Year |
Citation |
Score |
2023 |
Romanuka J, Folkers GE, Gnida M, Kovačič L, Wienk H, Kaptein R, Boelens R. Genetic switching by the Lac repressor is based on two-state Monod-Wyman-Changeux allostery. Proceedings of the National Academy of Sciences of the United States of America. 120: e2311240120. PMID 38019859 DOI: 10.1073/pnas.2311240120 |
0.718 |
|
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 |
0.576 |
|
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 |
0.793 |
|
2015 |
Pravdivtsev AN, Ivanov KL, Yurkovskaya AV, Petrov PA, Limbach HH, Kaptein R, Vieth HM. Spin polarization transfer mechanisms of SABRE: A magnetic field dependent study. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 261: 73-82. PMID 26529205 DOI: 10.1016/j.jmr.2015.10.006 |
0.329 |
|
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 |
0.714 |
|
2015 |
Kaptein R, Wagner G. NMR studies of membrane proteins. Journal of Biomolecular Nmr. 61: 181-4. PMID 25840906 DOI: 10.1007/s10858-015-9918-7 |
0.339 |
|
2013 |
Pravdivtsev AN, Yurkovskaya AV, Vieth HM, Ivanov KL, Kaptein R. Level anti-crossings are a key factor for understanding para-hydrogen-induced hyperpolarization in SABRE experiments. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 14: 3327-31. PMID 23959909 DOI: 10.1002/cphc.201300595 |
0.335 |
|
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 |
0.742 |
|
2013 |
Kaptein R. NMR studies on protein-nucleic acid interaction. Journal of Biomolecular Nmr. 56: 1-2. PMID 23657842 DOI: 10.1007/s10858-013-9736-8 |
0.339 |
|
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 |
0.67 |
|
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 |
0.669 |
|
2012 |
Dyakonova ES, Koval VV, Ishchenko AA, Saparbaev MK, Kaptein R, Fedorova OS. Kinetic mechanism of the interaction of Saccharomyces cerevisiae AP-endonuclease 1 with DNA substrates. Biochemistry. Biokhimii͡A. 77: 1162-71. PMID 23157296 DOI: 10.1134/S0006297912100082 |
0.336 |
|
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 |
0.745 |
|
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 |
0.814 |
|
2012 |
Boelens R, Kaptein R. ChemInform Abstract: Homonuclear 3D NMR of Biomolecules Cheminform. 43: no-no. DOI: 10.1002/chin.201236269 |
0.597 |
|
2011 |
Kaptein R. A Tribute to Renad Z. Sagdeev on the Occasion of His 70th Birthday. Applied Magnetic Resonance. 41: 111-112. PMID 22162913 DOI: 10.1007/s00723-011-0287-4 |
0.305 |
|
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 |
0.614 |
|
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 |
0.635 |
|
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 |
0.789 |
|
2009 |
Wienk H, Lammers I, Hotze A, Wu J, Wechselberger RW, Owens R, Stammers DK, Stuart D, Kaptein R, Folkers GE. The tandem zinc-finger region of human ZHX adopts a novel C2H2 zinc finger structure with a C-terminal extension. Biochemistry. 48: 4431-9. PMID 19348505 DOI: 10.1021/bi9001997 |
0.588 |
|
2008 |
Diercks T, AB E, Daniels MA, de Jong RN, Besseling R, Kaptein R, Folkers GE. Solution structure and characterization of the DNA-binding activity of the B3BP-Smr domain. Journal of Molecular Biology. 383: 1156-70. PMID 18804481 DOI: 10.1016/j.jmb.2008.09.005 |
0.609 |
|
2008 |
de Jong RN, Truffault V, Diercks T, Ab E, Daniels MA, Kaptein R, Folkers GE. Structure and DNA binding of the human Rtf1 Plus3 domain. Structure (London, England : 1993). 16: 149-59. PMID 18184592 DOI: 10.1016/j.str.2007.10.018 |
0.589 |
|
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 |
0.799 |
|
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 |
0.808 |
|
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 |
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 |
0.792 |
|
2006 |
de Jong RN, Daniëls MA, Kaptein R, Folkers GE. Enzyme free cloning for high throughput gene cloning and expression. Journal of Structural and Functional Genomics. 7: 109-18. PMID 17295099 DOI: 10.1007/s10969-006-9014-z |
0.483 |
|
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 |
0.791 |
|
2006 |
Au K, Berrow NS, Blagova E, Boucher IW, Boyle MP, Brannigan JA, Carter LG, Dierks T, Folkers G, Grenha R, Harlos K, Kaptein R, Kalliomaa AK, Levdikov VM, Meier C, et al. Application of high-throughput technologies to a structural proteomics-type analysis of Bacillus anthracis. Acta Crystallographica. Section D, Biological Crystallography. 62: 1267-75. PMID 17001104 DOI: 10.1107/S0907444906033555 |
0.544 |
|
2006 |
Ab E, Atkinson AR, Banci L, Bertini I, Ciofi-Baffoni S, Brunner K, Diercks T, Dötsch V, Engelke F, Folkers GE, Griesinger C, Gronwald W, Günther U, Habeck M, de Jong RN, ... ... Kaptein R, et al. NMR in the SPINE Structural Proteomics project. Acta Crystallographica. Section D, Biological Crystallography. 62: 1150-61. PMID 17001092 DOI: 10.1107/S0907444906032070 |
0.598 |
|
2006 |
Grenha R, Rzechorzek NJ, Brannigan JA, de Jong RN, Ab E, Diercks T, Truffault V, Ladds JC, Fogg MJ, Bongiorni C, Perego M, Kaptein R, Wilson KS, Folkers GE, Wilkinson AJ. Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli. The Journal of Biological Chemistry. 281: 37993-8003. PMID 17001075 DOI: 10.1074/jbc.M607617200 |
0.569 |
|
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 |
0.794 |
|
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 |
0.68 |
|
2006 |
Jonker HR, Wechselberger RW, Pinkse M, Kaptein R, Folkers GE. Gradual phosphorylation regulates PC4 coactivator function. The Febs Journal. 273: 1430-44. PMID 16689930 DOI: 10.1111/j.1742-4658.2006.05165.x |
0.539 |
|
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 |
0.753 |
|
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 |
0.795 |
|
2006 |
de Jong RN, Ab E, Diercks T, Truffault V, Daniëls M, Kaptein R, Folkers GE. Solution structure of the human ubiquitin-specific protease 15 DUSP domain. The Journal of Biological Chemistry. 281: 5026-31. PMID 16298993 DOI: 10.1074/jbc.M510993200 |
0.578 |
|
2006 |
Hsu STD, Breukink E, Kaptein R. Structural motifs of lipid II-binding lantibiotics as a blueprint for novel antibiotics Anti-Infective Agents in Medicinal Chemistry. 5: 245-254. DOI: 10.2174/187152106777697880 |
0.311 |
|
2006 |
Grenha R, Rzechorzek NJ, Brannigan JA, Ab E, Folkers GE, Jong RND, Diercks T, Wilkinson AJ, Kaptein R, Wilson KS. Nmr Solution Structure Of A Protein Aspartic Acid Phosphate Phosphatase From Bacillus Anthracis Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr7349 |
0.586 |
|
2005 |
Diercks T, Daniels M, Kaptein R. Extended flip-back schemes for sensitivity enhancement in multidimensional HSQC-type out-and-back experiments. Journal of Biomolecular Nmr. 33: 243-59. PMID 16341753 DOI: 10.1007/s10858-005-3868-4 |
0.327 |
|
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 |
0.8 |
|
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 |
0.804 |
|
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 |
0.8 |
|
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 |
0.809 |
|
2005 |
Patterson HM, Brannigan JA, Cutting SM, Wilson KS, Wilkinson AJ, Ab E, Diercks T, de Jong RN, Truffault V, Folkers GE, Kaptein R. The structure of bypass of forespore C, an intercompartmental signaling factor during sporulation in Bacillus. The Journal of Biological Chemistry. 280: 36214-20. PMID 16049010 DOI: 10.1074/jbc.M506910200 |
0.55 |
|
2005 |
Doreleijers JF, Nederveen AJ, Vranken W, Lin J, Bonvin AM, Kaptein R, Markley JL, Ulrich EL. BioMagResBank databases DOCR and FRED containing converted and filtered sets of experimental NMR restraints and coordinates from over 500 protein PDB structures. Journal of Biomolecular Nmr. 32: 1-12. PMID 16041478 DOI: 10.1007/S10858-005-2195-0 |
0.693 |
|
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 |
0.686 |
|
2005 |
Nederveen AJ, Doreleijers JF, Vranken W, Miller Z, Spronk CA, Nabuurs SB, Güntert P, Livny M, Markley JL, Nilges M, Ulrich EL, Kaptein R, Bonvin AM. RECOORD: a recalculated coordinate database of 500+ proteins from the PDB using restraints from the BioMagResBank. Proteins. 59: 662-72. PMID 15822098 DOI: 10.1002/Prot.20408 |
0.72 |
|
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 |
0.729 |
|
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 |
0.609 |
|
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 |
0.597 |
|
2004 |
Hsu ST, Breukink E, Tischenko E, Lutters MA, de Kruijff B, Kaptein R, Bonvin AM, van Nuland NA. The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics. Nature Structural & Molecular Biology. 11: 963-7. PMID 15361862 DOI: 10.1038/Nsmb830 |
0.683 |
|
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 |
0.802 |
|
2004 |
Folkers GE, van Buuren BN, Kaptein R. Expression screening, protein purification and NMR analysis of human protein domains for structural genomics. Journal of Structural and Functional Genomics. 5: 119-31. PMID 15263851 DOI: 10.1023/B:JSFG.0000029200.66197.0c |
0.555 |
|
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 |
0.811 |
|
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 |
0.819 |
|
2004 |
Hsu S, Breukink E, Tischenko E, Lutters M, Kruijff Bd, Kaptein R, Bonvin A, Nuland Nv. The pyrophosphate cage: the structure of the nisin/lipid II complex provides a blueprint for novel antibiotics Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb1Uzt/Pdb |
0.778 |
|
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 |
0.811 |
|
2003 |
Siebert HC, André S, Lu SY, Frank M, Kaltner H, van Kuik JA, Korchagina EY, Bovin N, Tajkhorshid E, Kaptein R, Vliegenthart JF, von der Lieth CW, Jiménez-Barbero J, Kopitz J, Gabius HJ. Unique conformer selection of human growth-regulatory lectin galectin-1 for ganglioside GM1 versus bacterial toxins. Biochemistry. 42: 14762-73. PMID 14674750 DOI: 10.1021/Bi035477C |
0.386 |
|
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 |
0.659 |
|
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 |
0.798 |
|
2003 |
Stockner T, Sterk H, Kaptein R, Bonvin AM. Molecular dynamics studies of a molecular switch in the glucocorticoid receptor. Journal of Molecular Biology. 328: 325-34. PMID 12691744 DOI: 10.1016/S0022-2836(03)00316-4 |
0.737 |
|
2003 |
Hsu ST, Breukink E, Bierbaum G, Sahl HG, de Kruijff B, Kaptein R, van Nuland NA, Bonvin AM. NMR study of mersacidin and lipid II interaction in dodecylphosphocholine micelles. Conformational changes are a key to antimicrobial activity. The Journal of Biological Chemistry. 278: 13110-7. PMID 12562773 DOI: 10.1074/Jbc.M211144200 |
0.708 |
|
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 |
0.646 |
|
2003 |
Hsu S, Breukink E, Bierbaum G, Sahl H, Kruijff Bd, Kaptein R, Nuland Nv, Bonvin A. NMR solution structure of type-B lantibiotics mersacidin in DPC micelles Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb1Mqy/Pdb |
0.793 |
|
2003 |
Hsu S, Breukink E, Bierbaum G, Sahl H, Kruijff Bd, Kaptein R, Nuland Nv, Bonvin A. NMR solution structure of type-B lantibiotics mersacidin in MeOH/H2O mixture Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr5581 |
0.795 |
|
2003 |
Hsu S, Breukink E, Bierbaum G, Sahl H, Kruijff Bd, Kaptein R, Nuland Nv, Bonvin A. NMR solution structure of type-B lantibiotics mersacidin bound to lipid II in DPC micelles Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr5580 |
0.791 |
|
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 |
0.826 |
|
2002 |
Siebert HC, Lü SY, Frank M, Kramer J, Wechselberger R, Joosten J, André S, Rittenhouse-Olson K, Roy R, von der Lieth CW, Kaptein R, Vliegenthart JF, Heck AJ, Gabius HJ. Analysis of protein-carbohydrate interaction at the lower size limit of the protein part (15-mer peptide) by NMR spectroscopy, electrospray ionization mass spectrometry, and molecular modeling. Biochemistry. 41: 9707-17. PMID 12135393 DOI: 10.1021/Bi025891X |
0.395 |
|
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 |
0.81 |
|
2002 |
Hsu ST, Breukink E, de Kruijff B, Kaptein R, Bonvin AM, van Nuland NA. Mapping the targeted membrane pore formation mechanism by solution NMR: the nisin Z and lipid II interaction in SDS micelles. Biochemistry. 41: 7670-6. PMID 12056898 DOI: 10.1021/Bi025679T |
0.704 |
|
2002 |
D'Amelio N, Bonvin AM, Czisch M, Barker P, Kaptein R. The C terminus of apocytochrome b562 undergoes fast motions and slow exchange among ordered conformations resembling the folded state. Biochemistry. 41: 5505-14. PMID 11969411 DOI: 10.1021/Bi011863N |
0.732 |
|
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 |
0.818 |
|
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 |
0.768 |
|
2002 |
D'Amelio N, Bonvin A, Czisch M, Barker P, Kaptein R. 1Ha and 13Ca, 13Cb shifts of apocytochrome b562 at pH 5.1 (temperature 293 K) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4767 |
0.627 |
|
2001 |
Raves ML, Doreleijers JF, Vis H, Vorgias CE, Wilson KS, Kaptein R. Joint refinement as a tool for thorough comparison between NMR and x-ray data and structures of HU protein Journal of Biomolecular Nmr. 21: 235-248. PMID 11775740 DOI: 10.1023/A:1012927325963 |
0.358 |
|
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 |
0.785 |
|
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 |
0.811 |
|
2001 |
Wüthrich K, Bax A, Billeter M, Kaptein R, Palmer AG, Sykes BD, Wagner G. Letter from the Editor-in-Chief Journal of Biomolecular Nmr. 19: 1. DOI: 10.1023/A:1008382926453 |
0.445 |
|
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 |
0.754 |
|
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 |
0.638 |
|
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 |
0.666 |
|
2000 |
Boetzel R, Czisch M, Kaptein R, Hemmings AM, James R, Kleanthous C, Moore GR. NMR investigation of the interaction of the inhibitor protein Im9 with its partner DNase. Protein Science : a Publication of the Protein Society. 9: 1709-18. PMID 11045617 DOI: 10.1110/Ps.9.9.1709 |
0.468 |
|
2000 |
Arnesano F, Banci L, Bertini I, Van Der Wetering K, Czisch M, Kaptein R. The auto-orientation in high magnetic fields of oxidized cytochrome b562 as source of constraints for solution structure determination. Journal of Biomolecular Nmr. 17: 295-304. PMID 11014593 DOI: 10.1023/A:1008308501053 |
0.3 |
|
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 |
0.664 |
|
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 |
0.813 |
|
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 |
0.796 |
|
2000 |
Whittaker SB, Czisch M, Wechselberger R, Kaptein R, Hemmings AM, James R, Kleanthous C, Moore GR. Slow conformational dynamics of an endonuclease persist in its complex with its natural protein inhibitor. Protein Science : a Publication of the Protein Society. 9: 713-20. PMID 10794413 DOI: 10.1110/Ps.9.4.713 |
0.434 |
|
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 |
0.809 |
|
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 |
0.778 |
|
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 |
0.681 |
|
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 |
0.779 |
|
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 |
0.814 |
|
1999 |
Doreleijers JF, Raves ML, Rullmann T, Kaptein R. Completeness of NOEs in protein structure: a statistical analysis of NMR. Journal of Biomolecular Nmr. 14: 123-32. PMID 10610141 DOI: 10.1023/A:1008335423527 |
0.397 |
|
1999 |
Doreleijers JF, Vriend G, Raves ML, Kaptein R. Validation of nuclear magnetic resonance structures of proteins and nucleic acids: hydrogen geometry and nomenclature. Proteins. 37: 404-16. PMID 10591100 DOI: 10.1002/(SICI)1097-0134(19991115)37:3<404::AID-PROT8>3.0.CO;2-2 |
0.379 |
|
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 |
0.717 |
|
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 |
0.702 |
|
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 |
0.67 |
|
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 |
0.817 |
|
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 |
0.824 |
|
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 |
0.812 |
|
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 |
0.788 |
|
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 |
0.678 |
|
1998 |
Boetzel R, Czisch M, MacDonald CJ, Kaptein R, Hemmings AM, James R, Kleanthous C, Moore GR. Assignment of 1H, 13C and 15N signals of the inhibitor protein Im9 bound to the DNase domain of colicin E9. Journal of Biomolecular Nmr. 12: 567-8. PMID 9917143 DOI: 10.1023/A:1008397523780 |
0.319 |
|
1998 |
Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K. Recommendations for the presentation of NMR structures of proteins and nucleic acids--IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy. European Journal of Biochemistry / Febs. 256: 1-15. PMID 9746340 DOI: 10.1046/J.1432-1327.1998.2560001.X |
0.717 |
|
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 |
Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K. Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy. Journal of Biomolecular Nmr. 12: 1-23. PMID 9729785 DOI: 10.1023/A:1008290618449 |
0.717 |
|
1998 |
Doreleijers JF, Rullmann JA, Kaptein R. Quality assessment of NMR structures: a statistical survey. Journal of Molecular Biology. 281: 149-64. PMID 9680482 DOI: 10.1006/jmbi.1998.1808 |
0.338 |
|
1998 |
Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K. Recommendations for the presentation of NMR structures of proteins and nucleic acids. Journal of Molecular Biology. 280: 933-52. PMID 9671561 DOI: 10.1006/Jmbi.1998.1852 |
0.712 |
|
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 |
0.807 |
|
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 |
0.641 |
|
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 |
0.612 |
|
1998 |
Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K. Recommendations for the presentation of NMR structures of proteins and nucleic acids (IUPAC Recommendations 1998) Pure and Applied Chemistry. 70: 117-142. DOI: 10.1351/Pac199870010117 |
0.717 |
|
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 |
0.625 |
|
1998 |
Vis H, Vorgias CE, Wilson KS, Kaptein R, Boelens R. Journal of Biomolecular Nmr. 11: 265-277. DOI: 10.1023/A:1008208615714 |
0.56 |
|
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 |
0.789 |
|
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 |
Siebert HC, André S, Reuter G, Kaptein R, Vliegenthart JF, Gabius HJ. Comparison between intact and desialylated human serum amyloid P component by laser photo CIDNP (chemically induced dynamic nuclear polarization) technique: an indication for a conformational impact of sialic acid. Glycoconjugate Journal. 14: 945-9. PMID 9486427 DOI: 10.1023/A:1018570912192 |
0.32 |
|
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 |
Siebert HC, Adar R, Arango R, Burchert M, Kaltner H, Kayser G, Tajkhorshid E, von der Lieth CW, Kaptein R, Sharon N, Vliegenthart JF, Gabius HJ. Involvement of laser photo-CIDNP (chemically induced dynamic nuclear polarization)-reactive amino acid side chains in ligand binding by galactoside-specific lectins in solution. European Journal of Biochemistry / Febs. 249: 27-38. PMID 9363750 DOI: 10.1111/J.1432-1033.1997.00027.X |
0.404 |
|
1997 |
Siebert HC, Kaptein R, Beintema JJ, Soedjanaatmadja UM, Wright CS, Rice A, Kleineidam RG, Kruse S, Schauer R, Pouwels PJ, Kamerling JP, Gabius HJ, Vliegenthart JF. Carbohydrate-protein interaction studies by laser photo CIDNP NMR methods. Glycoconjugate Journal. 14: 531-4. PMID 9249155 DOI: 10.1023/A:1018572023153 |
0.419 |
|
1997 |
Siebert HC, von der Lieth CW, Kaptein R, Beintema JJ, Dijkstra K, van Nuland N, Soedjanaatmadja UM, Rice A, Vliegenthart JF, Wright CS, Gabius HJ. Role of aromatic amino acids in carbohydrate binding of plant lectins: laser photo chemically induced dynamic nuclear polarization study of hevein domain-containing lectins. Proteins. 28: 268-84. PMID 9188743 DOI: 10.1002/(Sici)1097-0134(199706)28:2<268::Aid-Prot14>3.0.Co;2-G |
0.425 |
|
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 |
0.694 |
|
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 |
0.677 |
|
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 |
0.792 |
|
1997 |
Tajkhorshid E, Siebert HC, Burchert M, Kaltner H, Kayser G, Von Der Lieth CW, Kaptein R, Vliegenthart JFG, Gabius HJ. A combined molecular modelling and CIDNP study of similarities in the pattern of ligand binding in mammalian and avian galectins Journal of Molecular Modeling. 3: 325-331. DOI: 10.1007/S008940050046 |
0.343 |
|
1997 |
Düx P, Whitehead B, Boelens R, Kaptein R, Vuister GW. Measurement of 15N-1H coupling constants in uniformly 15N-labeled proteins: Application to the photoactive yellow protein Journal of Biomolecular Nmr. 10: 301-306. |
0.678 |
|
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 |
0.812 |
|
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 |
0.681 |
|
1996 |
Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. Journal of Biomolecular Nmr. 8: 477-86. PMID 9008363 DOI: 10.1007/Bf00228148 |
0.397 |
|
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 |
0.656 |
|
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 |
0.61 |
|
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 |
0.648 |
|
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 |
0.679 |
|
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 |
0.82 |
|
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 |
0.619 |
|
1996 |
Dumoulin P, Ebright RH, Knegtel R, Kaptein R, Granger-Schnarr M, Schnarr M. Structure of the LexA repressor-DNA complex probed by affinity cleavage and affinity photo-cross-linking. Biochemistry. 35: 4279-86. PMID 8605176 DOI: 10.1021/Bi9529162 |
0.406 |
|
1996 |
Gates CM, Stemmer WP, Kaptein R, Schatz PJ. Affinity selective isolation of ligands from peptide libraries through display on a lac repressor "headpiece dimer". Journal of Molecular Biology. 255: 373-86. PMID 8568883 DOI: 10.1006/jmbi.1996.0031 |
0.33 |
|
1996 |
von der Lieth C, Siebert H, Tajkhorshid E, Kruse S, Schauer R, Kaptein R, Gabius H, Kleineidam RG, Vliegenthart JFG. Knowledge-based Homology Modeling and Experimental Determination of Amino Acid Side Chain Accessibility by the Laser Photo CIDNP (Chemically Induced Dynamic Nuclear Polarization) Approach in Solution: Lessons from the Small Sialidase of Clostridium perfringens Journal of Molecular Modeling. 2: 446-455. DOI: 10.1007/S0089460020446 |
0.393 |
|
1996 |
Siebert H, vonderLieth C, Kaptein R, Soedjanaatmadja U, Vliegenthart J, Wright C, Gabius H. Role of aromatic amino acids in carbohydrate binding, laser photo CIDNP (chemically induced dynamic nuclear polarisation) and molecular modeling study of hevein-domain containing lectins Journal of Molecular Modeling. 2: 351-353. DOI: 10.1007/S0089460020351 |
0.323 |
|
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 |
0.669 |
|
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 |
0.636 |
|
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 |
0.7 |
|
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 |
0.711 |
|
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 |
0.683 |
|
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 |
0.687 |
|
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 |
0.687 |
|
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 |
0.681 |
|
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 |
0.815 |
|
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 |
0.669 |
|
1995 |
Siebert HC, André S, Reuter G, Gabius HJ, Kaptein R, Vliegenthart JF. Effect of enzymatic desialylation of human serum amyloid P component on surface exposure of laser photo CIDNP (chemically induced dynamic nuclear polarization)--reactive histidine, tryptophan and tyrosine residues. Febs Letters. 371: 13-6. PMID 7664874 DOI: 10.1016/0014-5793(95)00845-Z |
0.308 |
|
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 |
0.632 |
|
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 |
0.671 |
|
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 |
0.717 |
|
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 |
0.673 |
|
1995 |
Pouwels PJ, Hartman RF, Rose SD, Kaptein R. Photo-CIDNP study of pyrimidine dimer splitting. I: Reactions involving pyrimidine radical cation intermediates. Photochemistry and Photobiology. 61: 563-74. PMID 7568403 DOI: 10.1111/j.1751-1097.1995.tb09871.x |
0.304 |
|
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 |
0.656 |
|
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 |
0.667 |
|
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 |
0.658 |
|
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 |
0.671 |
|
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 |
0.626 |
|
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 |
0.645 |
|
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 |
0.78 |
|
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 |
0.68 |
|
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 |
0.67 |
|
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 |
0.806 |
|
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 |
0.713 |
|
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 |
0.644 |
|
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 |
0.703 |
|
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 |
0.699 |
|
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 |
0.626 |
|
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 |
0.663 |
|
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 |
0.67 |
|
1994 |
Pouwels PJW, Kaptein R. Photo-CIDNP study of the splitting of the dinucleotide cis, syn-thymine dimer with reduced flavin as a sensitizer: Evidence for a thymine radical anion intermediate Applied Magnetic Resonance. 7: 107-113. DOI: 10.1007/Bf03162551 |
0.349 |
|
1994 |
Zhdanov R, Kaptein R. Sequence-dependent DNA conformation and DNA-phospholipid recognition Applied Magnetic Resonance. 7: IX-XII. DOI: 10.1007/BF03162543 |
0.334 |
|
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 |
0.631 |
|
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 |
0.665 |
|
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 |
0.716 |
|
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 |
0.692 |
|
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 |
0.793 |
|
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 |
0.786 |
|
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 |
0.647 |
|
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 |
0.803 |
|
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 |
0.692 |
|
1993 |
Kaptein R. Protein-nucleic acid interaction by NMR Current Opinion in Structural Biology. 3: 50-56. DOI: 10.1016/0959-440X(93)90201-U |
0.45 |
|
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 |
0.626 |
|
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 |
0.806 |
|
1992 |
Blommers MJ, Lucasius CB, Kateman G, Kaptein R. Conformational analysis of a dinucleotide photodimer with the aid of the genetic algorithm. Biopolymers. 32: 45-52. PMID 1617149 DOI: 10.1002/BIP.360320107 |
0.347 |
|
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 |
0.672 |
|
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 |
0.782 |
|
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 |
0.673 |
|
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 |
0.674 |
|
1992 |
Kaptein R. Zinc-finger structures Current Opinion in Structural Biology. 2: 109-115. DOI: 10.1016/0959-440X(92)90185-A |
0.322 |
|
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 |
0.772 |
|
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 |
0.6 |
|
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 |
0.678 |
|
1991 |
Koning TMG, Van Soest JJG, Kaptein R. NMR studies of bipyrimidine cyclobutane photodimers European Journal of Biochemistry. 195: 29-40. PMID 1991475 DOI: 10.1111/j.1432-1033.1991.tb15672.x |
0.345 |
|
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 |
0.643 |
|
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 |
0.628 |
|
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 |
0.669 |
|
1991 |
Snel MM, Kaptein R, de Kruijff B. Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl sulfate micelles monitored by photochemically induced dynamic nuclear polarization 1H NMR and fluorescence spectroscopy. Biochemistry. 30: 3387-95. PMID 1849424 DOI: 10.1021/BI00228A005 |
0.371 |
|
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 |
0.809 |
|
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 |
0.784 |
|
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 |
0.733 |
|
1991 |
Ottleben G, Messori L, Rüterjans H, Kaptein R, Granger-Schnarr M, Schnarr M. 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator. Journal of Biomolecular Structure & Dynamics. 9: 447-461. PMID 1815638 DOI: 10.1080/07391102.1991.10507928 |
0.455 |
|
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 |
0.633 |
|
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 |
0.684 |
|
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 |
0.766 |
|
1991 |
Kaptein R. Zinc fingers Current Opinion in Structural Biology. 1: 63-70. DOI: 10.1016/0959-440X(91)90013-J |
0.385 |
|
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 |
0.593 |
|
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 |
0.651 |
|
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 |
0.697 |
|
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 |
0.686 |
|
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 |
0.813 |
|
1990 |
Koning TMG, Davies RJH, Kaptein R. The solution structure of the intramolecular photoproduct of d(TpA) derived with the use of NMR and a combination of distance geometry and molecular dynamics Nucleic Acids Research. 18: 277-284. PMID 2326164 DOI: 10.1093/Nar/18.2.277 |
0.399 |
|
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 |
0.658 |
|
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 |
0.694 |
|
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 |
0.646 |
|
1990 |
Pieters JM, de Vroom E, van der Marel GA, van Boom JH, Koning TM, Kaptein R, Altona C. Hairpin structures in DNA containing arabinofuranosylcytosine. A combination of nuclear magnetic resonance and molecular dynamics. Biochemistry. 29: 788-99. PMID 2159791 DOI: 10.1021/Bi00455A029 |
0.402 |
|
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 |
0.712 |
|
1990 |
Berliner LJ, Kaptein R, Koga K, Musci G. NMR studies of the structure and environment of the milk protein alpha-lactalbumin. Basic Life Sciences. 56: 231-53. PMID 2078172 DOI: 10.1007/978-1-4684-5868-8_13 |
0.324 |
|
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 |
0.8 |
|
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 |
0.611 |
|
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 |
0.794 |
|
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 |
0.727 |
|
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 |
0.623 |
|
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 |
0.691 |
|
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 |
0.658 |
|
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 |
0.656 |
|
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 |
0.704 |
|
1989 |
Scheek RM, van Gunsteren WF, Kaptein R. Molecular dynamics simulation techniques for determination of molecular structures from nuclear magnetic resonance data. Methods in Enzymology. 177: 204-18. PMID 2607980 DOI: 10.1016/0076-6879(89)77012-9 |
0.355 |
|
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 |
0.675 |
|
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 |
0.767 |
|
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 |
0.56 |
|
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 |
0.787 |
|
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 |
0.788 |
|
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 |
0.739 |
|
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 |
0.656 |
|
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 |
0.788 |
|
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 |
0.66 |
|
1988 |
Endo T, Oya M, Kaptein R, Vuister GW, Kihara H, Mohri N, Tanaka S, Ohno M. Proton NMR resonance assignments and surface accessibility of tryptophan residues of a dimeric phospholipase A2 from Trimeresurus flavoviridis. Febs Letters. 230: 57-60. PMID 3350151 DOI: 10.1016/0014-5793(88)80641-0 |
0.73 |
|
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 |
0.677 |
|
1988 |
Kemmink J, Eker APM, van der Marel GA, van Boom JH, Kaptein R. Photoreactivation of the thymine dimer containing DNA octamer d(GCGT TGCG)·d(CGCAACGC) by the photoreactivating enzyme from Anacystis nidulans Journal of Photochemistry and Photobiology, B: Biology. 1: 323-328. PMID 3149667 DOI: 10.1016/1011-1344(88)85020-6 |
0.36 |
|
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 |
0.668 |
|
1988 |
Kaptein R, Boelens R, Scheek RM, van Gunsteren WF. Protein structures from NMR. Biochemistry. 27: 5389-95. PMID 3052574 DOI: 10.1021/Bi00415A001 |
0.679 |
|
1988 |
de Vlieg J, Scheek RM, van Gunsteren WF, Berendsen HJ, Kaptein R, Thomason J. Combined procedure of distance geometry and restrained molecular dynamics techniques for protein structure determination from nuclear magnetic resonance data: application to the DNA binding domain of lac repressor from Escherichia coli. Proteins. 3: 209-18. PMID 3047742 DOI: 10.1002/Prot.340030402 |
0.434 |
|
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 |
0.639 |
|
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 |
0.79 |
|
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 |
0.815 |
|
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 |
0.668 |
|
1988 |
NUSSELDER JJH, ENGBERTS JBFN, BOELENS R, KAPTEIN R. ChemInform Abstract: Micellar Structure Studied by 2D NMR Cheminform. 19. DOI: 10.1002/chin.198826051 |
0.627 |
|
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 |
0.654 |
|
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 |
0.681 |
|
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 |
0.66 |
|
1987 |
Lautz J, Kessler H, Kaptein R, Gunsteren WFv. Molecular dynamics simulations of cyclosporin A: The crystal structure and dynamic modelling of a structure in apolar solution based on NMR data Journal of Computer-Aided Molecular Design. 1: 219-241. PMID 3504965 DOI: 10.1007/Bf01677046 |
0.355 |
|
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 |
0.66 |
|
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 |
0.688 |
|
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 |
0.626 |
|
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 |
0.748 |
|
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 |
0.664 |
|
1986 |
Mayo KH, Schaudies P, Savage CR, De Marco A, Kaptein R. Structural characterization and exposure of aromatic residues in epidermal growth factor from the rat. The Biochemical Journal. 239: 13-8. PMID 3492201 DOI: 10.1042/Bj2390013 |
0.382 |
|
1986 |
Mayo KH, De Marco A, Kaptein R. Photo-CIDNP nuclear magnetic resonance as a probe for conformational changes in epidermal growth factor. Biochimica Et Biophysica Acta. 874: 181-6. PMID 3490880 DOI: 10.1016/0167-4838(86)90116-0 |
0.36 |
|
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 |
0.639 |
|
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 |
0.781 |
|
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 |
0.616 |
|
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 |
0.646 |
|
1985 |
Redfield C, Dobson CM, Scheek RM, Stob S, Kaptein R. Surface accessibility of aromatic residues in human lysozyme using photochemically induced dynamic nuclear polarization NMR spectroscopy. Febs Letters. 185: 248-52. PMID 3996602 DOI: 10.1016/0014-5793(85)80916-9 |
0.414 |
|
1985 |
Zuiderweg ER, Scheek RM, Kaptein R. Two-dimensional 1H-nmr studies on the lac repressor DNA binding domain: further resonance assignments and identification of nuclear Overhauser enhancements. Biopolymers. 24: 2257-77. PMID 3912012 DOI: 10.1002/Bip.360241208 |
0.685 |
|
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 |
0.786 |
|
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 |
0.78 |
|
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 |
0.674 |
|
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 |
0.67 |
|
1985 |
De Marco A, Zetta L, Kaptein R. Photo-CIDNP 1H-NMR of proteins: Exposure, mobility and orientation of the tyrosyl side chains European Biophysics Journal. 11: 187-193. DOI: 10.1007/BF00257397 |
0.348 |
|
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 |
0.635 |
|
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 |
0.602 |
|
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 |
0.657 |
|
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 |
0.639 |
|
1984 |
Garner WH, Spector A, Schleich T, Kaptein R. Determination of the solvent accessibility of specific aromatic residues in gamma-crystallin by photo-CIDNP NMR measurements. Current Eye Research. 3: 127-35. PMID 6690216 DOI: 10.3109/02713688408997194 |
0.407 |
|
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 |
0.795 |
|
1984 |
Zetta L, Kaptein R. Interaction of beta-endorphin with sodium dodecyl sulfate in aqueous solution. 1H-NMR investigation. European Journal of Biochemistry / Febs. 145: 181-6. PMID 6092079 DOI: 10.1111/J.1432-1033.1984.Tb08538.X |
0.389 |
|
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 |
0.664 |
|
1984 |
Nicolay K, Scheffers WA, Bruinenberg PM, Kaptein R. The dynamics of phosphate pools and intracellular pH in yeasts as studied by 31P nuclear magnetic resonance Antonie Van Leeuwenhoek. 50: 95-95. DOI: 10.1007/Bf00404934 |
0.484 |
|
1984 |
Nicolay K, van Gemerden H, Hellingwerf KJ, Konings WN, Kaptein R. In vivo 31P and 13C NMR studies on acetate incorporation in Chromatium vinosum Antonie Van Leeuwenhoek. 50: 94-95. DOI: 10.1007/Bf00404933 |
0.603 |
|
1983 |
Nicolay K, van Gemerden H, Hellingwerf KJ, Konings WN, Kaptein R. In vivo 31P and 13C nuclear magnetic resonance studies of acetate metabolism in Chromatium vinosum. Journal of Bacteriology. 155: 634-42. PMID 6874640 DOI: 10.1128/Jb.155.2.634-642.1983 |
0.616 |
|
1983 |
Egmond MR, Hore PJ, Kaptein R. Photo-CIDNP 1H-NMR studies of bovine pancreatic phospholipase A2 and its zymogen. Biochimica Et Biophysica Acta. 744: 23-7. PMID 6830822 DOI: 10.1016/0167-4838(83)90335-7 |
0.36 |
|
1983 |
Nicolay K, Scheffers WA, Bruinenberg PM, Kaptein R. In vivo 31P NMR studies on the role of the vacuole in phosphate metabolism in yeasts. Archives of Microbiology. 134: 270-5. PMID 6684418 DOI: 10.1007/Bf00407801 |
0.464 |
|
1983 |
Zuiderweg ER, Kaptein R, Wüthrich K. Sequence-specific resonance assignments in the 1H nuclear-magnetic-resonance spectrum of the lac repressor DNA-binding domain 1-51 from Escherichia coli by two-dimensional spectroscopy. European Journal of Biochemistry / Febs. 137: 279-92. PMID 6360686 DOI: 10.1111/J.1432-1033.1983.Tb07827.X |
0.727 |
|
1983 |
Zuiderweg ER, Kaptein R, Wüthrich K. Secondary structure of the lac repressor DNA-binding domain by two-dimensional 1H nuclear magnetic resonance in solution. Proceedings of the National Academy of Sciences of the United States of America. 80: 5837-41. PMID 6351066 DOI: 10.1073/Pnas.80.19.5837 |
0.742 |
|
1983 |
Buck F, Hahn KD, Zemann W, Rüterjans H, Sadler JR, Beyreuther K, Kaptein R, Scheek R, Hull WE. NMR study of the interaction between the lac repressor and the lac operator European Journal of Biochemistry. 132: 321-327. PMID 6341060 DOI: 10.1111/J.1432-1033.1983.Tb07365.X |
0.429 |
|
1983 |
Scheek RM, Zuiderweg ER, Klappe KJ, van Boom JH, Kaptein R, Rüterjans H, Beyreuther K. lac Repressor headpiece binds specifically to half of the lac operator: a proton nuclear magnetic resonance study. Biochemistry. 22: 228-35. PMID 6338916 DOI: 10.1021/Bi00270A033 |
0.657 |
|
1983 |
Zetta L, Hore PJ, Kaptein R. Investigation by photochemically-induced dynamic nuclear polarization and nuclear Overhauser enhancement 1H-NMR of the interaction between beta-endorphin and phospholipid micelles. European Journal of Biochemistry / Febs. 134: 371-6. PMID 6307694 DOI: 10.1111/J.1432-1033.1983.Tb07577.X |
0.329 |
|
1983 |
Nicolay K, van Gemerden H, Hellingwerf KJ, Konings WN, Kaptein R. In vivo 31P and 13C nuclear magnetic resonance studies of acetate metabolism in Chromatium vinosum. Journal of Bacteriology. 155: 634-642. DOI: 10.1128/jb.155.2.634-642.1983 |
0.55 |
|
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 |
0.64 |
|
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 |
0.672 |
|
1982 |
Moonen CT, Hore PJ, Müller F, Kaptein R, Mayhew SG. A photo-CIDNP study of the active sites of Megasphaera elsdenii and Clostridium MP flavodoxins. Febs Letters. 149: 141-6. PMID 7152030 DOI: 10.1016/0014-5793(82)81090-9 |
0.351 |
|
1982 |
van Schagen CG, Müller F, Kaptein R. Photochemically induced dynamic nuclear polarization study on flavin adenine dinucleotide and flavoproteins. Biochemistry. 21: 402-7. PMID 7074024 DOI: 10.1021/BI00531A030 |
0.343 |
|
1982 |
Nicolay K, Hellingwerf KJ, Kaptein R, Konings WN. Carbon-13 nuclear magnetic resonance studies of acetate metabolism in intact cells of rhodopseudomonas sphaeroides. Biochimica Et Biophysica Acta. 720: 250-8. PMID 6980672 DOI: 10.1016/0167-4889(82)90048-9 |
0.582 |
|
1982 |
Schleich T, Scheek RM, Stob S, Alma NCM, Hilbers CW, Kaptein R. PHOTO-CIDNP STUDY OF ADENYLYL-CONTAINING DEOXY-DINUCLEOTIDES. PAIR SUBSTITUTION EFFECTS DUE TO INTRAMOLECULAR CATION RADICAL DEPROTONATION Photochemistry and Photobiology. 35: 575-577. DOI: 10.1111/J.1751-1097.1982.Tb02612.X |
0.344 |
|
1982 |
Hors P, Egmond M, Edzes H, Kaptein R. Cross-relaxation effects in the photo-CIDNP spectra of amino acids and proteins Journal of Magnetic Resonance (1969). 49: 122-150. DOI: 10.1016/0022-2364(82)90302-X |
0.366 |
|
1982 |
Hore PJ, Scheek RM, Volbeda A, Kaptein R, van Boom JH. 1H NMR assignments and connectivis of cytosines in lac operator DNA via double quantum coherence Journal of Magnetic Resonance (1969). 50: 328-334. DOI: 10.1016/0022-2364(82)90063-4 |
0.33 |
|
1982 |
Nicolay K, Hellingwerf KJ, Van Gemerden H, Kaptein R, Konings WN. 31P NMR studies of photophosphorylation in intact cells ofChromatium vinosum Febs Letters. 138: 249-254. DOI: 10.1016/0014-5793(82)80453-5 |
0.598 |
|
1982 |
Nicolay K, Scheffers WA, Bruinenberg PM, Kaptein R. Phosphorus-31 nuclear magnetic resonance studies of intracellular pH, phosphate compartmentation and phosphate transport in yeasts Archives of Microbiology. 133: 83-89. DOI: 10.1007/Bf00413516 |
0.476 |
|
1982 |
Broek AD, Courtin JML, Mellema JR, Lugtenburg J, Nicolay K, Dijkstra K, Kaptein R. Structural assignment of isomeric chain demethylated retinals by1H NMR spectroscopy Organic Magnetic Resonance. 19: 105-107. DOI: 10.1002/Mrc.1270190213 |
0.547 |
|
1982 |
HORE PJ, ZUIDERWEG ERP, NICOLAY K, DIJKSTRA K, KAPTEIN R. ChemInform Abstract: MULTIPLET SELECTION IN CROWDED PROTON NMR SPECTRA VIA DOUBLE QUANTUM COHERENCE Chemischer Informationsdienst. 13. DOI: 10.1002/chin.198244067 |
0.439 |
|
1982 |
Hore PJ, Zuiderweg ERP, Nicolay K, Dijkstra K, Kaptein R. Multiplet selection in crowded proton NMR spectra via double quantum coherence Journal of the American Chemical Society. 104: 4286-4288. DOI: 10.1002/Chin.198244067 |
0.502 |
|
1981 |
Rathelot J, Canioni P, Bosc-Bierne I, Sarda L, Kamoun A, Kaptein R, Cozzone PJ. Limited trypsinolysis of porcine and equine colipases. Spectroscopic and kinetic studies. Biochimica Et Biophysica Acta. 671: 155-63. PMID 7326262 DOI: 10.1016/0005-2795(81)90129-X |
0.362 |
|
1981 |
Zuiderweg ER, Scheek RM, Veeneman G, van Boom JH, Kaptein R, Rüterjans H, Beyreuther K. 1H NMR studies of lac-operator DNA fragments. Nucleic Acids Research. 9: 6553-69. PMID 7322923 DOI: 10.1093/Nar/9.23.6553 |
0.659 |
|
1981 |
Van Dijck PW, Nicolay K, Leunissen-Bijvelt J, Van Dam K, Kaptein R. 31P-Nuclear magnetic resonance and freeze-fracture electron microscopic studies on reconstituted bacteriorhodopsin vesicles. European Journal of Biochemistry / Febs. 117: 639-45. PMID 7285909 DOI: 10.1111/J.1432-1033.1981.Tb06386.X |
0.464 |
|
1981 |
Cozzone PJ, Canioni P, Sarda L, Kaptein R. 360-MHz nuclear magnetic resonance and laser photochemically induced dynamic nuclear polarization studies of bile salt interaction with porcine colipase A. European Journal of Biochemistry / Febs. 114: 119-26. PMID 7215346 DOI: 10.1111/J.1432-1033.1981.Tb06181.X |
0.41 |
|
1981 |
Berliner LJ, Kaptein R. Nuclear magnetic resonance characterization of aromatic residues of alpha-lactalbumins. Laser photo chemically induced dynamic nuclear polarization nuclear magnetic resonance studies of surface exposure. Biochemistry. 20: 799-807. PMID 7213614 DOI: 10.1021/Bi00507A023 |
0.322 |
|
1981 |
Nicolay K, Kaptein R, Hellingwerf KJ, Konings WN. 31P nuclear magnetic resonance studies of energy transduction in Rhodopseudomonas sphaeroides. European Journal of Biochemistry / Febs. 116: 191-7. PMID 6972869 DOI: 10.1111/J.1432-1033.1981.Tb05318.X |
0.614 |
|
1981 |
Nicolay K, Lolkema J, Hellingwerf KJ, Kaptein R, Konings WN. Quantitative agreement between the values for the light-induced delta pH in Rhodopseudomonas sphaeroides measured with automated follow-dialysis and 31P NMR. Febs Letters. 123: 319-23. PMID 6971766 DOI: 10.1016/0014-5793(81)80318-3 |
0.59 |
|
1981 |
Hore P, Zuiderweg E, Kaptein R, Dijkstra K. Flash photolysis NMR- CIDNP time dependence in cyclic photochemical reactions Chemical Physics Letters. 83: 376-383. DOI: 10.1016/0009-2614(81)85483-8 |
0.313 |
|
1981 |
Scheck RM, Stob S, Schleich T, Alma NCM, Hilbers CW, Kaptein R. Photo-CIDNP study of adenosine 5′-monophosphate. Pair-substitution effects due to cation radical deprotonation Journal of the American Chemical Society. 103: 5930-5932. |
0.436 |
|
1980 |
Müller F, van Schagen CG, Kaptein R. Application of nuclear magnetic resonance and photochemically induced dynamic nuclear polarization to free and protein-bound flavins. Methods in Enzymology. 66: 385-416. PMID 7374481 DOI: 10.1016/0076-6879(80)66483-0 |
0.42 |
|
1980 |
Egmond MR, Slotboom AJ, De Haas GH, Dijkstra K, Kaptein R. 1H-NMR and photochemically-induced dynamic nuclear polarization studies on bovine pancreatic phospholipase A2. Biochimica Et Biophysica Acta. 623: 461-6. PMID 7190440 DOI: 10.1016/0005-2795(80)90276-7 |
0.338 |
|
1980 |
Buck F, Rüterjans H, Kaptein R, Beyreuther K. Photochemically induced dynamic nuclear polarization investigation of complex formation of the NH2-terminal DNA-binding domain of lac repressor with poly[d(AT)]. Proceedings of the National Academy of Sciences of the United States of America. 77: 5145-8. PMID 6933550 DOI: 10.1073/Pnas.77.9.5145 |
0.435 |
|
1980 |
Feeney J, Roberts GC, Kaptein R, Birdsall B, Gronenborn A, Burgen AS. Photo-CIDNP studies of the influence of ligand binding on the surface accessibility of aromatic residues in dihydrofolate reductase. Biochemistry. 19: 2466-72. PMID 6770894 DOI: 10.1021/Bi00552A026 |
0.364 |
|
1980 |
Mellink WA, Kaptein R. Determination of the methyl group rotation energy barrier in some substituted tricyclo [3.1.0.02,6]hexanes by carbon-13 spinlattice relaxation Organic Magnetic Resonance. 13: 279-281. DOI: 10.1002/MRC.1270130413 |
0.301 |
|
1979 |
Scheek RM, Kaptein R, Verhoeven JW. Resolution of specific histidine resonances in the 360 MHz 1H NMR spectrum of glyceraldehyde-3-phosphate dehydrogenase, a 145 000 molecular weight protein, by photo-CIDNP. Febs Letters. 107: 288-90. PMID 41741 DOI: 10.1016/0014-5793(79)80392-0 |
0.39 |
|
1979 |
Lenstra JA, Bolscher BG, Beintema JJ, Kaptein R. The aromatic residues of bovine pancreatic ribonuclease studied by 1H nuclear magnetic resonance. European Journal of Biochemistry / Febs. 98: 385-97. PMID 39752 DOI: 10.1111/J.1432-1033.1979.Tb13198.X |
0.381 |
|
1979 |
Kaptein R, Nicolay K, Dijkstra K. Photo-Cidnp In Nucleic-Acid Bases And Nucleotides Journal of the Chemical Society, Chemical Communications. 1092-1094. DOI: 10.1039/C39790001092 |
0.506 |
|
1978 |
Kaptein R, Dijkstra K, Nicolay K. Laser photo-CIDNP as a surface probe for proteins in solution. Nature. 274: 293-4. PMID 683312 DOI: 10.1038/274293A0 |
0.569 |
|
1978 |
Garssen GJ, Kaptein R, Schoenmakers JG, Hilbers CW. A photo-CIDNP study of the interaction of oligonucleotides with gene-5 protein of bacteriophage M13. Proceedings of the National Academy of Sciences of the United States of America. 75: 5281-5. PMID 364473 DOI: 10.1073/Pnas.75.11.5281 |
0.626 |
|
1977 |
De Kanter FJJ, Den Hollander JA, Huizer AH, Kaptein R. Biradical CIDNP and the dynamics of polymethylene chains Molecular Physics. 34: 857-874. DOI: 10.1080/00268977700102161 |
0.718 |
|
1976 |
Den Hollander JA, Kaptein R. Radical pair substitution in CIDNP. spin-uncorrelated geminate radical pairs Chemical Physics Letters. 41: 257-263. DOI: 10.1016/0009-2614(76)80805-6 |
0.703 |
|
1974 |
Kaptein R, Freeman R, Hill H. Carbon-13 CIDNP from biradicals in the photolysis of cyclic ketones Chemical Physics Letters. 26: 104-107. DOI: 10.1016/0009-2614(74)89096-2 |
0.508 |
|
1974 |
KAPTEIN R, FREEMAN R, HILL HDW, BARGON J. ChemInform Abstract: CARBON-13 CIDNP IN THE REVERSIBLE ADDITION OF PENTAFLUOROBENZOYLOXY RADICALS TO CHLOROBENZENE Chemischer Informationsdienst. 5: no-no. DOI: 10.1002/Chin.197414086 |
0.428 |
|
1973 |
Kaptein R, Freeman R, Hill HDW, Bargon J. Carbon-13 CIDNP in the reversible addition of pentafluorobenzoyloxy radicals to chlorobenzene Journal of the Chemical Society, Chemical Communications. 953-954. DOI: 10.1039/C39730000953 |
0.455 |
|
1972 |
Freeman R, Hill H, Kaptein R. Proton-decoupled NMR. Spectra of carbon-13 With the nuclear overhauser effect suppressed Journal of Magnetic Resonance (1969). 7: 327-329. DOI: 10.1016/0022-2364(72)90194-1 |
0.521 |
|
1972 |
Freeman R, Hill H, Kaptein R. An adaptive scheme for measuring NMR spin-lattice relaxation times Journal of Magnetic Resonance (1969). 7: 82-98. DOI: 10.1016/0022-2364(72)90148-5 |
0.493 |
|
1972 |
KAPTEIN R, DEN HOLLANDER JA. ChemInform Abstract: CHEMISCH INDUZIERTE DYNAMISCHE KERNPOLARISATION 10. MITT. ABHAENGIGKEIT VOM MAGNETISCHEN FELD Chemischer Informationsdienst. 3. DOI: 10.1002/chin.197247121 |
0.69 |
|
1972 |
Kaptein R, Den Hollander JA. Chemically induced dynamic nuclear polarization. X. On the magnetic field dependence Journal of the American Chemical Society. 94: 6269-6280. |
0.69 |
|
1971 |
Kaptein R, Verheus FW, Oosterhoff LJ. Chemically induced dynamic nuclear polarization. Sign reversal of the polarization in the reaction of isobutyryl peroxide with bromotrichloromethane Journal of the Chemical Society D: Chemical Communications. 877-878. DOI: 10.1039/C29710000877 |
0.772 |
|
1971 |
Kaptein R, Fráter-Schröder M, Oosterhoff LJ. Chemically induced dynamic nuclear polarization: NMR enhancements in biradical products Chemical Physics Letters. 12: 16-19. DOI: 10.1016/0009-2614(71)80606-1 |
0.789 |
|
1971 |
den Hollander JA, Kaptein R, Brand PATM. Chemically induced dynamic nuclear polarization (CIDNP) VII. Photoreactions of aliphatic ketones Chemical Physics Letters. 10: 430-435. DOI: 10.1016/0009-2614(71)80327-5 |
0.718 |
|
1970 |
Kaptein R, Den Hollander JA, Antheunis D, Oosterhoff LJ. Chemically induced dynamic nuclear polarization. Triplet and siglet state photosensitization of peroxide decompositions Journal of the Chemical Society D: Chemical Communications. 1687-1689. DOI: 10.1039/C29700001687 |
0.775 |
|
1968 |
Kaptein R. Chemically induced dynamic nuclear polarization in five alkyl radicals Chemical Physics Letters. 2: 261-267. DOI: 10.1016/0009-2614(68)85020-1 |
0.307 |
|
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