich, AH Smits, T Pfaffeneder, PWTC Jansen, C Bauer, ...
Cell 152 (5), 1146-1159, 2013
7132013
Solution structure of the glucocorticoid receptor DNA-binding domain
T Hard, E Kellenbach, R Boelens, BA Maler, K Dahlman, LP Freedman, ...
Science 249 (4965), 157-160, 1990
6031990
A protein structure from nuclear magnetic resonance data: lac repressor headpiece
R Kaptein, ERP Zuiderweg, RM Scheek, R Boelens, WF Van Gunsteren
Journal of molecular biology 182 (1), 179-182, 1985
4961985
Structure and flexibility adaptation in nonspecific and specific protein-DNA complexes
CG Kalodimos, N Biris, AMJJ Bonvin, MM Levandoski, M Guennuegues, ...
Science 305 (5682), 386-389, 2004
4952004
Thiol ester-linked p-coumaric acid as a new photoactive prosthetic group in a protein with rhodopsin-like photochemistry
WD Hoff, P Dux, K Hard, B Devreese, IM Nugteren-Roodzant, W Crielaard, ...
Biochemistry 33 (47), 13959-13962, 1994
3031994
Iterative procedure for structure determination from proton-proton NOEs using a full relaxation matrix approach. Application to a DNA octamer
R Boelens, TMG Koning, GA Van der Marel, JH Van Boom, R Kaptein
Journal of Magnetic Resonance (1969) 82 (2), 290-308, 1989
2831989
New insights into the structure and composition of technical lignins: a comparative characterisation study
S Constant, HLJ Wienk, AE Frissen, P de Peinder, R Boelens, DS Van Es, ...
Green Chemistry 18 (9), 2651-2665, 2016
2732016
The DNA-binding domain of HIV-1 integrase has an SH3-like fold
APAM Eijkelenboom, RAP Lutzke, R Boelens, RHA Plasterk, R Kaptein, ...
Nature structural biology 2 (9), 807, 1995
2721995
Sequential resonance assignments in proton NMR spectra of oligonucleotides by two-dimensional NMR spectroscopy
RM Scheek, R Boelens, N Russo, JH Van Boom, R Kaptein
Biochemistry 23 (7), 1371-1376, 1984
2641984
Determination of biomolecular structures from proton-proton NOE's using a relaxation matrix approach
R Boelens, TMG Koning, R Kaptein
Journal of Molecular Structure 173, 299-311, 1988
2551988
Sequential resonance assignments in DNA proton NMR spectra by two-dimensional NOE spectroscopy
RM Scheek, N Russo, R Boelens, R Kaptein, JH Van Boom
Journal of the American Chemical Society 105 (9), 2914-2916, 1983
2491983
Peroxidases
HB Dunford, T Araiso, D Job, J Ricard, R Rutter, LP Hager, R Wever, ...
The Biological Chemistry of Iron, 337-355, 1982
2391982
Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins
FAA Mulder, D Schipper, R Bott, R Boelens
Journal of molecular biology 292 (1), 111-123, 1999
2331999
Protein structures from NMR
R Kaptein, R Boelens, RM Scheek, WF Van Gunsteren
Biochemistry 27 (15), 5389-5395, 1988
2321988
Structure of Arc represser in solution: evidence for a family of β-sheet DMA-binding proteins
JN Breg, JHJ van Opheusden, MJM Burgering, R Boelens, R Kaptein
Nature 346 (6284), 586, 1990
2081990
Data‐driven docking for the study of biomolecular complexes
ADJ Van Dijk, R Boelens, AMJJ Bonvin
The FEBS journal 272 (2), 293-312, 2005
2062005
Structural and dynamic changes of photoactive yellow protein during its photocycle in solution
G Rubinstenn, GW Vuister, FAA Mulder, PE Düx, R Boelens, ...
Nature Structural & Molecular Biology 5 (7), 568, 1998
2021998
Sequential assignment of imino-and amino-proton resonances in 1H NMR spectra of oligonucleotides by two-dimensional NMR spectroscopy. Application to a lac operator fragment
R Boelens, RM Scheek, K Dijkstra, R Kaptein
Journal of Magnetic Resonance (1969) 62 (3), 378-386, 1985
1971985
Identification of a ubiquitin–protein ligase subunit within the CCR4–NOT transcription repressor complex
TK Albert, H Hanzawa, YIA Legtenberg, MJ de Ruwe, ...
The EMBO journal 21 (3), 355-364, 2002
1922002
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