Rolf Boelens - Publications

Affiliations: 
Utrecht University, Utrecht, Netherlands 
Area:
gene regulation, transcription, NMR
Website:
http://profs.library.uu.nl/index.php/profrec/getprofdata/221/9/126/0

315 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2020 Giassa IC, Vavrinská A, Zelinka J, Šebera J, Sychrovský V, Boelens R, Fiala R, Trantírek L. HERMES - A Software Tool for the Prediction and Analysis of Magnetic-Field-Induced Residual Dipolar Couplings in Nucleic Acids. Chempluschem. 85: 2177-2185. PMID 32986260 DOI: 10.1002/Cplu.202000505  0.322
2019 Shahul Hameed D, van Tilburg GBA, Merkx R, Flierman D, Wienk H, El Oualid F, Hofmann K, Boelens R, Ovaa H. Diubiquitin-Based NMR Analysis: Interactions Between Lys6-Linked diUb and UBA Domain of UBXN1. Frontiers in Chemistry. 7: 921. PMID 32039147 DOI: 10.3389/Fchem.2019.00921  0.432
2018 Faridounnia M, Folkers GE, Boelens R. Function and Interactions of ERCC1-XPF in DNA Damage Response. Molecules (Basel, Switzerland). 23. PMID 30563071 DOI: 10.3390/Molecules23123205  0.552
2018 Emendato A, Guerrini R, Marzola E, Wienk H, Boelens R, Leone S, Picone D. Disordered Peptides Looking for Their Native Environment: Structural Basis of CB1 Endocannabinoid Receptor Binding to Pepcans. Frontiers in Molecular Biosciences. 5: 100. PMID 30505835 DOI: 10.3389/Fmolb.2018.00100  0.332
2018 Lancefield CS, Wienk HLJ, Boelens R, Weckhuysen BM, Bruijnincx PCA. Identification of a diagnostic structural motif reveals a new reaction intermediate and condensation pathway in kraft lignin formation. Chemical Science. 9: 6348-6360. PMID 30310563 DOI: 10.1039/C8Sc02000K  0.312
2018 Corbeski I, Dolinar K, Wienk H, Boelens R, van Ingen H. DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surface. Nucleic Acids Research. PMID 29905837 DOI: 10.1093/Nar/Gky507  0.352
2018 Ingen Hv, Corbeski I, Dolinar K, Wienk H, Boelens R. Backbone 1H, 13C, and 15N Chemical Shift Assignments for APLF acidic domain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27186  0.323
2017 Kaptein R, Boelens R, Luchinat C. Nicolaas Bloembergen: a pioneer in magnetic resonance and in maser and laser physics. Journal of Biomolecular Nmr. PMID 29134388 DOI: 10.1007/S10858-017-0143-4  0.561
2016 Das D, Faridounnia M, Kovacic L, Kaptein R, Boelens R, Folkers GE. Single-strand DNA Binding by the Helix-Hairpin-Helix Domain of XPF Contributes to Substrate Specificity of ERCC1-XPF. The Journal of Biological Chemistry. PMID 28028171 DOI: 10.1074/Jbc.M116.747857  0.796
2016 Oliveira LC, Souza DP, Oka GU, Lima FD, Oliveira RJ, Favaro DC, Wienk H, Boelens R, Farah CS, Salinas RK. VirB7 and VirB9 Interactions Are Required for the Assembly and Antibacterial Activity of a Type IV Secretion System. Structure (London, England : 1993). PMID 27594685 DOI: 10.1016/J.Str.2016.07.015  0.32
2016 Dongre R, Folkers GE, Gualerzi CO, Boelens R, Wienk H. A model for the interaction of the G3-subdomain of Geobacillus stearothermophilus IF2 with the 30S ribosomal subunit. Protein Science : a Publication of the Protein Society. PMID 27364543 DOI: 10.1002/Pro.2977  0.563
2016 Dongre R, Folkers G, Gualerzi C, Boelens R, Wienk H. Structure and Dynamics of the Geobacillus stearothermophilus IF2 G3-subdomain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25975  0.519
2015 Vavřinská A, Zelinka J, Šebera J, Sychrovský V, Fiala R, Boelens R, Sklenář V, Trantírek L. Impact of nucleic acid self-alignment in a strong magnetic field on the interpretation of indirect spin-spin interactions. Journal of Biomolecular Nmr. PMID 26685997 DOI: 10.1007/S10858-015-0005-X  0.307
2015 Nieto L, Tharun IM, Balk M, Wienk H, Boelens R, Ottmann C, Milroy LG, Brunsveld L. Estrogen Receptor Folding Modulates cSrc Kinase SH2 Interaction via a Helical Binding Mode. Acs Chemical Biology. PMID 26352092 DOI: 10.1021/Acschembio.5B00568  0.393
2015 Faridounnia M, Wienk H, Kovačič L, Folkers GE, Jaspers NG, Kaptein R, Hoeijmakers JH, Boelens R. The Cerebro-oculo-facio-skeletal Syndrome Point Mutation F231L in the ERCC1 DNA Repair Protein Causes Dissociation of the ERCC1-XPF Complex. The Journal of Biological Chemistry. 290: 20541-55. PMID 26085086 DOI: 10.1074/Jbc.M114.635169  0.716
2015 Sinnige T, Weingarth M, Daniëls M, Boelens R, Bonvin AM, Houben K, Baldus M. Conformational Plasticity of the POTRA 5 Domain in the Outer Membrane Protein Assembly Factor BamA. Structure (London, England : 1993). PMID 26027731 DOI: 10.1016/J.Str.2015.04.014  0.714
2015 Sinnige T, Houben K, Pritisanac I, Renault M, Boelens R, Baldus M. Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach. Journal of Biomolecular Nmr. 61: 321-32. PMID 25567766 DOI: 10.1007/S10858-014-9891-6  0.396
2015 Oliveira L, Souza D, Salinas R, Wienk H, Boelens R, Farah S. NMR structure of VirB9 C-terminal domain in complex with VirB7 N-terminal domain from Xanthomonas citri's T4SS. Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2N01/Pdb  0.36
2014 Ferguson FM, Dias DM, Rodrigues JP, Wienk H, Boelens R, Bonvin AM, Abell C, Ciulli A. Binding hotspots of BAZ2B bromodomain: Histone interaction revealed by solution NMR driven docking. Biochemistry. 53: 6706-16. PMID 25266743 DOI: 10.1021/Bi500909D  0.773
2014 Tuppo L, Spadaccini R, Alessandri C, Wienk H, Boelens R, Giangrieco I, Tamburrini M, Mari A, Picone D, Ciardiello MA. Structure, stability, and IgE binding of the peach allergen Peamaclein (Pru p 7). Biopolymers. 102: 416-25. PMID 25130872 DOI: 10.1002/Bip.22530  0.402
2014 Khan F, Daniëls MA, Folkers GE, Boelens R, Saqlan Naqvi SM, van Ingen H. Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA-binding protein: implications for its RNA chaperone function. Nucleic Acids Research. 42: 8705-18. PMID 24957607 DOI: 10.1093/Nar/Gku468  0.588
2014 Scheepstra M, Nieto L, Hirsch AK, Fuchs S, Leysen S, Lam CV, in het Panhuis L, van Boeckel CA, Wienk H, Boelens R, Ottmann C, Milroy LG, Brunsveld L. A natural-product switch for a dynamic protein interface. Angewandte Chemie (International Ed. in English). 53: 6443-8. PMID 24821627 DOI: 10.1002/Anie.201403773  0.325
2014 Kastritis PL, Rodrigues JP, Folkers GE, Boelens R, Bonvin AM. Proteins feel more than they see: fine-tuning of binding affinity by properties of the non-interacting surface. Journal of Molecular Biology. 426: 2632-52. PMID 24768922 DOI: 10.1016/J.Jmb.2014.04.017  0.801
2014 Spadaccini R, Ercole C, Graziano G, Wechselberger R, Boelens R, Picone D. Mechanism of 3D domain swapping in bovine seminal ribonuclease. The Febs Journal. 281: 842-50. PMID 24616921 DOI: 10.1111/Febs.12651  0.434
2014 Karagöz GE, Duarte AM, Akoury E, Ippel H, Biernat J, Morán Luengo T, Radli M, Didenko T, Nordhues BA, Veprintsev DB, Dickey CA, Mandelkow E, Zweckstetter M, Boelens R, Madl T, et al. Hsp90-Tau complex reveals molecular basis for specificity in chaperone action. Cell. 156: 963-74. PMID 24581495 DOI: 10.1016/J.Cell.2014.01.037  0.314
2014 Popovic M, Wienk H, Coglievina M, Boelens R, Pongor S, Pintar A. The basic helix-loop-helix region of the transcriptional repressor hairy and enhancer of split 1 is preorganized to bind DNA. Proteins. 82: 537-45. PMID 24403087 DOI: 10.1002/Prot.24507  0.413
2014 Sinnige T, Houben K, Weingarth M, Baker L, Boelens R, Baldus M. Protein Plasticity and Protein-Lipid Interactions of the Beta-Barrel Assembly Machinery Biophysical Journal. 106: 47a. DOI: 10.1016/J.Bpj.2013.11.339  0.346
2014 Weiss J, Wienk H, Boelens R, Laschewsky A. Block copolymer micelles with an intermediate star-/flower-like structure studied by 1H NMR relaxometry Macromolecular Chemistry and Physics. 215: 915-919. DOI: 10.1002/Macp.201300753  0.323
2013 Wienk H, Slootweg JC, Speerstra S, Kaptein R, Boelens R, Folkers GE. The Fanconi anemia associated protein FAAP24 uses two substrate specific binding surfaces for DNA recognition. Nucleic Acids Research. 41: 6739-49. PMID 23661679 DOI: 10.1093/Nar/Gkt354  0.743
2013 van Nuland R, van Schaik FM, Simonis M, van Heesch S, Cuppen E, Boelens R, Timmers HM, van Ingen H. Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain. Epigenetics & Chromatin. 6: 12. PMID 23656834 DOI: 10.1186/1756-8935-6-12  0.378
2013 da Silva Almeida AC, Hocking HG, Boelens R, Strous GJ, van Rossum AG. βTrCP interacts with the ubiquitin-dependent endocytosis motif of the GH receptor in an unconventional manner. The Biochemical Journal. 453: 291-301. PMID 23607312 DOI: 10.1042/Bj20121843  0.319
2013 Loth K, Gnida M, Romanuka J, Kaptein R, Boelens R. Sliding and target location of DNA-binding proteins: an NMR view of the lac repressor system. Journal of Biomolecular Nmr. 56: 41-9. PMID 23568265 DOI: 10.1007/S10858-013-9723-0  0.662
2013 Spruijt CG, Gnerlich F, Smits AH, Pfaffeneder T, Jansen PW, Bauer C, Münzel M, Wagner M, Müller M, Khan F, Eberl HC, Mensinga A, Brinkman AB, Lephikov K, Müller U, ... ... Boelens R, et al. Dynamic readers for 5-(hydroxy)methylcytosine and its oxidized derivatives. Cell. 152: 1146-59. PMID 23434322 DOI: 10.1016/J.Cell.2013.02.004  0.326
2013 Koharudin LM, Boelens R, Kaptein R, Gronenborn AM. A NMR guided approach for CsrA-RNA crystallization. Journal of Biomolecular Nmr. 56: 31-9. PMID 23359257 DOI: 10.1007/S10858-013-9712-3  0.662
2013 Emmer J, Vavrinská A, Sychrovský V, Benda L, Kříž Z, Koča J, Boelens R, Sklenář V, Trantírek L. Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic ¹⁵N chemical shielding anisotropy tensors. Journal of Biomolecular Nmr. 55: 59-70. PMID 23202985 DOI: 10.1007/S10858-012-9686-6  0.314
2013 Augustyniak W, Wienk H, Boelens R, Reetz MT. 1H, 13C and 15N resonance assignments of wild-type Bacillus subtilis Lipase A and its mutant evolved towards thermostability Biomolecular Nmr Assignments. 7: 249-252. PMID 22996591 DOI: 10.1007/S12104-012-9420-Z  0.355
2012 Hospes M, Ippel JH, Boelens R, Hellingwerf KJ, Hendriks J. Binding of hydrogen-citrate to photoactive yellow protein is affected by the structural changes related to signaling state formation. The Journal of Physical Chemistry. B. 116: 13172-82. PMID 23078029 DOI: 10.1021/Jp306891S  0.323
2012 Markley JL, Akutsu H, Asakura T, Baldus M, Boelens R, Bonvin A, Kaptein R, Bax A, Bezsonova I, Gryk MR, Hoch JC, Korzhnev DM, Maciejewski MW, Case D, Chazin WJ, et al. In support of the BMRB. Nature Structural & Molecular Biology. 19: 854-60. PMID 22955930 DOI: 10.1038/Nsmb.2371  0.742
2012 Das D, Folkers GE, van Dijk M, Jaspers NG, Hoeijmakers JH, Kaptein R, Boelens R. The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix- hairpin-helix domains in ss/ds DNA recognition. Structure (London, England : 1993). 20: 667-75. PMID 22483113 DOI: 10.1016/J.Str.2012.02.009  0.815
2012 Li Y, Karagöz GE, Seo YH, Zhang T, Jiang Y, Yu Y, Duarte AM, Schwartz SJ, Boelens R, Carroll K, Rüdiger SG, Sun D. Sulforaphane inhibits pancreatic cancer through disrupting Hsp90-p50(Cdc37) complex and direct interactions with amino acids residues of Hsp90. The Journal of Nutritional Biochemistry. 23: 1617-26. PMID 22444872 DOI: 10.1016/J.Jnutbio.2011.11.004  0.332
2012 Wienk H, Tishchenko E, Belardinelli R, Tomaselli S, Dongre R, Spurio R, Folkers GE, Gualerzi CO, Boelens R. Structural dynamics of bacterial translation initiation factor IF2. The Journal of Biological Chemistry. 287: 10922-32. PMID 22308033 DOI: 10.1074/Jbc.M111.333393  0.577
2012 Augustyniak W, Brzezinska AA, Pijning T, Wienk H, Boelens R, Dijkstra BW, Reetz MT. Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: Factors contributing to increased activity retention Protein Science. 21: 487-497. PMID 22267088 DOI: 10.1002/Pro.2031  0.309
2012 Spadaccini R, Ercole C, Gentile MA, Sanfelice D, Boelens R, Wechselberger R, Batta G, Bernini A, Niccolai N, Picone D. NMR studies on structure and dynamics of the monomeric derivative of BS-RNase: new insights for 3D domain swapping. Plos One. 7: e29076. PMID 22253705 DOI: 10.1371/Journal.Pone.0029076  0.455
2012 Favreau P, Benoit E, Hocking HG, Carlier L, D' hoedt D, Leipold E, Markgraf R, Schlumberger S, Córdova MA, Gaertner H, Paolini-Bertrand M, Hartley O, Tytgat J, Heinemann SH, Bertrand D, ... Boelens R, et al. A novel µ-conopeptide, CnIIIC, exerts potent and preferential inhibition of NaV1.2/1.4 channels and blocks neuronal nicotinic acetylcholine receptors. British Journal of Pharmacology. 166: 1654-68. PMID 22229737 DOI: 10.1111/J.1476-5381.2012.01837.X  0.69
2012 Wassenaar TA, van Dijk M, Loureiro-Ferreira N, van der Schot G, de Vries SJ, Schmitz C, van der Zwan J, Boelens R, Giachetti A, Ferella L, Rosato A, Bertini I, Herrmann T, Jonker HRA, Bagaria A, et al. WeNMR: Structural Biology on the Grid Journal of Grid Computing. 10: 743-767. DOI: 10.1007/s10723-012-9246-z  0.783
2012 Boelens R, Kaptein R. ChemInform Abstract: Homonuclear 3D NMR of Biomolecules Cheminform. 43: no-no. DOI: 10.1002/chin.201236269  0.579
2011 Peters F, Maestre-Martinez M, Leonov A, Kovačič L, Becker S, Boelens R, Griesinger C. Cys-Ph-TAHA: a lanthanide binding tag for RDC and PCS enhanced protein NMR. Journal of Biomolecular Nmr. 51: 329-37. PMID 21892794 DOI: 10.1007/S10858-011-9560-Y  0.403
2011 Stratmann D, Boelens R, Bonvin AM. Quantitative use of chemical shifts for the modeling of protein complexes. Proteins. 79: 2662-70. PMID 21744392 DOI: 10.1002/Prot.23090  0.712
2011 Berger I, Blanco AG, Boelens R, Cavarelli J, Coll M, Folkers GE, Nie Y, Pogenberg V, Schultz P, Wilmanns M, Moras D, Poterszman A. Structural insights into transcription complexes. Journal of Structural Biology. 175: 135-46. PMID 21571073 DOI: 10.1016/J.Jsb.2011.04.015  0.577
2011 Huang A, Hibbert RG, de Jong RN, Das D, Sixma TK, Boelens R. Symmetry and asymmetry of the RING-RING dimer of Rad18. Journal of Molecular Biology. 410: 424-35. PMID 21549715 DOI: 10.1016/J.Jmb.2011.04.051  0.597
2011 Koehler C, Carlier L, Veggi D, Balducci E, Di Marcello F, Ferrer-Navarro M, Pizza M, Daura X, Soriani M, Boelens R, Bonvin AM. Structural and biochemical characterization of NarE, an iron-containing ADP-ribosyltransferase from Neisseria meningitidis. The Journal of Biological Chemistry. 286: 14842-51. PMID 21367854 DOI: 10.1074/Jbc.M110.193623  0.802
2011 Neumoin A, Leonchiks A, Petit P, Vuillard L, Pizza M, Soriani M, Boelens R, Bonvin AM. 1H, 13C and 15N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis. Biomolecular Nmr Assignments. 5: 135-8. PMID 21188561 DOI: 10.1007/S12104-010-9285-Y  0.684
2011 Karagöz GE, Duarte AM, Ippel H, Uetrecht C, Sinnige T, van Rosmalen M, Hausmann J, Heck AJ, Boelens R, Rüdiger SG. N-terminal domain of human Hsp90 triggers binding to the cochaperone p23. Proceedings of the National Academy of Sciences of the United States of America. 108: 580-5. PMID 21183720 DOI: 10.1073/Pnas.1011867108  0.367
2011 Didenko T, Boelens R, Rüdiger SG. 3D DOSY-TROSY to determine the translational diffusion coefficient of large protein complexes. Protein Engineering, Design & Selection : Peds. 24: 99-103. PMID 21062757 DOI: 10.1093/Protein/Gzq091  0.358
2011 Carlier L, Koehler C, Veggi D, Pizza M, Soriani M, Boelens R, Bonvin AM. NMR resonance assignments of NarE, a putative ADP-ribosylating toxin from Neisseria meningitidis. Biomolecular Nmr Assignments. 5: 35-8. PMID 20737254 DOI: 10.1007/S12104-010-9261-6  0.805
2011 Huang A, Hibbert RG, deJong RN, Das D, Sixma TK, Boelens R. Solution structure of human ubiquitin conjugating enzyme Rad6b Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr17443  0.582
2010 Huang A, de Jong RN, Folkers GE, Boelens R. NMR characterization of foldedness for the production of E3 RING domains. Journal of Structural Biology. 172: 120-7. PMID 20682345 DOI: 10.1016/J.Jsb.2010.07.014  0.588
2010 Krzeminski M, Loth K, Boelens R, Bonvin AM. SAMPLEX: automatic mapping of perturbed and unperturbed regions of proteins and complexes. Bmc Bioinformatics. 11: 51. PMID 20102599 DOI: 10.1186/1471-2105-11-51  0.815
2010 Brondijk TH, de Ruiter T, Ballering J, Wienk H, Lebbink RJ, van Ingen H, Boelens R, Farndale RW, Meyaard L, Huizinga EG. Crystal structure and collagen-binding site of immune inhibitory receptor LAIR-1: unexpected implications for collagen binding by platelet receptor GPVI. Blood. 115: 1364-73. PMID 20007810 DOI: 10.1182/Blood-2009-10-246322  0.33
2010 Hibbert RG, Knipscheer P, Huang A, Boelens R, Buchwald G, Mattiroli F, Sixma TK. Protein interactions regulate ubiquitin and SUMO conjugation Acta Crystallographica Section a Foundations of Crystallography. 66: s2-s2. DOI: 10.1107/S0108767310099988  0.301
2010 Kellenbach ER, van den Elst H, Boelens R, van der Marel GA, van Boom JH, Kaptein R. A convenient synthesis of DNA fragments nitrogen-15 labeled at the exocyclic cytosine amino group Recueil Des Travaux Chimiques Des Pays-Bas. 110: 387-388. DOI: 10.1002/Recl.19911100907  0.604
2010 Nusselder JJH, Engberts JBFN, Boelens R, Kaptein R. Micellar structure studied by 2D-NMR Recueil Des Travaux Chimiques Des Pays-Bas. 107: 105-107. DOI: 10.1002/Recl.19881070210  0.623
2009 Sette M, Spurio R, Trotta E, Brandizi C, Brandi A, Pon CL, Barbato G, Boelens R, Gualerzi CO. Sequence-specific recognition of DNA by the C-terminal domain of nucleoid-associated protein H-NS. The Journal of Biological Chemistry. 284: 30453-62. PMID 19740756 DOI: 10.1074/Jbc.M109.044313  0.365
2009 van Wijk SJ, de Vries SJ, Kemmeren P, Huang A, Boelens R, Bonvin AM, Timmers HT. A comprehensive framework of E2-RING E3 interactions of the human ubiquitin-proteasome system. Molecular Systems Biology. 5: 295. PMID 19690564 DOI: 10.1038/Msb.2009.55  0.708
2009 Romanuka J, van den Bulke H, Kaptein R, Boelens R, Folkers GE. Novel strategies to overcome expression problems encountered with toxic proteins: application to the production of Lac repressor proteins for NMR studies. Protein Expression and Purification. 67: 104-12. PMID 19460439 DOI: 10.1016/J.Pep.2009.05.008  0.722
2009 Romanuka J, Folkers GE, Biris N, Tishchenko E, Wienk H, Bonvin AM, Kaptein R, Boelens R. Specificity and affinity of Lac repressor for the auxiliary operators O2 and O3 are explained by the structures of their protein-DNA complexes. Journal of Molecular Biology. 390: 478-89. PMID 19450607 DOI: 10.1016/J.Jmb.2009.05.022  0.792
2009 Krzeminski M, Fuentes G, Boelens R, Bonvin AM. MINOES: a new approach to select a representative ensemble of structures in NMR studies of (partially) unfolded states. Application to Delta25-PYP. Proteins. 74: 895-904. PMID 18704926 DOI: 10.1002/Prot.22197  0.806
2008 Codutti L, van Ingen H, Vascotto C, Fogolari F, Corazza A, Tell G, Quadrifoglio F, Viglino P, Boelens R, Esposito G. The solution structure of DNA-free Pax-8 paired box domain accounts for redox regulation of transcriptional activity in the pax protein family. The Journal of Biological Chemistry. 283: 33321-8. PMID 18829450 DOI: 10.1074/Jbc.M805717200  0.421
2008 van Ingen H, van Schaik FM, Wienk H, Ballering J, Rehmann H, Dechesne AC, Kruijzer JA, Liskamp RM, Timmers HT, Boelens R. Structural insight into the recognition of the H3K4me3 mark by the TFIID subunit TAF3. Structure (London, England : 1993). 16: 1245-56. PMID 18682226 DOI: 10.1016/J.Str.2008.04.015  0.382
2008 Harper SM, Wienk H, Wechselberger RW, Bos JL, Boelens R, Rehmann H. Structural dynamics in the activation of Epac. The Journal of Biological Chemistry. 283: 6501-8. PMID 18167352 DOI: 10.1074/Jbc.M707849200  0.383
2008 Das D, Tripsianes K, Jaspers NG, Hoeijmakers JH, Kaptein R, Boelens R, Folkers GE. The HhH domain of the human DNA repair protein XPF forms stable homodimers. Proteins. 70: 1551-63. PMID 17912758 DOI: 10.1002/Prot.21635  0.803
2008 Codutti L, Esposito G, Corazza A, Fogolari F, Tell G, Vascotto C, Ingen Hv, Boelens R, Viglino P, Quadrifoglio F. Solution structure of Human Pax8 Paired Box Domain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2K27/Pdb  0.331
2008 Ingen Hv, Schaik Fv, Wienk H, Timmers M, Boelens R. Solution structure of the TAF3 PHD domain in complex with a H3K4me3 peptide Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2K17/Pdb  0.322
2007 Tripsianes K, Folkers GE, Zheng C, Das D, Grinstead JS, Kaptein R, Boelens R. Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization. Nucleic Acids Research. 35: 5789-98. PMID 17720715 DOI: 10.1093/Nar/Gkm503  0.813
2007 Gauden M, Grinstead JS, Laan W, van Stokkum IH, Avila-Perez M, Toh KC, Boelens R, Kaptein R, van Grondelle R, Hellingwerf KJ, Kennis JT. On the role of aromatic side chains in the photoactivation of BLUF domains. Biochemistry. 46: 7405-15. PMID 17542622 DOI: 10.1021/Bi7006433  0.787
2007 van Dijk AD, Ciofi-Baffoni S, Banci L, Bertini I, Boelens R, Bonvin AM. Modeling protein-protein complexes involved in the cytochrome C oxidase copper-delivery pathway. Journal of Proteome Research. 6: 1530-9. PMID 17338559 DOI: 10.1021/Pr060651F  0.695
2007 Monti MC, Hernández-Arriaga AM, Kamphuis MB, López-Villarejo J, Heck AJ, Boelens R, Díaz-Orejas R, van den Heuvel RH. Interactions of Kid-Kis toxin-antitoxin complexes with the parD operator-promoter region of plasmid R1 are piloted by the Kis antitoxin and tuned by the stoichiometry of Kid-Kis oligomers. Nucleic Acids Research. 35: 1737-49. PMID 17317682 DOI: 10.1093/Nar/Gkm073  0.348
2007 Kamphuis MB, Monti MC, van den Heuvel RH, López-Villarejo J, Díaz-Orejas R, Boelens R. Structure and function of bacterial kid-kis and related toxin-antitoxin systems. Protein and Peptide Letters. 14: 113-24. PMID 17305597 DOI: 10.2174/092986607779816096  0.331
2007 Kamphuis MB, Monti MC, van den Heuvel RH, Santos-Sierra S, Folkers GE, Lemonnier M, Díaz-Orejas R, Heck AJ, Boelens R. Interactions between the toxin Kid of the bacterial parD system and the antitoxins Kis and MazE. Proteins. 67: 219-31. PMID 17206710 DOI: 10.1002/Prot.21254  0.597
2007 Tripsianes K, Folkers G, Zheng C, Das D, Grinstead J, Kaptein R, Boelens R. Solution structure of the ERCC1 central domain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Jpd/Pdb  0.793
2006 Grinstead JS, Avila-Perez M, Hellingwerf KJ, Boelens R, Kaptein R. Light-induced flipping of a conserved glutamine sidechain and its orientation in the AppA BLUF domain. Journal of the American Chemical Society. 128: 15066-7. PMID 17117839 DOI: 10.1021/Ja0660103  0.79
2006 Milon P, Tischenko E, Tomsic J, Caserta E, Folkers G, La Teana A, Rodnina MV, Pon CL, Boelens R, Gualerzi CO. The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor. Proceedings of the National Academy of Sciences of the United States of America. 103: 13962-7. PMID 16968770 DOI: 10.1073/Pnas.0606384103  0.544
2006 Tomaselli S, Crescenzi O, Sanfelice D, Ab E, Wechselberger R, Angeli S, Scaloni A, Boelens R, Tancredi T, Pelosi P, Picone D. Solution structure of a chemosensory protein from the desert locust Schistocerca gregaria. Biochemistry. 45: 10606-13. PMID 16939212 DOI: 10.1021/Bi060998W  0.435
2006 Sibille N, Favier A, Azuaga AI, Ganshaw G, Bott R, Bonvin AM, Boelens R, van Nuland NA. Comparative NMR study on the impact of point mutations on protein stability of Pseudomonas mendocina lipase. Protein Science : a Publication of the Protein Society. 15: 1915-27. PMID 16823035 DOI: 10.1110/Ps.062213706  0.697
2006 van Dijk M, van Dijk AD, Hsu V, Boelens R, Bonvin AM. Information-driven protein-DNA docking using HADDOCK: it is a matter of flexibility. Nucleic Acids Research. 34: 3317-25. PMID 16820531 DOI: 10.1093/Nar/Gkl412  0.721
2006 AB E, Pugh DJ, Kaptein R, Boelens R, Bonvin AM. Direct use of unassigned resonances in NMR structure calculations with proxy residues. Journal of the American Chemical Society. 128: 7566-71. PMID 16756312 DOI: 10.1021/Ja058504Q  0.791
2006 Salinas RK, Diercks T, Kaptein R, Boelens R. Cooperative alpha-helix unfolding in a protein-DNA complex from hydrogen-deuterium exchange. Protein Science : a Publication of the Protein Society. 15: 1752-9. PMID 16751603 DOI: 10.1110/Ps.051938006  0.671
2006 van Dijk AD, Kaptein R, Boelens R, Bonvin AM. Combining NMR relaxation with chemical shift perturbation data to drive protein-protein docking. Journal of Biomolecular Nmr. 34: 237-44. PMID 16645814 DOI: 10.1007/S10858-006-0024-8  0.782
2006 Jonker HR, Wechselberger RW, Boelens R, Kaptein R, Folkers GE. The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions. Biochemistry. 45: 5067-81. PMID 16605275 DOI: 10.1021/Bi052531B  0.756
2006 Kamphuis MB, Bonvin AM, Monti MC, Lemonnier M, Muñoz-Gómez A, van den Heuvel RH, Díaz-Orejas R, Boelens R. Model for RNA binding and the catalytic site of the RNase Kid of the bacterial parD toxin-antitoxin system. Journal of Molecular Biology. 357: 115-26. PMID 16413033 DOI: 10.1016/J.Jmb.2005.12.033  0.691
2006 Grinstead JS, Hsu ST, Laan W, Bonvin AM, Hellingwerf KJ, Boelens R, Kaptein R. The solution structure of the AppA BLUF domain: insight into the mechanism of light-induced signaling. Chembiochem : a European Journal of Chemical Biology. 7: 187-93. PMID 16323221 DOI: 10.1002/Cbic.200500270  0.796
2006 Wienk H, Tomaselli S, Spurio R, Gualerzi C, Boelens R. dynamics within the fMet-tRNA binding domain of translation initiation factor IF2 from Bacillus stearothermophilus Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr7088  0.309
2005 Tripsianes K, Folkers G, Ab E, Das D, Odijk H, Jaspers NG, Hoeijmakers JH, Kaptein R, Boelens R. The structure of the human ERCC1/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair. Structure (London, England : 1993). 13: 1849-58. PMID 16338413 DOI: 10.1016/J.Str.2005.08.014  0.804
2005 Fuentes G, Nederveen AJ, Kaptein R, Boelens R, Bonvin AM. Describing partially unfolded states of proteins from sparse NMR data. Journal of Biomolecular Nmr. 33: 175-86. PMID 16331422 DOI: 10.1007/S10858-005-3207-9  0.805
2005 Bonvin AM, Boelens R, Kaptein R. NMR analysis of protein interactions. Current Opinion in Chemical Biology. 9: 501-8. PMID 16122968 DOI: 10.1016/J.Cbpa.2005.08.011  0.803
2005 Kopke Salinas R, Folkers GE, Bonvin AM, Das D, Boelens R, Kaptein R. Altered specificity in DNA binding by the lac repressor: a mutant lac headpiece that mimics the gal repressor. Chembiochem : a European Journal of Chemical Biology. 6: 1628-37. PMID 16094693 DOI: 10.1002/Cbic.200500049  0.81
2005 Wienk H, Tomaselli S, Bernard C, Spurio R, Picone D, Gualerzi CO, Boelens R. Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2. Protein Science : a Publication of the Protein Society. 14: 2461-8. PMID 16081655 DOI: 10.1110/Ps.051531305  0.413
2005 Bernard C, Houben K, Derix NM, Marks D, van der Horst MA, Hellingwerf KJ, Boelens R, Kaptein R, van Nuland NA. The solution structure of a transient photoreceptor intermediate: Delta25 photoactive yellow protein. Structure (London, England : 1993). 13: 953-62. PMID 16004868 DOI: 10.1016/J.Str.2005.04.017  0.678
2005 Houben K, Wasielewski E, Dominguez C, Kellenberger E, Atkinson RA, Timmers HT, Kieffer B, Boelens R. Dynamics and metal exchange properties of C4C4 RING domains from CNOT4 and the p44 subunit of TFIIH. Journal of Molecular Biology. 349: 621-37. PMID 15890366 DOI: 10.1016/J.Jmb.2005.04.007  0.798
2005 Kellenberger E, Dominguez C, Fribourg S, Wasielewski E, Moras D, Poterszman A, Boelens R, Kieffer B. Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions. The Journal of Biological Chemistry. 280: 20785-92. PMID 15790571 DOI: 10.1074/Jbc.M412999200  0.81
2005 van Dijk AD, Boelens R, Bonvin AM. Data-driven docking for the study of biomolecular complexes. The Febs Journal. 272: 293-312. PMID 15654870 DOI: 10.1111/J.1742-4658.2004.04473.X  0.702
2005 Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. Structural properties of the promiscuous VP16 activation domain. Biochemistry. 44: 827-39. PMID 15654739 DOI: 10.1021/Bi0482912  0.733
2005 Bernard C, Houben K, Derix N, Marks D, Horst Mvd, Hellingwerf K, Boelens R, Kaptein R, Nuland Nv. Chemical Shift assignment of the blue shifted inetrmediate state of Delta25-PYP Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr6322  0.597
2005 Bernard C, Houben K, Derix N, Horst Mvd, Hellingwerf K, Boelens R, Kaptein R, Nuland Nv. Chemical Shift assignment of the Ground-State of Delta25-PYP Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr6321  0.586
2004 Houben K, Dominguez C, van Schaik FM, Timmers HT, Bonvin AM, Boelens R. Solution structure of the ubiquitin-conjugating enzyme UbcH5B. Journal of Molecular Biology. 344: 513-26. PMID 15522302 DOI: 10.1016/J.Jmb.2004.09.054  0.8
2004 Kalodimos CG, Boelens R, Kaptein R. Toward an integrated model of protein-DNA recognition as inferred from NMR studies on the Lac repressor system. Chemical Reviews. 104: 3567-86. PMID 15303828 DOI: 10.1021/Cr0304065  0.806
2004 Kalodimos CG, Biris N, Bonvin AM, Levandoski MM, Guennuegues M, Boelens R, Kaptein R. Structure and flexibility adaptation in nonspecific and specific protein-DNA complexes. Science (New York, N.Y.). 305: 386-9. PMID 15256668 DOI: 10.1126/Science.1097064  0.815
2004 Durney MA, Wechselberger RW, Kalodimos CG, Kaptein R, Vorgias CE, Boelens R. An alternate conformation of the hyperthermostable HU protein from Thermotoga maritima has unexpectedly high flexibility. Febs Letters. 563: 49-54. PMID 15063721 DOI: 10.1016/S0014-5793(04)00247-9  0.822
2004 Dominguez C, Bonvin AM, Winkler GS, van Schaik FM, Timmers HT, Boelens R. Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches. Structure (London, England : 1993). 12: 633-44. PMID 15062086 DOI: 10.1016/J.Str.2004.03.004  0.825
2004 Winkler GS, Albert TK, Dominguez C, Legtenberg YI, Boelens R, Timmers HT. An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair. Journal of Molecular Biology. 337: 157-65. PMID 15001359 DOI: 10.1016/J.Jmb.2004.01.031  0.79
2004 Kalodimos CG, Bonvin AMJJ, Boelens R, Kaptein R. Solution structure of a dimeric lactose DNA-binding domain complexed to a nonspecific DNA sequence Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb1Osl/Pdb  0.812
2003 Derix NM, Wechselberger RW, van der Horst MA, Hellingwerf KJ, Boelens R, Kaptein R, van Nuland NA. Lack of negative charge in the E46Q mutant of photoactive yellow protein prevents partial unfolding of the blue-shifted intermediate. Biochemistry. 42: 14501-6. PMID 14661962 DOI: 10.1021/Bi034877X  0.652
2003 Koharudin LM, Bonvin AM, Kaptein R, Boelens R. Use of very long-distance NOEs in a fully deuterated protein: an approach for rapid protein fold determination. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 163: 228-35. PMID 12914838 DOI: 10.1016/S1090-7807(03)00149-6  0.795
2003 Dominguez C, Boelens R, Bonvin AM. HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. Journal of the American Chemical Society. 125: 1731-7. PMID 12580598 DOI: 10.1021/Ja026939X  0.814
2003 Feiters MC, Eijkelenboom AP, Nolting HF, Krebs B, van den Ent FM, Plasterk RH, Kaptein R, Boelens R. X-ray absorption spectroscopic studies of zinc in the N-terminal domain of HIV-2 integrase and model compounds. Journal of Synchrotron Radiation. 10: 86-95. PMID 12511797 DOI: 10.1107/S0909049502016205  0.643
2002 Singh S, Folkers GE, Bonvin AM, Boelens R, Wechselberger R, Niztayev A, Kaptein R. Solution structure and DNA-binding properties of the C-terminal domain of UvrC from E.coli. The Embo Journal. 21: 6257-66. PMID 12426397 DOI: 10.1093/Emboj/Cdf627  0.829
2002 Hargreaves D, Santos-Sierra S, Giraldo R, Sabariegos-Jareño R, de la Cueva-Méndez G, Boelens R, Díaz-Orejas R, Rafferty JB. Structural and functional analysis of the kid toxin protein from E. coli plasmid R1. Structure (London, England : 1993). 10: 1425-33. PMID 12377128 DOI: 10.1016/S0969-2126(02)00856-0  0.379
2002 Boelens R, Gualerzi CO. Structure and function of bacterial initiation factors. Current Protein & Peptide Science. 3: 107-19. PMID 12370015 DOI: 10.2174/1389203023380765  0.317
2002 Kalodimos CG, Bonvin AM, Salinas RK, Wechselberger R, Boelens R, Kaptein R. Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain. The Embo Journal. 21: 2866-76. PMID 12065400 DOI: 10.1093/Emboj/Cdf318  0.812
2002 Kalodimos CG, Boelens R, Kaptein R. A residue-specific view of the association and dissociation pathway in protein--DNA recognition. Nature Structural Biology. 9: 193-7. PMID 11850636 DOI: 10.1038/Nsb763  0.82
2002 Albert TK, Hanzawa H, Legtenberg YI, de Ruwe MJ, van den Heuvel FA, Collart MA, Boelens R, Timmers HT. Identification of a ubiquitin-protein ligase subunit within the CCR4-NOT transcription repressor complex. The Embo Journal. 21: 355-64. PMID 11823428 DOI: 10.1093/Emboj/21.3.355  0.332
2002 Hargreaves D, Giraldo R, Santos-Sierra S, Boelens R, Rice DW, Díaz Orejas R, Rafferty JB. Crystallization and preliminary X-ray crystallographic studies on the parD-encoded protein Kid from Escherichia coli plasmid R1. Acta Crystallographica. Section D, Biological Crystallography. 58: 355-8. PMID 11807276 DOI: 10.1107/S0907444901020753  0.348
2002 Kalodimos C, Bonvin A, Salinas R, Wechselberger R, Boelens R, Kaptein R. Assignment of lac repressor headpiece complexed of its natural operator Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr5345  0.77
2001 Bonvin AM, Houben K, Guenneugues M, Kaptein R, Boelens R. Rapid protein fold determination using secondary chemical shifts and cross-hydrogen bond 15N-13C' scalar couplings (3hbJNC'). Journal of Biomolecular Nmr. 21: 221-33. PMID 11775739 DOI: 10.1023/A:1012935005256  0.783
2001 Kalodimos CG, Folkers GE, Boelens R, Kaptein R. Strong DNA binding by covalently linked dimeric Lac headpiece: evidence for the crucial role of the hinge helices. Proceedings of the National Academy of Sciences of the United States of America. 98: 6039-44. PMID 11353825 DOI: 10.1073/Pnas.101129898  0.813
2001 Hanzawa H, de Ruwe MJ, Albert TK, van Der Vliet PC, Timmers HT, Boelens R. The structure of the C4C4 ring finger of human NOT4 reveals features distinct from those of C3HC4 RING fingers. The Journal of Biological Chemistry. 276: 10185-90. PMID 11087754 DOI: 10.1074/Jbc.M009298200  0.361
2000 Nooren IM, Folkers GE, Kaptein R, Sauer RT, Boelens R. Structure and dynamics of the tetrameric mnt repressor and a model for its DNA complex. Journal of Biomolecular Structure & Dynamics. 17: 113-22. PMID 22607414 DOI: 10.1080/07391102.2000.10506611  0.755
2000 Eijkelenboom AP, van den Ent FM, Wechselberger R, Plasterk RH, Kaptein R, Boelens R. Refined solution structure of the dimeric N-terminal HHCC domain of HIV-2 integrase. Journal of Biomolecular Nmr. 18: 119-28. PMID 11101216 DOI: 10.1023/A:1008342312269  0.634
2000 Craven CJ, Derix NM, Hendriks J, Boelens R, Hellingwerf KJ, Kaptein R. Probing the nature of the blue-shifted intermediate of photoactive yellow protein in solution by NMR: hydrogen-deuterium exchange data and pH studies. Biochemistry. 39: 14392-9. PMID 11087391 DOI: 10.1021/Bi001628P  0.655
2000 Guenneugues M, Caserta E, Brandi L, Spurio R, Meunier S, Pon CL, Boelens R, Gualerzi CO. Mapping the fMet-tRNA(f)(Met) binding site of initiation factor IF2. The Embo Journal. 19: 5233-40. PMID 11013225 DOI: 10.1093/Emboj/19.19.5233  0.322
2000 van Tilborg MA, Lefstin JA, Kruiskamp M, Teuben J, Boelens R, Yamamoto KR, Kaptein R. Mutations in the glucocorticoid receptor DNA-binding domain mimic an allosteric effect of DNA. Journal of Molecular Biology. 301: 947-58. PMID 10966797 DOI: 10.1006/Jmbi.2000.4001  0.659
2000 van Tilborg PJ, Czisch M, Mulder FA, Folkers GE, Bonvin AM, Nair M, Boelens R, Kaptein R. Changes in dynamical behavior of the retinoid X receptor DNA-binding domain upon binding to a 14 base-pair DNA half site. Biochemistry. 39: 8747-57. PMID 10913286 DOI: 10.1021/Bi991550G  0.814
2000 Melacini G, Bonvin AM, Goodman M, Boelens R, Kaptein R. Hydration dynamics of the collagen triple helix by NMR. Journal of Molecular Biology. 300: 1041-9. PMID 10903852 DOI: 10.1006/Jmbi.2000.3919  0.794
2000 Erbel PJ, Karimi-Nejad Y, van Kuik JA, Boelens R, Kamerling JP, Vliegenthart JF. Effects of the N-linked glycans on the 3D structure of the free alpha-subunit of human chorionic gonadotropin. Biochemistry. 39: 6012-21. PMID 10821673 DOI: 10.1021/Bi992786N  0.437
2000 Meunier S, Spurio R, Czisch M, Wechselberger R, Guenneugues M, Gualerzi CO, Boelens R. Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2. The Embo Journal. 19: 1918-26. PMID 10775275 DOI: 10.1093/Emboj/19.8.1918  0.401
2000 Spronk CAEM, Bonvin AMJJ, Radha PK, Melacini G, Boelens R, Kaptein R. Nmr Structure Of Lac Repressor Hp62-Dna Complex Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb1Cjg/Pdb  0.808
1999 Melacini G, Boelens R, Kaptein R. Band-selective editing of exchange-relay in protein-water NOE experiments. Journal of Biomolecular Nmr. 13: 67-71. PMID 21080264 DOI: 10.1023/A:1008350918005  0.777
1999 Nooren IM, George AV, Kaptein R, Sauer RT, Boelens R. NMR structure determination of the tetramerization domain of the Mnt repressor: An asymmetric alpha-helical assembly in slow exchange. Journal of Biomolecular Nmr. 15: 39-53. PMID 20703962 DOI: 10.1023/A:1008312309535  0.672
1999 Melacini G, Boelens R, Kaptein R. Water-macromolecule interactions by NMR: a quadrature-free constant-time approach and its application to CI2. Journal of Biomolecular Nmr. 15: 189-201. PMID 10677822 DOI: 10.1023/A:1008316612907  0.78
1999 Spronk CA, Bonvin AM, Radha PK, Melacini G, Boelens R, Kaptein R. The solution structure of Lac repressor headpiece 62 complexed to a symmetrical lac operator. Structure (London, England : 1993). 7: 1483-92. PMID 10647179 DOI: 10.1016/S0969-2126(00)88339-2  0.819
1999 Spronk CA, Folkers GE, Noordman AM, Wechselberger R, van den Brink N, Boelens R, Kaptein R. Hinge-helix formation and DNA bending in various lac repressor-operator complexes. The Embo Journal. 18: 6472-80. PMID 10562559 DOI: 10.1093/Emboj/18.22.6472  0.715
1999 Mulder FA, Schipper D, Bott R, Boelens R. Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins. Journal of Molecular Biology. 292: 111-23. PMID 10493861 DOI: 10.1006/Jmbi.1999.3034  0.789
1999 Eijkelenboom AP, Sprangers R, Hård K, Puras Lutzke RA, Plasterk RH, Boelens R, Kaptein R. Refined solution structure of the C-terminal DNA-binding domain of human immunovirus-1 integrase. Proteins. 36: 556-64. PMID 10450096 DOI: 10.1002/(Sici)1097-0134(19990901)36:4<556::Aid-Prot18>3.0.Co;2-6  0.701
1999 Bott R, Boelens R. The role of high-resolution structural studies in the development of commercial enzymes. Current Opinion in Biotechnology. 10: 391-7. PMID 10449323 DOI: 10.1016/S0958-1669(99)80071-8  0.32
1999 Nooren IM, Kaptein R, Sauer RT, Boelens R. The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils. Nature Structural Biology. 6: 755-9. PMID 10426954 DOI: 10.1038/11531  0.667
1999 Nooren IM, Rietveld AW, Melacini G, Sauer RT, Kaptein R, Boelens R. The solution structure and dynamics of an Arc repressor mutant reveal premelting conformational changes related to DNA binding. Biochemistry. 38: 6035-42. PMID 10320329 DOI: 10.1021/Bi982677T  0.816
1999 Mulder FA, van Tilborg PJ, Kaptein R, Boelens R. Microsecond time scale dynamics in the RXR DNA-binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements. Journal of Biomolecular Nmr. 13: 275-88. PMID 10212986 DOI: 10.1023/A:1008354232281  0.823
1999 Erbel PJ, Karimi-Nejad Y, De Beer T, Boelens R, Kamerling JP, Vliegenthart JF. Solution structure of the alpha-subunit of human chorionic gonadotropin. European Journal of Biochemistry / Febs. 260: 490-8. PMID 10095786 DOI: 10.1046/J.1432-1327.1999.00188.X  0.371
1999 Rubinstenn G, Vuister GW, Zwanenburg N, Hellingwerf KJ, Boelens R, Kaptein R. NMR experiments for the study of photointermediates: application to the photoactive yellow protein. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 137: 443-7. PMID 10089180 DOI: 10.1006/Jmre.1999.1705  0.794
1999 van Tilborg PJ, Mulder FA, de Backer MM, Nair M, van Heerde EC, Folkers G, van der Saag PT, Karimi-Nejad Y, Boelens R, Kaptein R. Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation. Biochemistry. 38: 1951-6. PMID 10026278 DOI: 10.1021/Bi982526Q  0.815
1999 Melacini G, Kaptein R, Boelens R. Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of protein-water interactions. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 136: 214-8. PMID 9986764 DOI: 10.1006/Jmre.1998.1646  0.786
1999 Werten S, Wechselberger R, Boelens R, van der Vliet PC, Kaptein R. Identification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR. The Journal of Biological Chemistry. 274: 3693-9. PMID 9920920 DOI: 10.1074/Jbc.274.6.3693  0.676
1999 Sette M, Spurio R, van Tilborg P, Gualerzi CO, Boelens R. Identification of the ribosome binding sites of translation initiation factor IF3 by multidimensional heteronuclear NMR spectroscopy. Rna (New York, N.Y.). 5: 82-92. PMID 9917068 DOI: 10.1017/S1355838299981487  0.394
1999 Karimi-Nejad Y, Löhr F, Schipper D, Rüterjans H, Boelens R. Gradient-purged isotope filter experiments for the detection of bound water in proteins Chemical Physics Letters. 300: 706-712. DOI: 10.1016/S0009-2614(98)01421-3  0.332
1998 Düx P, Rubinstenn G, Vuister GW, Boelens R, Mulder FA, Hård K, Hoff WD, Kroon AR, Crielaard W, Hellingwerf KJ, Kaptein R. Solution structure and backbone dynamics of the photoactive yellow protein. Biochemistry. 37: 12689-99. PMID 9737845 DOI: 10.1021/Bi9806652  0.818
1998 Rubinstenn G, Vuister GW, Mulder FA, Düx PE, Boelens R, Hellingwerf KJ, Kaptein R. Structural and dynamic changes of photoactive yellow protein during its photocycle in solution. Nature Structural Biology. 5: 568-70. PMID 9665170 DOI: 10.1038/823  0.806
1998 Mulder FAA, de Graaf RA, Kaptein R, Boelens R. An Off-resonance Rotating Frame Relaxation Experiment for the Investigation of Macromolecular Dynamics Using Adiabatic Rotations Journal of Magnetic Resonance (San Diego, Calif. : 1997). 131: 351-7. PMID 9571112 DOI: 10.1006/Jmre.1998.1380  0.624
1998 van Zuylen CW, de Beer T, Leeflang BR, Boelens R, Kaptein R, Kamerling JP, Vliegenthart JF. Mobilities of the inner three core residues and the Man(alpha 1--6) branch of the glycan at Asn78 of the alpha-subunit of human chorionic gonadotropin are restricted by the protein. Biochemistry. 37: 1933-40. PMID 9485320 DOI: 10.1021/Bi9718548  0.607
1998 KARIMI-NEJAD Y, WARREN GL, SCHIPPER D, BRÜNGER AT, BOELENS R. NMR structure calculation methods for large proteins Application of torsion angle dynamics and distance geometry/simulated annealing to the 269-residue protein serine protease PB92 Molecular Physics. 95: 1099-1112. DOI: 10.1080/00268979809483242  0.599
1998 Vis H, Vorgias CE, Wilson KS, Kaptein R, Boelens R. Journal of Biomolecular Nmr. 11: 265-277. DOI: 10.1023/A:1008208615714  0.549
1998 Vis H, Vorgias CE, Wilson KS, Kaptein R, Boelens R. Mobility of NH bonds in DNA-binding protein HU of Bacillus stearothermophilus from reduced spectral density mapping analysis at multiple NMR fields Journal of Biomolecular Nmr. 11: 265-277. DOI: 10.1023/A:1008208615714  0.618
1997 Düx P, Whitehead B, Boelens R, Kaptein R, Vuister GW. Measurement of (15)N- (1)H coupling constants in uniformly (15)N-labeled proteins: Application to the photoactive yellow protein. Journal of Biomolecular Nmr. 10: 301-6. PMID 20700833 DOI: 10.1023/A:1018393225804  0.787
1997 Whitehead B, Tessari M, Düx P, Boelens R, Kaptein R, Vuister GW. A 15n-filtered 2D 1H TOCSY experiment for assignment of aromatic ring resonances and selective identification of tyrosine ring resonances in proteins: Description and application to Photoactive Yellow Protein. Journal of Biomolecular Nmr. 9: 313-6. PMID 20680663 DOI: 10.1023/A:1018687127330  0.789
1997 Eijkelenboom AP, van den Ent FM, Vos A, Doreleijers JF, Hård K, Tullius TD, Plasterk RH, Kaptein R, Boelens R. The solution structure of the amino-terminal HHCC domain of HIV-2 integrase: a three-helix bundle stabilized by zinc. Current Biology : Cb. 7: 739-46. PMID 9368756 DOI: 10.1016/S0960-9822(06)00332-0  0.67
1997 Sette M, van Tilborg P, Spurio R, Kaptein R, Paci M, Gualerzi CO, Boelens R. The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif. The Embo Journal. 16: 1436-43. PMID 9135158 DOI: 10.1093/Emboj/16.6.1436  0.698
1997 Martin JR, Mulder FA, Karimi-Nejad Y, van der Zwan J, Mariani M, Schipper D, Boelens R. The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site. Structure (London, England : 1993). 5: 521-32. PMID 9115441 DOI: 10.1016/S0969-2126(97)00208-6  0.8
1997 Slijper M, Boelens R, Davis AL, Konings RN, van der Marel GA, van Boom JH, Kaptein R. Backbone and side chain dynamics of lac repressor headpiece (1-56) and its complex with DNA. Biochemistry. 36: 249-54. PMID 8993340 DOI: 10.1021/Bi961670D  0.67
1997 Tessari M, Vis H, Boelens R, Kaptein R, Vuister GW. Quantitative measurement of relaxation interference effects between 1H(N) CSA and 1H-15N dipolar interaction: Correlation with secondary structure Journal of the American Chemical Society. 119: 8985-8990. DOI: 10.1021/Ja970573K  0.791
1997 Tessari M, Mulder FA, Boelens R, Vuister GW. Determination of Amide Proton CSA in15N-Labeled Proteins Using1H CSA/15N–1H Dipolar and15N CSA/15N–1H Dipolar Cross-Correlation Rates Journal of Magnetic Resonance. 127: 128-133. DOI: 10.1006/Jmre.1997.1199  0.787
1996 Mulder FA, Spronk CA, Slijper M, Kaptein R, Boelens R. Improved HSQC experiments for the observation of exchange broadened signals. Journal of Biomolecular Nmr. 8: 223-8. PMID 22911143 DOI: 10.1007/Bf00211169  0.81
1996 Boelens R, Vis H, Vorgias CE, Wilson KS, Kaptein R. Structure and dynamics of the DNA binding protein HU from Bacillus stearothermophilus by NMR spectroscopy. Biopolymers. 40: 553-9. PMID 9101760 DOI: 10.1002/(Sici)1097-0282(1996)40:5<553::Aid-Bip13>3.0.Co;2-I  0.674
1996 Doreleijers JF, Langedijk JP, Hård K, Boelens R, Rullmann JA, Schaaper WM, van Oirschot JT, Kaptein R. Solution structure of the immunodominant region of protein G of bovine respiratory syncytial virus. Biochemistry. 35: 14684-8. PMID 8942628 DOI: 10.1021/Bi9621627  0.652
1996 Spronk CA, Slijper M, van Boom JH, Kaptein R, Boelens R. Formation of the hinge helix in the lac repressor is induced upon binding to the lac operator. Nature Structural Biology. 3: 916-9. PMID 8901866 DOI: 10.1038/Nsb1196-916  0.603
1996 De Beer T, Van Zuylen CW, Leeflang BR, Hård K, Boelens R, Kaptein R, Kamerling JP, Vliegenthart JF. NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit. European Journal of Biochemistry / Febs. 241: 229-42. PMID 8898911 DOI: 10.1111/J.1432-1033.1996.0229T.X  0.642
1996 van Geerestein-Ujah EC, Mariani M, Vis H, Boelens R, Kaptein R. Use of graph theory for secondary structure recognition and sequential assignment in heteronuclear (13C, 15N) NMR spectra: application to HU protein from Bacillus stearothermophilus. Biopolymers. 39: 691-707. PMID 8875823 DOI: 10.1002/(Sici)1097-0282(199611)39:5<691::Aid-Bip8>3.0.Co;2-R  0.671
1996 Slijper M, Bonvin AM, Boelens R, Kaptein R. Refined structure of lac repressor headpiece (1-56) determined by relaxation matrix calculations from 2D and 3D NOE data: change of tertiary structure upon binding to the lac operator. Journal of Molecular Biology. 259: 761-73. PMID 8683581 DOI: 10.1006/Jmbi.1996.0356  0.819
1996 Slijper M, Kaptein R, Boelens R. Simultaneous 13C and 15N isotope editing of biomolecular complexes. Application to a mutant lac repressor headpiece DNA complex. Journal of Magnetic Resonance. Series B. 111: 199-203. PMID 8661282 DOI: 10.1006/Jmrb.1996.0083  0.617
1996 Vis H, Vageli O, Nagel J, Vorgias CE, Wilson KS, Kaptein R, Boelens R. NMR Study of the Interaction of the HU Protein fromBacillus Stearothermophiluswith DNA Magnetic Resonance in Chemistry. 34: S81-S86. DOI: 10.1002/(SICI)1097-458X(199612)34:133.0.CO;2-7  0.63
1996 Vis H, Vageli O, Nagel J, Vorgias CE, Wilson KS, Kaptein R, Boelens R. NMR study of the interaction of the HU protein from Bacillus stearothermophilus with DNA Magnetic Resonance in Chemistry. 34: S81-S86. DOI: 10.1002/(Sici)1097-458X(199612)34:133.0.Co;2-7  0.664
1995 Kaptein R, Slijper M, Boelens R. Structure and dynamics of the lac repressor-operator complex as determined by NMR. Toxicology Letters. 82: 591-9. PMID 8597114 DOI: 10.1016/0378-4274(95)03586-9  0.695
1995 Kaptein R, Boelens R, Chuprina VP, Rullmann JA, Slijper M. NMR and nucleic acid-protein interactions: the lac repressor-operator system. Methods in Enzymology. 261: 513-24. PMID 8569509 DOI: 10.1016/S0076-6879(95)61022-7  0.709
1995 van Houte LP, Chuprina VP, van der Wetering M, Boelens R, Kaptein R, Clevers H. Solution structure of the sequence-specific HMG box of the lymphocyte transcriptional activator Sox-4. The Journal of Biological Chemistry. 270: 30516-24. PMID 8530483 DOI: 10.1074/Jbc.270.51.30516  0.679
1995 Breg JN, Sarda L, Cozzone PJ, Rugani N, Boelens R, Kaptein R. Solution structure of porcine pancreatic procolipase as determined from 1H homonuclear two-dimensional and three-dimensional NMR. European Journal of Biochemistry / Febs. 227: 663-72. PMID 7867624 DOI: 10.1111/J.1432-1033.1995.0663P.X  0.682
1995 van Nuland NA, Boelens R, Scheek RM, Robillard GT. High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data. Journal of Molecular Biology. 246: 180-93. PMID 7853396 DOI: 10.1006/Jmbi.1994.0075  0.633
1995 Fogh RH, Schipper D, Boelens R, Kaptein R. Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus. Journal of Biomolecular Nmr. 5: 259-70. PMID 7787423 DOI: 10.1007/Bf00211753  0.679
1995 Knegtel RM, Fogh RH, Ottleben G, Rüterjans H, Dumoulin P, Schnarr M, Boelens R, Kaptein R. A model for the LexA repressor DNA complex. Proteins. 21: 226-36. PMID 7784426 DOI: 10.1002/Prot.340210305  0.676
1995 van Tilborg MA, Bonvin AM, Hård K, Davis AL, Maler B, Boelens R, Yamamoto KR, Kaptein R. Structure refinement of the glucocorticoid receptor-DNA binding domain from NMR data by relaxation matrix calculations. Journal of Molecular Biology. 247: 689-700. PMID 7723024 DOI: 10.1016/S0022-2836(05)80148-2  0.814
1995 van den Berg B, Tessari M, Boelens R, Dijkman R, Kaptein R, de Haas GH, Verheij HM. Solution structure of porcine pancreatic phospholipase A2 complexed with micelles and a competitive inhibitor. Journal of Biomolecular Nmr. 5: 110-21. PMID 7703697 DOI: 10.1007/Bf00208802  0.678
1995 Burgering MJ, Hald M, Boelens R, Breg JN, Kaptein R. Hydrogen exchange studies of the Arc repressor: evidence for a monomeric folding intermediate. Biopolymers. 35: 217-26. PMID 7696567 DOI: 10.1002/Bip.360350210  0.663
1995 van den Berg B, Tessari M, Boelens R, Dijkman R, de Haas GH, Kaptein R, Verheij HM. NMR structures of phospholipase A2 reveal conformational changes during interfacial activation. Nature Structural Biology. 2: 402-6. PMID 7664098 DOI: 10.1038/Nsb0595-402  0.63
1995 van Geerestein-Ujah EC, Slijper M, Boelens R, Kaptein R. Graph-theoretical assignment of secondary structure in multidimensional protein NMR spectra: application to the lac repressor headpiece. Journal of Biomolecular Nmr. 6: 67-78. PMID 7663143 DOI: 10.1007/Bf00417493  0.664
1995 Cox M, van Tilborg PJ, de Laat W, Boelens R, van Leeuwen HC, van der Vliet PC, Kaptein R. Solution structure of the Oct-1 POU homeodomain determined by NMR and restrained molecular dynamics. Journal of Biomolecular Nmr. 6: 23-32. PMID 7663141 DOI: 10.1007/Bf00417488  0.714
1995 Knegtel RM, van Tilborg MA, Boelens R, Kaptein R. NMR structural studies on the zinc finger domains of nuclear hormone receptors. Exs. 73: 279-95. PMID 7579977  0.672
1995 van den Berg B, Tessari M, de Haas GH, Verheij HM, Boelens R, Kaptein R. Solution structure of porcine pancreatic phospholipase A2. The Embo Journal. 14: 4123-31. PMID 7556053 DOI: 10.1002/J.1460-2075.1995.Tb00086.X  0.655
1995 Eijkelenboom AP, Lutzke RA, Boelens R, Plasterk RH, Kaptein R, Hård K. The DNA-binding domain of HIV-1 integrase has an SH3-like fold. Nature Structural Biology. 2: 807-10. PMID 7552753 DOI: 10.1038/Nsb0995-807  0.661
1995 Chupin V, Killian JA, Breg J, de Jongh HH, Boelens R, Kaptein R, de Kruijff B. PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, which is modulated by the environment. A two-dimensional 1H NMR study. Biochemistry. 34: 11617-24. PMID 7547893 DOI: 10.1021/Bi00036A038  0.649
1995 Vis H, Mariani M, Vorgias CE, Wilson KS, Kaptein R, Boelens R. Solution structure of the HU protein from Bacillus stearothermophilus. Journal of Molecular Biology. 254: 692-703. PMID 7500343 DOI: 10.1006/Jmbi.1995.0648  0.666
1995 Tessari M, Mariani M, Boelens R, Kaptein R. (H)XYH-COSY and (H)XYH-E.COSY Experiments for Backbone and Side-Chain Assignment and Determination of 3JHH′ Coupling Constants in (13C, 15N)-Labeled Proteins Journal of Magnetic Resonance, Series B. 108: 89-93. DOI: 10.1006/Jmrb.1995.1108  0.621
1994 Boelens R, Burgering M, Fogh RH, Kaptein R. Time-saving methods for heteronuclear multidimensional NMR of ((13)C, (15)N) doubly labeled proteins. Journal of Biomolecular Nmr. 4: 201-13. PMID 22911218 DOI: 10.1007/Bf00175248  0.638
1994 Bonvin AM, Boelens R, Kaptein R. Time- and ensemble-averaged direct NOE restraints. Journal of Biomolecular Nmr. 4: 143-9. PMID 22911161 DOI: 10.1007/Bf00178343  0.778
1994 Fogh RH, Schipper D, Boelens R, Kaptein R. (1)H, (13)C and (15)N NMR backbone assignments of the 269-residue serine protease PB92 from Bacillus alcalophilus. Journal of Biomolecular Nmr. 4: 123-8. PMID 22911160 DOI: 10.1007/Bf00178340  0.675
1994 Knegtel RM, Antoon J, Rullmann C, Boelens R, Kaptein R. MONTY: a Monte Carlo approach to protein-DNA recognition. Journal of Molecular Biology. 235: 318-24. PMID 8289251 DOI: 10.1016/S0022-2836(05)80035-X  0.677
1994 Cox M, Schaller J, Boelens R, Kaptein R, Rickli E, Llinás M. Kringle solution structures via NMR: two-dimensional 1H-NMR analysis of horse plasminogen kringle 4. Chemistry and Physics of Lipids. 67: 43-58. PMID 8187244 DOI: 10.1016/0009-3084(94)90123-6  0.663
1994 Bonvin AM, Vis H, Breg JN, Burgering MJ, Boelens R, Kaptein R. Nuclear magnetic resonance solution structure of the Arc repressor using relaxation matrix calculations. Journal of Molecular Biology. 236: 328-41. PMID 8107113 DOI: 10.1006/Jmbi.1994.1138  0.802
1994 Fogh RH, Ottleben G, Rüterjans H, Schnarr M, Boelens R, Kaptein R. Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy. The Embo Journal. 13: 3936-44. PMID 8076591 DOI: 10.1002/J.1460-2075.1994.Tb06709.X  0.71
1994 de Beer T, van Zuylen CW, Hård K, Boelens R, Kaptein R, Kamerling JP, Vliegenthart JF. Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein. Application of gradient-enhanced natural abundance 1H-13C HSQC and HSQC-TOCSY to the alpha-subunit of human chorionic gonadotropin. Febs Letters. 348: 1-6. PMID 8026573 DOI: 10.1016/0014-5793(94)00547-8  0.635
1994 Burgering MJ, Boelens R, Gilbert DE, Breg JN, Knight KL, Sauer RT, Kaptein R. Solution structure of dimeric Mnt repressor (1-76). Biochemistry. 33: 15036-45. PMID 7999761 DOI: 10.1021/Bi00254A012  0.699
1994 Vis H, Boelens R, Mariani M, Stroop R, Vorgias CE, Wilson KS, Kaptein R. 1H, 13C, and 15N resonance assignments and secondary structure analysis of the HU protein from Bacillus stearothermophilus using two- and three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy. Biochemistry. 33: 14858-70. PMID 7993912 DOI: 10.1021/Bi00253A025  0.693
1994 Hoff WD, Düx P, Hård K, Devreese B, Nugteren-Roodzant IM, Crielaard W, Boelens R, Kaptein R, van Beeumen J, Hellingwerf KJ. Thiol ester-linked p-coumaric acid as a new photoactive prosthetic group in a protein with rhodopsin-like photochemistry. Biochemistry. 33: 13959-62. PMID 7947803 DOI: 10.1021/Bi00251A001  0.622
1994 Knegtel RM, Boelens R, Kaptein R. Monte Carlo docking of protein-DNA complexes: incorporation of DNA flexibility and experimental data. Protein Engineering. 7: 761-7. PMID 7937706 DOI: 10.1093/Protein/7.6.761  0.659
1994 Holm L, Sander C, Rüterjans H, Schnarr M, Fogh R, Boelens R, Kaptein R. LexA repressor and iron uptake regulator from Escherichia coli: new members of the CAP-like DNA binding domain superfamily. Protein Engineering. 7: 1449-53. PMID 7716155 DOI: 10.1093/Protein/7.12.1449  0.674
1994 Mariani M, Tessari M, Boelens R, Vis H, Kaptein R. Assignment of the Protein Backbone from a Single 3D, 15N, 13C, Time-Shared Hxyh Experiment Journal of Magnetic Resonance, Series B. 104: 294-297. DOI: 10.1006/Jmrb.1994.1089  0.628
1994 Bonvin AMJJ, Boelens R, Kaptein R. Direct nuclear Overhauser effect refinement of crambin from two-dimensional nmr data using a slow-cooling annealing protocol Biopolymers. 34: 39-50. DOI: 10.1002/Bip.360340106  0.655
1993 Cox M, Dekker N, Boelens R, Verrijzer CP, van der Vliet PC, Kaptein R. NMR studies of the POU-specific DNA-binding domain of Oct-1: sequential 1H and 15N assignments and secondary structure. Biochemistry. 32: 6032-40. PMID 8507639 DOI: 10.1021/Bi00074A014  0.71
1993 Dekker N, Cox M, Boelens R, Verrijzer CP, van der Vliet PC, Kaptein R. Solution structure of the POU-specific DNA-binding domain of Oct-1. Nature. 362: 852-5. PMID 8479524 DOI: 10.1038/362852A0  0.689
1993 Bonvin AM, Rullmann JA, Lamerichs RM, Boelens R, Kaptein R. "Ensemble" iterative relaxation matrix approach: a new NMR refinement protocol applied to the solution structure of crambin. Proteins. 15: 385-400. PMID 8460109 DOI: 10.1002/Prot.340150406  0.789
1993 Knegtel RM, Boelens R, Ganadu ML, George AV, Katahira M, Bonvin AM, Eib D, van der Saag PT, Kaptein R. NMR studies of the human retinoic acid receptor-beta DNA-binding domain. Metal coordination and three-dimensional structure. Annals of the New York Academy of Sciences. 684: 49-62. PMID 8391240 DOI: 10.1111/J.1749-6632.1993.Tb32270.X  0.784
1993 Knegtel RM, Boelens R, Ganadu ML, George AV, van der Saag PT, Kaptein R. Heteronuclear 113Cd-1H NMR study of metal coordination in the human retinoic acid receptor-beta DNA binding domain. Biochemical and Biophysical Research Communications. 192: 492-8. PMID 8387280 DOI: 10.1006/Bbrc.1993.1442  0.64
1993 Knegtel RM, Katahira M, Schilthuis JG, Bonvin AM, Boelens R, Eib D, van der Saag PT, Kaptein R. The solution structure of the human retinoic acid receptor-beta DNA-binding domain. Journal of Biomolecular Nmr. 3: 1-17. PMID 8383553 DOI: 10.1007/Bf00242472  0.802
1993 Burgering MJ, Boelens R, Caffrey M, Breg JN, Kaptein R. Observation of inter-subunit nuclear Overhauser effects in a dimeric protein. Application to the Arc repressor. Febs Letters. 330: 105-9. PMID 8370451 DOI: 10.1016/0014-5793(93)80929-O  0.661
1993 Chuprina VP, Rullmann JA, Lamerichs RM, van Boom JH, Boelens R, Kaptein R. Structure of the complex of lac repressor headpiece and an 11 base-pair half-operator determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics. Journal of Molecular Biology. 234: 446-62. PMID 8230225 DOI: 10.1006/Jmbi.1993.1598  0.685
1993 Burgering M, Boelens R, Kaptein R. Observation of intersubunit NOEs in a dimeric P22 Mnt repressor mutant by a time-shared [15N, 13C] double half-filter technique Journal of Biomolecular Nmr. 3. DOI: 10.1007/Bf00198373  0.621
1993 Kleywegt GJ, Vuister GW, Padilla A, Knegtel RMA, Boelens R, Kaptein R. Computer-Assisted Assignment of Homonuclear 3D NMR Spectra of Proteins. Application to Pike Parvalbumin III Journal of Magnetic Resonance, Series B. 102: 166-176. DOI: 10.1006/Jmrb.1993.1079  0.804
1992 Kellenbach ER, Remerowski ML, Eib D, Boelens R, van der Marel GA, van den Elst H, van Boom JH, Kaptein R. Synthesis of isotope labeled oligonucleotides and their use in an NMR study of a protein-DNA complex. Nucleic Acids Research. 20: 653-7. PMID 1542561 DOI: 10.1093/Nar/20.4.653  0.669
1992 Peters AR, Dekker N, van den Berg L, Boelens R, Slotboom AJ, de Haas GH, Kaptein R. NMR studies of interactions between inhibitors and porcine pancreatic phospholipase A2. Biochimie. 74: 859-66. PMID 1467344 DOI: 10.1016/0300-9084(92)90069-Q  0.636
1992 de Waard P, Leeflang BR, Vliegenthart JF, Boelens R, Vuister GW, Kaptein R. Application of 2D and 3D NMR experiments to the conformational study of a diantennary oligosaccharide. Journal of Biomolecular Nmr. 2: 211-26. PMID 1392566 DOI: 10.1007/Bf01875317  0.78
1992 Peters AR, Dekker N, van den Berg L, Boelens R, Kaptein R, Slotboom AJ, de Haas GH. Conformational changes in phospholipase A2 upon binding to micellar interfaces in the absence and presence of competitive inhibitors. A 1H and 15N NMR study. Biochemistry. 31: 10024-30. PMID 1390760 DOI: 10.1021/Bi00156A023  0.674
1992 Katahira M, Knegtel R, Schilthius J, Boelens R, Eib D, van der Saag P, Kaptein R. The structure of the human retinoic acid receptor-beta DNA-binding domain determined by NMR. Nucleic Acids Symposium Series. 65-6. PMID 1337792  0.34
1992 Katahira M, Knegtel RM, Boelens R, Eib D, Schilthuis JG, van der Saag PT, Kaptein R. Homo- and heteronuclear NMR studies of the human retinoic acid receptor beta DNA-binding domain: sequential assignments and identification of secondary structure elements. Biochemistry. 31: 6474-80. PMID 1321662 DOI: 10.1021/Bi00143A017  0.666
1992 Vuister GW, Boelens R, Kaptein R, Burgering M, van Zijl PCM. Gradient-enhanced 3D NOESY-HMQC spectroscopy Journal of Biomolecular Nmr. 2: 301-305. DOI: 10.1007/Bf01875323  0.77
1992 Davis AL, Boelens R, Kaptein R. Rapid acquisition of three-dimensional triple-resonance experiments using pulsed field gradient techniques Journal of Biomolecular Nmr. 2: 395-400. DOI: 10.1007/Bf01874817  0.588
1991 Dekker N, Peters AR, Slotboom AJ, Boelens R, Kaptein R, de Haas G. Porcine pancreatic phospholipase A2: sequence-specific 1H and 15N NMR assignments and secondary structure. Biochemistry. 30: 3135-46. PMID 2007145 DOI: 10.1021/Bi00226A022  0.668
1991 Kellenbach E, Maler BA, Yamamoto KR, Boelens R, Kaptein R. Identification of the metal coordinating residues in the DNA binding domain of the glucocorticoid receptor by 113Cd-1H heteronuclear NMR spectroscopy. Febs Letters. 291: 367-70. PMID 1936288 DOI: 10.1016/0014-5793(91)81322-Y  0.639
1991 Dekker N, Peters AR, Slotboom AJ, Boelens R, Kaptein R, Dijkman R, de Haas G. Two-dimensional 1H-NMR studies of phospholipase-A2-inhibitor complexes bound to a micellar lipid-water interface. European Journal of Biochemistry / Febs. 199: 601-7. PMID 1868846 DOI: 10.1111/J.1432-1033.1991.Tb16160.X  0.632
1991 Koning TM, Boelens R, van der Marel GA, van Boom JH, Kaptein R. Structure determination of a DNA octamer in solution by NMR spectroscopy. Effect of fast local motions. Biochemistry. 30: 3787-97. PMID 1849738 DOI: 10.1021/Bi00229A028  0.655
1991 Vuister GW, Boelens R, Padilla A, Kaptein R. Statistical analysis of double NOE transfer pathways in proteins as measured in 3D NOE-NOE spectroscopy. Journal of Biomolecular Nmr. 1: 421-38. PMID 1841709 DOI: 10.1007/Bf02192864  0.808
1991 Bonvin AM, Boelens R, Kaptein R. Direct NOE refinement of biomolecular structures using 2D NMR data. Journal of Biomolecular Nmr. 1: 305-9. PMID 1841701 DOI: 10.1007/Bf01875523  0.779
1991 Kleywegt GJ, Boelens R, Cox M, Llinás M, Kaptein R. Computer-assisted assignment of 2D 1H NMR spectra of proteins: basic algorithms and application to phoratoxin B. Journal of Biomolecular Nmr. 1: 23-47. PMID 1841687 DOI: 10.1007/Bf01874567  0.729
1991 Kellenbach E, Härd T, Boelens R, Dahlman K, Carlstedt-Duke J, Gustafsson JA, van der Marel GA, van Boom JH, Maler B, Yamamoto KR. Photo-CIDNP study of the interaction between the glucocorticoid receptor DNA-binding domain and glucocorticoid response elements. Journal of Biomolecular Nmr. 1: 105-10. PMID 1841686 DOI: 10.1007/Bf01874574  0.387
1991 Knegtel RM, Boelens R, Ganadu ML, Kaptein R. The solution structure of a monomeric insulin. A two-dimensional 1H-NMR study of des-(B26-B30)-insulin in combination with distance geometry and restrained molecular dynamics. European Journal of Biochemistry / Febs. 202: 447-58. PMID 1761045 DOI: 10.1111/J.1432-1033.1991.Tb16394.X  0.622
1991 Remerowski ML, Kellenbach E, Boelens R, van der Marel GA, van Boom JH, Maler BA, Yamamoto KR, Kaptein R. 1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA binding domain with a half-site response element. Biochemistry. 30: 11620-4. PMID 1751485 DOI: 10.1021/Bi00114A003  0.682
1991 Vuister GW, Boelens R, Kaptein R, Hurd RE, John B, Van Zijl PCM. Gradient-enhanced HMQC and HSQC spectroscopy. Applications to 15N-labeled Mnt repressor Journal of the American Chemical Society. 113: 9688-9690. DOI: 10.1021/Ja00025A053  0.764
1991 Gonzalez C, Rullmann JAC, Bonvin AMJJ, Boelens R, Kaptein R. Toward an NMR R factor Journal of Magnetic Resonance (1969). 91: 659-664. DOI: 10.1016/0022-2364(91)90397-C  0.581
1991 Bonvin AMJJ, Boelens R, Kaptein R. Direct structure refinement using 3D NOE-NOE spectra of biomolecules Journal of Magnetic Resonance (1969). 95: 626-631. DOI: 10.1016/0022-2364(91)90180-2  0.641
1990 Breg JN, van Opheusden JH, Burgering MJ, Boelens R, Kaptein R. Structure of Arc repressor in solution: evidence for a family of beta-sheet DNA-binding proteins. Nature. 346: 586-9. PMID 2377232 DOI: 10.1038/346586A0  0.695
1990 Kaptein R, Lamerichs RM, Boelens R, Rullmann JA. Two-dimensional NMR study of a protein-DNA complex. lac repressor headpiece-operator interaction. Biochemical Pharmacology. 40: 89-96. PMID 2372315 DOI: 10.1016/0006-2952(90)90183-L  0.678
1990 Vuister GW, Boelens R, Padilla A, Kleywegt GJ, Kaptein R. Assignment strategies in homonuclear three-dimensional 1H NMR spectra of proteins. Biochemistry. 29: 1829-39. PMID 2331467 DOI: 10.1021/Bi00459A024  0.811
1990 Härd T, Kellenbach E, Boelens R, Kaptein R, Dahlman K, Carlstedt-Duke J, Freedman LP, Maler BA, Hyde EI, Gustafsson JA. 1H NMR studies of the glucocorticoid receptor DNA-binding domain: sequential assignments and identification of secondary structure elements. Biochemistry. 29: 9015-23. PMID 2271574  0.655
1990 Lamerichs RM, Boelens R, Van der Marel GA, Van Boom JH, Kaptein R. Assignment of the 1H-NMR spectrum of a lac repressor headpiece-operator complex in H2O and identification of NOEs. Consequences for protein-DNA interaction. European Journal of Biochemistry / Febs. 194: 629-37. PMID 2269288 DOI: 10.1111/J.1432-1033.1990.Tb15662.X  0.688
1990 Boelens R, Ganadu ML, Verheyden P, Kaptein R. Two-dimensional NMR studies on des-pentapeptide-insulin. Proton resonance assignments and secondary structure analysis. European Journal of Biochemistry / Febs. 191: 147-53. PMID 2199196 DOI: 10.1111/J.1432-1033.1990.Tb19104.X  0.633
1990 Härd T, Kellenbach E, Boelens R, Maler BA, Dahlman K, Freedman LP, Carlstedt-Duke J, Yamamoto KR, Gustafsson JA, Kaptein R. Solution structure of the glucocorticoid receptor DNA-binding domain. Science (New York, N.Y.). 249: 157-60. PMID 2115209 DOI: 10.1126/Science.2115209  0.71
1990 Padilla A, Vuister GW, Boelens R, Kleywegt GJ, Cave A, Parello J, Kaptein R. Homonuclear three-dimensional proton NMR spectroscopy of pike parvalbumin. Comparison of short- and medium-range NOEs from 2D and 3D NMR Journal of the American Chemical Society. 112: 5024-5030. DOI: 10.1021/Ja00169A005  0.796
1990 De Waard P, Boelens R, Vuister GW, Vliegenthart JFG. Structural studies by proton/carbon-13 two-dimensional and three-dimensional HMQC-NOE at natural abundance on complex carbohydrates Journal of the American Chemical Society. 112: 3232-3234. DOI: 10.1021/ja00164a066  0.692
1990 De Waard P, Boelens R, Vuister GW, Vliegenthart JFG. Structural studies by 1HX13C two-dimensional and three-dimensional HMQC-NOE at natural abundance on complex carbohydrates Journal of the American Chemical Society. 112: 3232-3234. DOI: 10.1021/Ja00164A066  0.681
1990 Koning TMG, Boelens R, Kaptein R. Calculation of the nuclear overhauser effect and the determination of proton-proton distances in the presence of internal motions Journal of Magnetic Resonance (1969). 90: 111-123. DOI: 10.1016/0022-2364(90)90369-K  0.597
1990 Breg JN, Boelens R, Vuister GW, Kaptein R. 3D NOE-NOE spectroscopy of proteins. Observation of sequential 3D NOE cross peaks in arc repressor Journal of Magnetic Resonance (1969). 87: 646-651. DOI: 10.1016/0022-2364(90)90324-3  0.791
1990 Kleywegt GJ, Boelens R, Kaptein R. A versatile approach toward the partially automatic recognition of cross peaks in 2D 1H NMR spectra Journal of Magnetic Resonance (1969). 88: 601-608. DOI: 10.1016/0022-2364(90)90291-G  0.722
1989 Mayo KH, Cavalli RC, Peters AR, Boelens R, Kaptein R. Sequence-specific 1H-n.m.r. assignments and peptide backbone conformation in rat epidermal growth factor. The Biochemical Journal. 257: 197-205. PMID 2784052 DOI: 10.1042/Bj2570197  0.616
1989 Lamerichs RM, Padilla A, Boelens R, Kaptein R, Ottleben G, Rüterjans H, Granger-Schnarr M, Oertel P, Schnarr M. The amino-terminal domain of LexA repressor is alpha-helical but differs from canonical helix-turn-helix proteins: a two-dimensional 1H NMR study. Proceedings of the National Academy of Sciences of the United States of America. 86: 6863-7. PMID 2780544 DOI: 10.1073/Pnas.86.18.6863  0.688
1989 Fisher J, Primrose WU, Roberts GC, Dekker N, Boelens R, Kaptein R, Slotboom AJ. 1H NMR studies of bovine and porcine phospholipase A2: assignment of aromatic resonances and evidence for a conformational equilibrium in solution. Biochemistry. 28: 5939-46. PMID 2775744 DOI: 10.1021/Bi00440A034  0.657
1989 Lamerichs RM, Boelens R, van der Marel GA, van Boom JH, Kaptein R, Buck F, Fera B, Rüterjans H. H NMR study of a complex between the lac repressor headpiece and a 22 base pair symmetric lac operator. Biochemistry. 28: 2985-91. PMID 2742823 DOI: 10.1021/Bi00433A037  0.65
1989 Breg JN, Boelens R, George AV, Kaptein R. Sequence-specific 1H NMR assignment and secondary structure of the Arc repressor of bacteriophage P22, as determined by two-dimensional 1H NMR spectroscopy. Biochemistry. 28: 9826-33. PMID 2611268 DOI: 10.1021/Bi00451A042  0.695
1989 De Marco A, Petros AM, Llinás M, Kaptein R, Boelens R. Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy. Biochimica Et Biophysica Acta. 994: 121-37. PMID 2535939 DOI: 10.1016/0167-4838(89)90151-9  0.663
1989 Boelens R, Vuister GW, Koning TMG, Kaptein R. Observation of spin-diffusion in biomolecules by three-dimensional NOE-NOE spectroscopy Journal of the American Chemical Society. 111: 8525-8526. DOI: 10.1021/ja00204a039  0.541
1989 Boelens R, Vuister GW, Koning TMG, Kaptein R. Observation of spin diffusion in biomolecules by three-dimensional NOE-NOE spectroscopy Journal of the American Chemical Society®. 111: 8525-8526. DOI: 10.1021/Ja00204A039  0.761
1989 Vuister GW, De Waard P, Boelens R, Vliegenthart JFG, Kaptein R. The use of three-dimensional NMR in structural studies of oligosaccharides Journal of the American Chemical Society. 111: 772-774. DOI: 10.1021/ja00184a078  0.786
1989 Vuister GW, De Waard P, Boelens R, Vliegenthart JFG, Kaptein R. The use of 3D NMR in structural studies of oligosaccharides Journal of the American Chemical Society. 111: 772-774. DOI: 10.1021/Ja00184A078  0.784
1989 Kleywegt GJ, Lamerichs RMJN, Boelens R, Kaptein R. Toward automatic assignment of protein 1H NMR spectra Journal of Magnetic Resonance (1969). 85: 186-197. DOI: 10.1016/0022-2364(89)90335-1  0.734
1989 Boelens R, Koning TMG, van der Marel GA, van Boom JH, Kaptein R. Iterative procedure for structure determination from proton-proton NOEs using a full relaxation matrix approach. Application to a DNA octamer Journal of Magnetic Resonance (1969). 82: 290-308. DOI: 10.1016/0022-2364(89)90032-2  0.643
1989 Kosasi S, van der Sluis W, Boelens R, Hart L, Labadie R. Labaditin, a novel cyclic decapeptide from the latex ofJatropha multifidaL. (Euphorbiaceae) Febs Letters. 256: 91-96. DOI: 10.1016/0014-5793(89)81724-7  0.315
1989 VUISTER GW, DE WAARD P, BOELENS R, VLIEGENTHART JFG, KAPTEIN R. ChemInform Abstract: The Use of 3D NMR in Structural Studies of Oligosaccharides Cheminform. 20. DOI: 10.1002/chin.198919060  0.784
1988 Pepermans H, Tourwé D, Van Binst G, Boelens R, Scheek RM, Van Gunsteren WF, Kaptein R. The combined use of NMR, distance geometry, and restrained molecular dynamics for the conformational study of a cyclic somatostatin analogue. Biopolymers. 27: 323-38. PMID 3359005 DOI: 10.1002/Bip.360270211  0.648
1988 Lamerichs RM, Berliner LJ, Boelens R, De Marco A, Llinàs M, Kaptein R. Secondary structure and hydrogen bonding of crambin in solution. A two-dimensional NMR study. European Journal of Biochemistry / Febs. 171: 307-12. PMID 3338468 DOI: 10.1111/J.1432-1033.1988.Tb13791.X  0.668
1988 Stob S, Scheek RM, Boelens R, Kaptein R. Photo-CIDNP study of the interaction between lac repressor headpiece and lac operator DNA. Febs Letters. 239: 99-104. PMID 3053247 DOI: 10.1016/0014-5793(88)80553-2  0.658
1988 Kaptein R, Boelens R, Scheek RM, van Gunsteren WF. Protein structures from NMR. Biochemistry. 27: 5389-95. PMID 3052574 DOI: 10.1021/Bi00415A001  0.675
1988 Boelens R, Koning TMG, Kaptein R. Determination of biomolecular structures from proton-proton NOE's using a relaxation matrix approach Journal of Molecular Structure. 173: 299-311. DOI: 10.1016/0022-2860(88)80062-0  0.627
1988 Vuister GW, Boelens R, Kaptein R. Nonselective three-dimensional nmr spectroscopy. The 3D NOE-HOHAHA experiment Journal of Magnetic Resonance (1969). 80: 176-185. DOI: 10.1016/0022-2364(88)90072-8  0.786
1988 Mayo KH, Schussheim A, Vuister GW, Boelens R, Kaptein R, Engelhard M, Hess B. Mobility and solvent exposure of aromatic residues in bacteriorhodopsin investigated by 1H-NMR and photo-CIDNP-NMR spectroscopy Febs Letters. 235: 163-168. DOI: 10.1016/0014-5793(88)81255-9  0.812
1988 Stob S, Scheek RM, Boelens R, Dukstra K, Kaptein R. Applications of Two-Dimensional1H NMR Methods to Photo-Chemically Induced Dynamic Nuclear Polarisation Spectroscopy Israel Journal of Chemistry. 28: 319-327. DOI: 10.1002/Ijch.198800043  0.656
1988 NUSSELDER JJH, ENGBERTS JBFN, BOELENS R, KAPTEIN R. ChemInform Abstract: Micellar Structure Studied by 2D NMR Cheminform. 19. DOI: 10.1002/chin.198826051  0.612
1987 Lautz J, Kessler H, Boelens R, Kaptein R, van Gunsteren WF. Conformational analysis of a cyclic thymopoietin-analogue by 1H n.m.r. spectroscopy and restrained molecular dynamics simulations. International Journal of Peptide and Protein Research. 30: 404-14. PMID 3692686 DOI: 10.1111/J.1399-3011.1987.Tb03348.X  0.645
1987 Boelens R, Scheek RM, van Boom JH, Kaptein R. Complex of lac repressor headpiece with a 14 base-pair lac operator fragment studied by two-dimensional nuclear magnetic resonance. Journal of Molecular Biology. 193: 213-6. PMID 3586020 DOI: 10.1016/0022-2836(87)90638-3  0.672
1987 Kemmink J, Boelens R, Kaptein R. Two-dimensional 1H NMR study of two cyclobutane type photodimers of thymidylyl-(3'----5')-thymidine. European Biophysics Journal : Ebj. 14: 293-9. PMID 3569163 DOI: 10.1007/Bf00254894  0.649
1987 Kemmink J, Boelens R, Koning T, van der Marel GA, van Boom JH, Kaptein R. 1H NMR study of the exchangeable protons of the duplex d(GCGTTGCG).d(CGCAACGC) containing a thymine photodimer. Nucleic Acids Research. 15: 4645-53. PMID 3035498 DOI: 10.1093/Nar/15.11.4645  0.647
1987 Kemmink J, Boelens R, Koning TM, Kaptein R, van der Marel GA, van Boom JH. Conformational changes in the oligonucleotide duplex d(GCGTTGCG) x d(CGCAACGC) induced by formation of a cis-syn thymine dimer. A two-dimensional NMR study. European Journal of Biochemistry / Febs. 162: 37-43. PMID 3028790 DOI: 10.1111/J.1432-1033.1987.Tb10538.X  0.674
1987 Vuister GW, Boelens R. Three-dimensional J-resolved NMR spectroscopy Journal of Magnetic Resonance (1969). 73: 328-333. DOI: 10.1016/0022-2364(87)90205-8  0.725
1987 Vermeulen JAWH, Lamerichs RMJN, Berliner LJ, De Marco A, Llinás M, Boelens R, Alleman J, Kaptein R. 1H NMR characterization of two crambin species Febs Letters. 219: 426-430. DOI: 10.1016/0014-5793(87)80265-X  0.615
1987 KEMMINK J, VUISTER GW, BOELENS R, DIJKSTRA K, KAPTEIN R. ChemInform Abstract: Nuclear Spin Coherence Transfer in Photochemical Reactions. Cheminform. 18. DOI: 10.1002/chin.198702055  0.741
1986 De Marco A, Zetta L, Petros AM, Llinás M, Boelens R, Kaptein R. Kringle 4 from human plasminogen: a proton magnetic resonance study via two-dimensional photochemically induced dynamic nuclear polarization spectroscopy. Biochemistry. 25: 7918-23. PMID 3801450 DOI: 10.1021/Bi00372A020  0.644
1986 Norton RS, Beress L, Stob S, Boelens R, Kaptein R. Photochemically induced dynamic nuclear polarisation NMR study of the aromatic residues of sea-anemone polypeptide cardiac stimulants. European Journal of Biochemistry / Febs. 157: 343-6. PMID 2872052 DOI: 10.1111/J.1432-1033.1986.Tb09674.X  0.624
1986 Kemmink J, Vuister GW, Boelens R, Dijkstra K, Kaptein R. Nuclear spin coherence transfer in photochemical reactions Journal of the American Chemical Society. 108: 5631-5633. DOI: 10.1021/Ja00278A048  0.775
1986 Boelens R, Podoplelov A, Kaptein R. Separation of net polarization and multiplet effect in coupled spin systems by two-dimensional CIDNP Journal of Magnetic Resonance (1969). 69: 116-123. DOI: 10.1016/0022-2364(86)90223-4  0.599
1986 De Vlieg J, Boelens R, Scheek RM, Kaptein R, van Gunsteren WF. Restrained Molecular Dynamics Procedure for Protein Tertiary Structure Determination from NMR Data: ALacRepressor Headpiece Structure Based on Information on J-coupling and from Presence and Absence of NOE's Israel Journal of Chemistry. 27: 181-188. DOI: 10.1002/Ijch.198600027  0.639
1985 Zuiderweg ER, Scheek RM, Boelens R, van Gunsteren WF, Kaptein R. Determination of protein structures from nuclear magnetic resonance data using a restrained molecular dynamics approach: the lac repressor DNA binding domain. Biochimie. 67: 707-15. PMID 3910108 DOI: 10.1016/S0300-9084(85)80158-9  0.785
1985 Kaptein R, Zuiderweg ER, Scheek RM, Boelens R, van Gunsteren WF. A protein structure from nuclear magnetic resonance data. lac repressor headpiece. Journal of Molecular Biology. 182: 179-82. PMID 3889346 DOI: 10.1016/0022-2836(85)90036-1  0.776
1985 Wever R, Boelens R, De Boer E, Van Gelder BF, Gorren AC, Rademaker H. The photoreactivity of the copper-NO complexes in cytochrome c oxidase and in other copper-containing proteins. Journal of Inorganic Biochemistry. 23: 227-32. PMID 2991461 DOI: 10.1016/0162-0134(85)85029-7  0.773
1985 Boelens R, Gros P, Scheek RM, Verpoorte JA, Kaptein R. Hydrogen exchange of individual amide protons in the E. coli lac repressor DNA-binding domain: a nuclear magnetic resonance study. Journal of Biomolecular Structure & Dynamics. 3: 269-80. PMID 2855972 DOI: 10.1080/07391102.1985.10508416  0.665
1985 Boelens R, Scheek RM, Dijkstra K, Kaptein R. 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 Journal of Magnetic Resonance (1969). 62: 378-386. DOI: 10.1016/0022-2364(85)90207-0  0.653
1985 Scheek RM, Stob S, Boelens R, Dijkstra K, Kaptein R. Applications of two-dimensional NMR methods in photochemically induced dynamic nuclear polarization spectroscopy Journal of the American Chemical Society. 107: 705-706. DOI: 10.1002/Chin.198524044  0.612
1985 SCHEEK RM, STOB S, BOELENS R, DIJKSTRA K, KAPTEIN R. ChemInform Abstract: APPLICATIONS OF TWO-DIMENSIONAL NMR METHODS IN PHOTOCHEMICALLY INDUCED DYNAMIC NUCLEAR POLARIZATION SPECTROSCOPY Chemischer Informationsdienst. 16. DOI: 10.1002/chin.198524044  0.574
1985 Zuiderweg ERP, Boelens R, Kaptein R. Stereospecific assignments of1H-nmr methyl lines and conformation of valyl residues in thelac repressor headpiece Biopolymers. 24: 601-611. DOI: 10.1002/Bip.360240402  0.643
1984 Moonen CT, Scheek RM, Boelens R, Müller F. The use of two-dimensional nuclear-magnetic-resonance spectroscopy and two-dimensional difference spectra in the elucidation of the active center of Megasphaera elsdenii flavodoxin. European Journal of Biochemistry / Febs. 141: 323-30. PMID 6734600 DOI: 10.1111/J.1432-1033.1984.Tb08195.X  0.368
1984 Scheek RM, Boelens R, Russo N, van Boom JH, Kaptein R. Sequential resonance assignments in 1H NMR spectra of oligonucleotides by two-dimensional NMR spectroscopy. Biochemistry. 23: 1371-6. PMID 6722097 DOI: 10.1021/Bi00302A006  0.624
1984 Zuiderweg ER, Billeter M, Boelens R, Scheek RM, Wüthrich K, Kaptein R. Spatial arrangement of the three alpha helices in the solution conformation of E. coli lac repressor DNA-binding domain. Febs Letters. 174: 243-7. PMID 6381097 DOI: 10.1016/0014-5793(84)81166-7  0.77
1984 Boelens R, Rademaker H, Wever R, Van Gelder BF. The cytochrome c oxidase-azide-nitric oxide complex as a model for the oxygen-binding site. Biochimica Et Biophysica Acta. 765: 196-209. PMID 6326819 DOI: 10.1016/0005-2728(84)90014-8  0.774
1984 Scheek RM, Stob S, Boelens R, Dijkstra K, Kaptein R. Applications of two-dimensional 1H nuclear magnetic resonance methods in photochemically induced dynamic nuclear polarisation spectroscopy Faraday Discussions of the Chemical Society. 78: 245-256. DOI: 10.1039/Dc9847800245  0.649
1983 Boelens R, Wever R, Van Gelder BF, Rademaker H. An EPR study of the photodissociation reactions of oxidised cytochrome c oxidase-nitric oxide complexes. Biochimica Et Biophysica Acta. 724: 176-83. PMID 6309220 DOI: 10.1016/0005-2728(83)90136-6  0.778
1983 SCHEEK RM, RUSSO N, BOELENS R, KAPTEIN R, VAN BOOM JH. ChemInform Abstract: SEQUENTIAL RESONANCE ASSIGNMENTS IN DNA PROTON NMR SPECTRA BY TWO-DIMENSIONAL NOE SPECTROSCOPY Chemischer Informationsdienst. 14. DOI: 10.1002/chin.198332337  0.618
1983 Scheek RM, Russo N, Boelens R, Kaptein R, Van Boom JH. Sequential resonance assignments in DNA proton NMR spectra by two-dimensional NOE spectroscopy Journal of the American Chemical Society. 105: 2914-2916. DOI: 10.1002/Chin.198332337  0.654
1982 Wever R, Kast WM, Kasinoedin JH, Boelens R. The peroxidation of thiocyanate catalysed by myeloperoxidase and lactoperoxidase. Biochimica Et Biophysica Acta. 709: 212-9. PMID 6295491 DOI: 10.1016/0167-4838(82)90463-0  0.621
1982 Boelens R, Wever R, Van Gelder BF. Electron transfer after flash photolysis of mixed-valence carboxycytochrome c oxidase. Biochimica Et Biophysica Acta. 682: 264-72. PMID 6293558 DOI: 10.1016/0005-2728(82)90107-4  0.767
1982 Boelens R, Rademaker H, Pel R, Wever R. EPR studies of the photodissociation reactions of cytochrome c oxidase-nitric oxide complexes. Biochimica Et Biophysica Acta. 679: 84-94. PMID 6275891 DOI: 10.1016/0005-2728(82)90258-4  0.632
1981 Wilms J, Dekker HL, Boelens R, van Gelder BF. The effect of pH and ionic strength on the pre-steady-state reaction of cytochrome c and cytochrome aa3. Biochimica Et Biophysica Acta. 637: 168-76. PMID 6269605 DOI: 10.1016/0005-2728(81)90223-1  0.725
1980 Boelens R, Wever R. Redox reactions in mixed-valence cytochrome c oxidase. Febs Letters. 116: 223-6. PMID 6250884 DOI: 10.1016/0014-5793(80)80649-1  0.607
1979 Boelens R, Wever R. Electron-transfer processes in carboxy-cytochrome c oxidase after photodissociation of cytochrome a3 2+ . CO. Biochimica Et Biophysica Acta. 547: 296-310. PMID 223638 DOI: 10.1016/0005-2728(79)90012-4  0.629
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