| Year |
Citation |
Score |
| 2012 |
Fonville JM, Swart M, Voká?ová Z, Sychrovský V, Šponer JE, Šponer J, Hilbers CW, Bickelhaupt FM, Wijmenga SS. Chemical shifts in nucleic acids studied by density functional theory calculations and comparison with experiment. Chemistry (Weinheim An Der Bergstrasse, Germany). 18: 12372-87. PMID 22899588 DOI: 10.1002/Chem.201103593 |
0.439 |
|
| 2012 |
Nabuurs CI, Hilbers CW, Wieringa B, Heerschap A. Letter to the editor: "Interpretation of (31)P NMR saturation transfer experiments: do not forget the spin relaxation properties". American Journal of Physiology. Cell Physiology. 302: C1566-7. PMID 22492653 DOI: 10.1152/Ajpcell.00409.2011 |
0.449 |
|
| 2010 |
Nabuurs C, Huijbregts B, Wieringa B, Hilbers CW, Heerschap A. 31P saturation transfer spectroscopy predicts differential intracellular macromolecular association of ATP and ADP in skeletal muscle. The Journal of Biological Chemistry. 285: 39588-96. PMID 20884612 DOI: 10.1074/Jbc.M110.164665 |
0.432 |
|
| 2010 |
Olsthoorn RC, Reumerman R, Hilbers CW, Pleij CW, Heus HA. Functional analysis of the SRV-1 RNA frameshifting pseudoknot. Nucleic Acids Research. 38: 7665-72. PMID 20639537 DOI: 10.1093/nar/gkq629 |
0.416 |
|
| 2010 |
Janssen B, Nabuurs C, Hilbers C, Heerschap A. P4.32 New light on calculating the free ADP concentration from the creatine kinase equilibrium Neuromuscular Disorders. 20: 667-668. DOI: 10.1016/J.Nmd.2010.07.228 |
0.351 |
|
| 2004 |
Kloks CP, Tessari M, Vuister GW, Hilbers CW. Cold shock domain of the human Y-box protein YB-1. Backbone dynamics and equilibrium between the native state and a partially unfolded state. Biochemistry. 43: 10237-46. PMID 15287751 DOI: 10.1021/bi049524s |
0.359 |
|
| 2003 |
Heus HA, Hilbers CW. Structures of non-canonical tandem base pairs in RNA helices: review. Nucleosides, Nucleotides & Nucleic Acids. 22: 559-71. PMID 14565230 DOI: 10.1081/NCN-120021955 |
0.384 |
|
| 2003 |
van't Slot KA, van den Burg HA, Kloks CP, Hilbers CW, Knogge W, Papavoine CH. Solution structure of the plant disease resistance-triggering protein NIP1 from the fungus Rhynchosporium secalis shows a novel beta-sheet fold. The Journal of Biological Chemistry. 278: 45730-6. PMID 12944393 DOI: 10.1074/jbc.M308304200 |
0.303 |
|
| 2003 |
Lescrinier EM, Tessari M, van Kuppeveld FJ, Melchers WJ, Hilbers CW, Heus HA. Structure of the pyrimidine-rich internal loop in the poliovirus 3'-UTR: the importance of maintaining pseudo-2-fold symmetry in RNA helices containing two adjacent non-canonical base-pairs. Journal of Molecular Biology. 331: 759-69. PMID 12909008 DOI: 10.1016/S0022-2836(03)00787-3 |
0.394 |
|
| 2002 |
Spronk CA, Linge JP, Hilbers CW, Vuister GW. Improving the quality of protein structures derived by NMR spectroscopy. Journal of Biomolecular Nmr. 22: 281-9. PMID 11991356 DOI: 10.1023/A:1014971029663 |
0.383 |
|
| 2002 |
Verhagen R, Wittlin A, Hilbers CW, van Kempen H, Kentgens AP. Spatially resolved spectroscopy and structurally encoded imaging by magnetic resonance force microscopy of quadrupolar spin systems. Journal of the American Chemical Society. 124: 1588-9. PMID 11853428 DOI: 10.1021/ja017693j |
0.331 |
|
| 2002 |
Kloks CP, Spronk CA, Lasonder E, Hoffmann A, Vuister GW, Grzesiek S, Hilbers CW. The solution structure and DNA-binding properties of the cold-shock domain of the human Y-box protein YB-1. Journal of Molecular Biology. 316: 317-26. PMID 11851341 DOI: 10.1006/jmbi.2001.5334 |
0.371 |
|
| 2001 |
Cromsigt JA, Hilbers CW, Wijmenga SS. Prediction of proton chemical shifts in RNA. Their use in structure refinement and validation. Journal of Biomolecular Nmr. 21: 11-29. PMID 11693565 DOI: 10.1023/A:1011914132531 |
0.323 |
|
| 2001 |
Michiels PJ, Versleijen AA, Verlaan PW, Pleij CW, Hilbers CW, Heus HA. Solution structure of the pseudoknot of SRV-1 RNA, involved in ribosomal frameshifting. Journal of Molecular Biology. 310: 1109-23. PMID 11501999 DOI: 10.1006/jmbi.2001.4823 |
0.408 |
|
| 2000 |
Michiels PJ, Schouten CH, Hilbers CW, Heus HA. Structure of the ribozyme substrate hairpin of Neurospora VS RNA: a close look at the cleavage site. Rna (New York, N.Y.). 6: 1821-32. PMID 11142381 DOI: 10.1017/S1355838200001394 |
0.449 |
|
| 2000 |
in 't Zandt HJ, Klomp DW, Oerlemans F, Wieringa B, Hilbers CW, Heerschap A. Proton MR spectroscopy of wild-type and creatine kinase deficient mouse skeletal muscle: dipole-dipole coupling effects and post-mortem changes. Magnetic Resonance in Medicine. 43: 517-24. PMID 10748426 DOI: 10.1002/(Sici)1522-2594(200004)43:4<517::Aid-Mrm5>3.0.Co;2-I |
0.445 |
|
| 1999 |
van Dongen MJ, Doreleijers JF, van der Marel GA, van Boom JH, Hilbers CW, Wijmenga SS. Structure and mechanism of formation of the H-y5 isomer of an intramolecular DNA triple helix. Nature Structural Biology. 6: 854-9. PMID 10467098 DOI: 10.1038/12313 |
0.54 |
|
| 1999 |
Prompers JJ, Hilbers CW, Pepermans HA. Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase. Febs Letters. 456: 409-16. PMID 10462054 DOI: 10.1016/S0014-5793(99)00990-4 |
0.302 |
|
| 1999 |
Prompers JJ, Groenewegen A, Hilbers CW, Pepermans HA. Backbone dynamics of Fusarium solani pisi cutinase probed by nuclear magnetic resonance: the lack of interfacial activation revisited. Biochemistry. 38: 5315-27. PMID 10220318 DOI: 10.1021/bi9827215 |
0.411 |
|
| 1999 |
Pineda-Lucena A, Vuister GW, Hilbers CW. Sequence-specific 1H, 13C and 15N assignment of the single-stranded DNA binding protein of the bacteriophage phi 29. Journal of Biomolecular Nmr. 13: 303-4. PMID 10212988 DOI: 10.1023/A:1008348505427 |
0.362 |
|
| 1999 |
Horstink LM, Abseher R, Nilges M, Hilbers CW. Functionally important correlated motions in the single-stranded DNA-binding protein encoded by filamentous phage Pf3. Journal of Molecular Biology. 287: 569-77. PMID 10092460 DOI: 10.1006/jmbi.1999.2629 |
0.34 |
|
| 1999 |
Verhagen R, Hilbers CW, Kentgens APM, Lenci L, Groeneveld R, Wittli A, Van Kempen H. Mechanical detection of NMR. Advantages of a digital approach Physical Chemistry Chemical Physics. 1: 4025-4031. DOI: 10.1039/a904045e |
0.314 |
|
| 1998 |
Hilbers CW, Michiels PJ, Heus HA. New developments in structure determination of pseudoknots. Biopolymers. 48: 137-53. PMID 10333742 DOI: 10.1002/(SICI)1097-0282(1998)48:2<137::AID-BIP4>3.0.CO;2-H |
0.367 |
|
| 1998 |
Kolk MH, van der Graaf M, Fransen CT, Wijmenga SS, Pleij CW, Heus HA, Hilbers CW. Structure of the 3'-hairpin of the TYMV pseudoknot: preformation in RNA folding. The Embo Journal. 17: 7498-504. PMID 9857204 DOI: 10.1093/emboj/17.24.7498 |
0.407 |
|
| 1998 |
Kloks CP, Hoffmann A, Omichinski JG, Vuister GW, Hilbers CW, Grzesiek S. Resonance assignment and secondary structure of the cold shock domain of the human YB-1 protein. Journal of Biomolecular Nmr. 12: 463-4. PMID 9835056 DOI: 10.1023/A:1008309216938 |
0.371 |
|
| 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 |
0.602 |
|
| 1998 |
Papavoine CH, Christiaans BE, Folmer RH, Konings RN, Hilbers CW. Solution structure of the M13 major coat protein in detergent micelles: a basis for a model of phage assembly involving specific residues. Journal of Molecular Biology. 282: 401-19. PMID 9735296 DOI: 10.1006/jmbi.1998.1860 |
0.391 |
|
| 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 |
0.602 |
|
| 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 |
0.595 |
|
| 1998 |
Abseher R, Horstink L, Hilbers CW, Nilges M. Essential spaces defined by NMR structure ensembles and molecular dynamics simulation show significant overlap. Proteins. 31: 370-82. PMID 9626697 DOI: 10.1002/(SICI)1097-0134(19980601)31:4<370::AID-PROT4>3.0.CO;2-M |
0.357 |
|
| 1998 |
Kolk MH, van der Graaf M, Wijmenga SS, Pleij CW, Heus HA, Hilbers CW. NMR structure of a classical pseudoknot: interplay of single- and double-stranded RNA. Science (New York, N.Y.). 280: 434-8. PMID 9545221 DOI: 10.1126/science.280.5362.434 |
0.394 |
|
| 1998 |
Prompers JJ, Groenewegen A, Hilbers CW, Pepermans HAM. Two-Dimensional NMR Experiments for the Assignment of Aromatic Side Chains in 13C-labeled Proteins Journal of Magnetic Resonance (San Diego, Calif. : 1997). 130: 68-75. PMID 9469899 DOI: 10.1006/Jmre.1997.1277 |
0.442 |
|
| 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 |
0.591 |
|
| 1998 |
Kolk MH, Wijmenga SS, Heus HA, Hilbers CW. On the NMR structure determination of a 44n RNA pseudoknot: Assignment strategies and derivation of torsion angle restraints Journal of Biomolecular Nmr. 12: 423-433. DOI: 10.1023/A:1008339405010 |
0.418 |
|
| 1997 |
Wijmenga SS, Kruithof M, Hilbers CW. Analysis of (1)H chemical shifts in DNA: Assessment of the reliability of (1)H chemical shift calculations for use in structure refinement. Journal of Biomolecular Nmr. 10: 337-50. PMID 20859781 DOI: 10.1023/A:1018348123074 |
0.328 |
|
| 1997 |
Prompers JJ, Groenewegen A, Van Schaik RC, Pepermans HA, Hilbers CW. 1H, 13C, and 15N resonance assignments of Fusarium solani pisi cutinase and preliminary features of the structure in solution. Protein Science : a Publication of the Protein Society. 6: 2375-84. PMID 9385640 DOI: 10.1002/pro.5560061111 |
0.469 |
|
| 1997 |
van den Hooven HW, Rollema HS, Siezen RJ, Hilbers CW, Kuipers OP. Structural features of the final intermediate in the biosynthesis of the lantibiotic nisin. Influence of the leader peptide. Biochemistry. 36: 14137-45. PMID 9369486 DOI: 10.1021/Bi9713106 |
0.342 |
|
| 1997 |
Heus HA, Wijmenga SS, Hoppe H, Hilbers CW. The detailed structure of tandem G.A mismatched base-pair motifs in RNA duplexes is context dependent. Journal of Molecular Biology. 271: 147-58. PMID 9300061 DOI: 10.1006/jmbi.1997.1158 |
0.438 |
|
| 1997 |
Folmer RH, Nilges M, Papavoine CH, Harmsen BJ, Konings RN, Hilbers CW. Refined structure, DNA binding studies, and dynamics of the bacteriophage Pf3 encoded single-stranded DNA binding protein. Biochemistry. 36: 9120-35. PMID 9230044 DOI: 10.1021/bi970251t |
0.414 |
|
| 1997 |
Folmer RH, Hilbers CW, Konings RN, Nilges M. Floating stereospecific assignment revisited: application to an 18 kDa protein and comparison with J-coupling data. Journal of Biomolecular Nmr. 9: 245-58. PMID 9229503 DOI: 10.1023/A:1018670623695 |
0.405 |
|
| 1997 |
Kolk MH, Heus HA, Hilbers CW. The structure of the isolated, central hairpin of the HDV antigenomic ribozyme: novel structural features and similarity of the loop in the ribozyme and free in solution. The Embo Journal. 16: 3685-92. PMID 9218809 DOI: 10.1093/emboj/16.12.3685 |
0.452 |
|
| 1997 |
van Dongen MJ, Mooren MM, Willems EF, van der Marel GA, van Boom JH, Wijmenga SS, Hilbers CW. Structural features of the DNA hairpin d(ATCCTA-GTTA-TAGGAT): formation of a G-A base pair in the loop. Nucleic Acids Research. 25: 1537-47. PMID 9092659 DOI: 10.1093/nar/25.8.1537 |
0.59 |
|
| 1996 |
van Dongen MJ, Wijmenga SS, van der Marel GA, van Boom JH, Hilbers CW. The transition from a neutral-pH double helix to a low-pH triple helix induces a conformational switch in the CCCG tetraloop closing a Watson-Crick stem. Journal of Molecular Biology. 263: 715-29. PMID 8947571 DOI: 10.1006/jmbi.1996.0611 |
0.61 |
|
| 1996 |
van Dongen MJ, Wijmenga SS, Eritja R, Azorín F, Hilbers CW. Through-bond correlation of adenine H2 and H8 protons in unlabeled DNA fragments by HMBC spectroscopy. Journal of Biomolecular Nmr. 8: 207-12. PMID 8914275 DOI: 10.1007/Bf00211166 |
0.433 |
|
| 1996 |
van den Hooven HW, Lagerwerf FM, Heerma W, Haverkamp J, Piard JC, Hilbers CW, Siezen RJ, Kuipers OP, Rollema HS. The structure of the lantibiotic lacticin 481 produced by Lactococcus lactis: location of the thioether bridges. Febs Letters. 391: 317-22. PMID 8764998 DOI: 10.1016/0014-5793(96)00771-5 |
0.379 |
|
| 1996 |
Rietman BH, Folkers PJ, Folmer RH, Tesser GI, Hilbers CW. The solution structure of the synthetic circular peptide CGVSRQGKPYC. NMR studies of the folding of a synthetic model for the DNA-binding loop of the ssDNA-binding protein encoded by gene V of phage M13. European Journal of Biochemistry / Febs. 238: 706-13. PMID 8706671 DOI: 10.1111/J.1432-1033.1996.0706W.X |
0.423 |
|
| 1996 |
Remerowski ML, Pepermans HA, Hilbers CW, Van De Ven FJ. Backbone dynamics of the 269-residue protease Savinase determined from 15N-NMR relaxation measurements. European Journal of Biochemistry / Febs. 235: 629-40. PMID 8654411 DOI: 10.1111/J.1432-1033.1996.00629.X |
0.393 |
|
| 1996 |
van Dongen MJ, Heus HA, Wymenga SS, van der Marel GA, van Boom JH, Hilbers CW. Unambiguous structure characterization of a DNA-RNA triple helix by 15N- and 13C-filtered NOESY spectroscopy. Biochemistry. 35: 1733-9. PMID 8639652 DOI: 10.1021/bi952002f |
0.503 |
|
| 1996 |
Van Den Hooven HW, Spronk CA, Van De Kamp M, Konings RN, Hilbers CW, Van De Van FJ. Surface location and orientation of the lantibiotic nisin bound to membrane-mimicking micelles of dodecylphosphocholine and of sodium dodecylsulphate. European Journal of Biochemistry / Febs. 235: 394-403. PMID 8631359 DOI: 10.1111/J.1432-1033.1996.00394.X |
0.361 |
|
| 1996 |
Van Den Hooven HW, Doeland CC, Van De Kamp M, Konings RN, Hilbers CW, Van De Ven FJ. Three-dimensional structure of the lantibiotic nisin in the presence of membrane-mimetic micelles of dodecylphosphocholine and of sodium dodecylsulphate. European Journal of Biochemistry / Febs. 235: 382-93. PMID 8631358 DOI: 10.1111/J.1432-1033.1996.00382.X |
0.416 |
|
| 1996 |
Ippel JH, Wijmenga SS, De Jong R, Heus HA, Hilbers CW, De Vroom E, Van Der Marel GA, Van Boom JH. Heteronuclear scalar couplings in the bases and sugar rings of nucleic acids: Their determination and application in assignment and conformational analysis Magnetic Resonance in Chemistry. 34: S156-S176. DOI: 10.1002/(Sici)1097-458X(199612)34:133.0.Co;2-U |
0.535 |
|
| 1995 |
Folmer RH, Hilbers CW, Konings RN, Hallenga K. A (13)C double-filtered NOESY with strongly reduced artefacts and improved sensitivity. Journal of Biomolecular Nmr. 5: 427-32. PMID 22911561 DOI: 10.1007/BF00182287 |
0.309 |
|
| 1995 |
van de Kamp M, Horstink LM, van den Hooven HW, Konings RN, Hilbers CW, Frey A, Sahl HG, Metzger JW, van de Ven FJ. Sequence analysis by NMR spectroscopy of the peptide lantibiotic epilancin K7 from Staphylococcus epidermidis K7. European Journal of Biochemistry / Febs. 227: 757-71. PMID 7867636 DOI: 10.1111/j.1432-1033.1995.tb20199.x |
0.36 |
|
| 1995 |
van de Kamp M, van den Hooven HW, Konings RN, Bierbaum G, Sahl HG, Kuipers OP, Siezen RJ, de Vos WM, Hilbers CW, van de Ven FJ. Elucidation of the primary structure of the lantibiotic epilancin K7 from Staphylococcus epidermidis K7. Cloning and characterisation of the epilancin-K7-encoding gene and NMR analysis of mature epilancin K7. European Journal of Biochemistry / Febs. 230: 587-600. PMID 7607233 DOI: 10.1111/J.1432-1033.1995.Tb20600.X |
0.309 |
|
| 1995 |
Prompers JJ, Folmer RH, Nilges M, Folkers PJ, Konings RN, Hilbers CW. Refined solution structure of the Tyr41-->His mutant of the M13 gene V protein. A comparison with the crystal structure. European Journal of Biochemistry / Febs. 232: 506-14. PMID 7556200 DOI: 10.1111/j.1432-1033.1995.506zz.x |
0.418 |
|
| 1995 |
Papavoine CH, Aelen JM, Konings RN, Hilbers CW, Van de Ven FJ. NMR studies of the major coat protein of bacteriophage M13. Structural information of gVIIIp in dodecylphosphocholine micelles. European Journal of Biochemistry / Febs. 232: 490-500. PMID 7556198 DOI: 10.1111/j.1432-1033.1995.490zz.x |
0.412 |
|
| 1995 |
Folmer RH, Nilges M, Konings RN, Hilbers CW. Solution structure of the single-stranded DNA binding protein of the filamentous Pseudomonas phage Pf3: similarity to other proteins binding to single-stranded nucleic acids. The Embo Journal. 14: 4132-42. PMID 7556054 DOI: 10.1002/J.1460-2075.1995.Tb00087.X |
0.39 |
|
| 1994 |
Folkers PJ, Nilges M, Folmer RH, Konings RN, Hilbers CW. The solution structure of the Tyr41-->His mutant of the single-stranded DNA binding protein encoded by gene V of the filamentous bacteriophage M13. Journal of Molecular Biology. 236: 229-46. PMID 8107108 DOI: 10.1006/jmbi.1994.1132 |
0.357 |
|
| 1994 |
Mooren MM, Wijmenga SS, van der Marel GA, van Boom JH, Hilbers CW. The solution structure of the circular trinucleotide cr(GpGpGp) determined by NMR and molecular mechanics calculation. Nucleic Acids Research. 22: 2658-66. PMID 8041628 |
0.514 |
|
| 1994 |
Guan Y, Zhang H, Konings RN, Hilbers CW, Terwilliger TC, Wang AH. Crystal structures of Y41H and Y41F mutants of gene V protein from Ff phage suggest possible protein-protein interactions in the GVP-ssDNA complex. Biochemistry. 33: 7768-78. PMID 8011642 DOI: 10.2210/Pdb1Yha/Pdb |
0.415 |
|
| 1994 |
Mooren MM, Pulleyblank DE, Wijmenga SS, van de Ven FJ, Hilbers CW. The solution structure of the hairpin formed by d(TCTCTC-TTT-GAGAGA). Biochemistry. 33: 7315-25. PMID 8003496 |
0.366 |
|
| 1994 |
Folmer RH, Folkers PJ, Kaan A, Jonker AJ, Aelen JM, Konings RN, Hilbers CW. Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR. European Journal of Biochemistry / Febs. 224: 663-76. PMID 7925383 DOI: 10.1111/J.1432-1033.1994.00663.X |
0.443 |
|
| 1994 |
Wijmenga SS, Heus HA, Werten B, van der Marel GA, van Boom JH, Hilbers CW. Assignment strategies and analysis of cross-peak patterns and intensities in the three-dimensional homonuclear TOCSY-NOESY of RNA. Journal of Magnetic Resonance. Series B. 103: 134-41. PMID 7511032 DOI: 10.1006/jmrb.1994.1021 |
0.5 |
|
| 1993 |
van den Hooven HW, Fogolari F, Rollema HS, Konings RN, Hilbers CW, van de Ven FJ. NMR and circular dichroism studies of the lantibiotic nisin in non-aqueous environments. Febs Letters. 319: 189-94. PMID 8454055 DOI: 10.1016/0014-5793(93)80065-3 |
0.384 |
|
| 1993 |
Folkers PJ, van Duynhoven JP, van Lieshout HT, Harmsen BJ, van Boom JH, Tesser GI, Konings RN, Hilbers CW. Exploring the DNA binding domain of gene V protein encoded by bacteriophage M13 with the aid of spin-labeled oligonucleotides in combination with 1H-NMR. Biochemistry. 32: 9407-16. PMID 8396429 DOI: 10.1021/Bi00087A020 |
0.526 |
|
| 1993 |
Van Duynhoven JP, Nooren IM, Swinkels DW, Folkers PJ, Harmsen BJ, Konings RN, Tesser GI, Hilbers CW. Exploration of the single-stranded DNA-binding domains of the gene V proteins encoded by the filamentous bacteriophages IKe and M13 by means of spin-labeled oligonucleotide and lanthanide-chelate complexes. European Journal of Biochemistry / Febs. 216: 507-17. PMID 8375389 DOI: 10.1111/J.1432-1033.1993.Tb18169.X |
0.384 |
|
| 1992 |
van Duynhoven JP, Folkers PJ, Prinse CW, Harmsen BJ, Konings RN, Hilbers CW. Assignment of the 1H NMR spectrum and secondary structure elucidation of the single-stranded DNA binding protein encoded by the filamentous bacteriophage IKe. Biochemistry. 31: 1254-62. PMID 1734970 |
0.334 |
|
| 1992 |
Stassen AP, Harmsen BJ, Schoenmakers JG, Hilbers CW, Konings RN. Fluorescence studies of the binding of bacteriophage M13 gene V mutant proteins to polynucleotides. European Journal of Biochemistry / Febs. 206: 605-12. PMID 1606950 DOI: 10.1111/J.1432-1033.1992.Tb16965.X |
0.335 |
|
| 1992 |
van de Kamp M, Canters GW, Wijmenga SS, Lommen A, Hilbers CW, Nar H, Messerschmidt A, Huber R. Complete sequential 1H and 15N nuclear magnetic resonance assignments and solution secondary structure of the blue copper protein azurin from Pseudomonas aeruginosa. Biochemistry. 31: 10194-207. PMID 1420141 DOI: 10.1021/Bi00157A006 |
0.332 |
|
| 1991 |
Lommen A, Wijmenga S, Hilbers CW, Canters GW. Assignment of the 600-MHz 1H-NMR spectrum of amicyanin from Thiobacillus versutus by two-dimensional NMR methods provides information on secondary structure. European Journal of Biochemistry / Febs. 201: 695-702. PMID 1935963 DOI: 10.1111/J.1432-1033.1991.Tb16330.X |
0.347 |
|
| 1991 |
Blommers MJ, van de Ven FJ, van der Marel GA, van Boom JH, Hilbers CW. The three-dimensional structure of a DNA hairpin in solution two-dimensional NMR studies and structural analysis of d(ATCCTATTTATAGGAT). European Journal of Biochemistry / Febs. 201: 33-51. PMID 1915376 DOI: 10.1111/J.1432-1033.1991.TB16253.X |
0.644 |
|
| 1991 |
Folkers PJ, Stassen AP, van Duynhoven JP, Harmsen BJ, Konings RN, Hilbers CW. Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR. European Journal of Biochemistry / Febs. 200: 139-48. PMID 1879419 DOI: 10.1111/J.1432-1033.1991.Tb21060.X |
0.386 |
|
| 1991 |
Smits GA, Heerschap A, Oosterhof GO, Ruys JH, Hilbers CW, Debruyne FM, Schalken JA. Early metabolic response to high energy shock waves in a human tumor kidney xenograft monitored by 31P magnetic resonance spectroscopy. Ultrasound in Medicine & Biology. 17: 791-801. PMID 1808797 DOI: 10.1016/0301-5629(91)90162-P |
0.407 |
|
| 1991 |
Van de Ven FJ, Van den Hooven HW, Konings RN, Hilbers CW. NMR studies of lantibiotics. The structure of nisin in aqueous solution. European Journal of Biochemistry / Febs. 202: 1181-8. PMID 1765078 DOI: 10.1111/J.1432-1033.1991.Tb16488.X |
0.454 |
|
| 1991 |
Folkers PJ, van Duynhoven JP, Jonker AJ, Harmsen BJ, Konings RN, Hilbers CW. Sequence-specific 1H-NMR assignment and secondary structure of the Tyr41----His mutant of the single-stranded DNA binding protein, gene V protein, encoded by the filamentous bacteriophage M13. European Journal of Biochemistry / Febs. 202: 349-60. PMID 1761038 DOI: 10.1111/j.1432-1033.1991.tb16382.x |
0.433 |
|
| 1991 |
Swinkels DW, Tesser GI, van Duynhoven JPM, Hilbers CW. Improved synthesis and application of lanthanide 1,4,7,10-tetrakis(phosphonomethyl)-1,4,7,10-tetraazacyclododecane complexes Ln(DOTP) Recueil Des Travaux Chimiques Des Pays-Bas. 110: 124-128. DOI: 10.1002/Recl.19911100406 |
0.36 |
|
| 1990 |
van Belkum A, Blommers MJ, van den Elst H, van Boom JH, Hilbers CW. Biochemical and biophysical studies on the folding of the core region of the origin of replication of bacteriophage M13. Nucleic Acids Research. 18: 4703-10. PMID 2395637 DOI: 10.1093/Nar/18.16.4703 |
0.59 |
|
| 1990 |
Mooren MM, Pulleyblank DE, Wijmenga SS, Blommers MJ, Hilbers CW. Polypurine/polypyrimidine hairpins form a triple helix structure at low pH. Nucleic Acids Research. 18: 6523-9. PMID 2251115 DOI: 10.1093/Nar/18.22.6523 |
0.455 |
|
| 1990 |
Blommers MJ, Slot HJ, van der Marel GA, van Boom JH, Hilbers CW. Conformational analysis of the 3'-5'-cyclic dinucleotide d less than pApA greater than by means of molecular mechanics. Journal of Biomolecular Structure & Dynamics. 8: 233-51. PMID 2176505 DOI: 10.1080/07391102.1990.10507804 |
0.526 |
|
| 1990 |
Akkerman MAJ, Neijman EWJF, Wijmenga SS, Hilbers CW, Bermel W. Studies of the solution structure of the bleomycin A2-iron(II)-carbon monoxide complex by means of two-dimensional NMR spectroscopy and distance geometry calculations Journal of the American Chemical Society. 112: 7462-7474. DOI: 10.1021/Ja00177A003 |
0.321 |
|
| 1989 |
Blommers MJ, Walters JA, Haasnoot CA, Aelen JM, van der Marel GA, van Boom JH, Hilbers CW. Effects of base sequence on the loop folding in DNA hairpins. Biochemistry. 28: 7491-8. PMID 2819083 DOI: 10.1021/BI00444A049 |
0.769 |
|
| 1989 |
van Belkum A, Wiersema PJ, Joordens J, Pleij C, Hilbers CW, Bosch L. Biochemical and biophysical analysis of pseudoknot-containing RNA fragments. Melting studies and NMR spectroscopy. European Journal of Biochemistry / Febs. 183: 591-601. PMID 2776753 DOI: 10.1111/J.1432-1033.1989.Tb21088.X |
0.406 |
|
| 1989 |
de Jong EA, van Duynhoven JP, Harmsen BJ, Tesser GI, Konings RN, Hilbers CW. Two-dimensional 1H nuclear magnetic resonance studies on the gene V-encoded single-stranded DNA-binding protein of the filamentous bacteriophage IKe. II. Characterization of the DNA-binding wing with the aid of spin-labelled oligonucleotides. Journal of Molecular Biology. 206: 133-52. PMID 2704038 DOI: 10.1016/0022-2836(89)90529-9 |
0.309 |
|
| 1989 |
de Jong EA, van Duynhoven JP, Harmsen BJ, Konings RN, Hilbers CW. Two-dimensional 1H nuclear magnetic resonance studies on the gene V-encoded single-stranded DNA-binding protein of the filamentous bacteriophage IKe. I. Structure elucidation of the DNA-binding wing. Journal of Molecular Biology. 206: 119-32. PMID 2704037 DOI: 10.1016/0022-2836(89)90528-7 |
0.354 |
|
| 1988 |
Bulsink H, Harmsen BJ, Hilbers CW. DNA-binding properties of gene-5 protein encoded by bacteriophage M13. 2. Further characterization of the different binding modes for poly- and oligodeoxynucleic acids. European Journal of Biochemistry / Febs. 176: 597-608. PMID 3262511 DOI: 10.1111/J.1432-1033.1988.Tb14319.X |
0.339 |
|
| 1988 |
Bulsink H, Harmsen BJ, Hilbers CW. DNA-binding properties of gene-5 protein encoded by bacteriophage M 13. 1. The kinetics of the dissociation of gene-5-protein.polynucleotide complexes upon addition of salt. European Journal of Biochemistry / Febs. 176: 589-96. PMID 3262510 DOI: 10.1111/J.1432-1033.1988.Tb14318.X |
0.349 |
|
| 1988 |
Van de Ven FJ, Hilbers CW. Nucleic acids and nuclear magnetic resonance. European Journal of Biochemistry / Febs. 178: 1-38. PMID 3060357 DOI: 10.1111/J.1432-1033.1988.Tb14425.X |
0.311 |
|
| 1988 |
Blommers MJ, Haasnoot CA, Walters JA, van der Marel GA, van Boom JH, Hilbers CW. Solution structure of the 3'-5' cyclic dinucleotide d(pApA). A combined NMR, UV melting, and molecular mechanics study. Biochemistry. 27: 8361-9. PMID 2853963 DOI: 10.1021/BI00422A011 |
0.784 |
|
| 1988 |
van de Ven FJ, Hilbers CW. Resonance assignments of non-exchangeable protons in B type DNA oligomers, an overview. Nucleic Acids Research. 16: 5713-26. PMID 2840632 DOI: 10.1093/nar/16.13.5713 |
0.348 |
|
| 1988 |
Akkerman MA, Haasnoot CA, Hilbers CW. Studies of the solution structure of the bleomycin-A2-zinc complex by means of two-dimensional NMR spectroscopy and distance geometry calculations. European Journal of Biochemistry / Febs. 173: 211-25. PMID 2451607 DOI: 10.1111/J.1432-1033.1988.Tb13987.X |
0.751 |
|
| 1988 |
Akkerman MAJ, Haasnoot CAG, Pandit UK, Hilbers CW. Complete assignment of the13C NMR spectra of bleomycin A2 and its zinc complex by means of two-dimensional NMR spectroscopy Magnetic Resonance in Chemistry. 26: 793-802. DOI: 10.1002/Mrc.1260260911 |
0.396 |
|
| 1987 |
de Jong EA, Konings RN, Harmsen BJ, Prinse CW, Hilbers CW. 1H-NMR studies on the gene-5-encoded single-stranded DNA binding protein of the filamentous bacteriophage IKe. General spectral and structural features. European Journal of Biochemistry / Febs. 167: 563-72. PMID 3308460 DOI: 10.1111/J.1432-1033.1987.Tb13373.X |
0.43 |
|
| 1987 |
Raap J, Dreef CE, van der Marel GA, van Boom JH, Hilbers CW. Synthesis and proton-NMR studies of oligonucleotides containing an apurinic (AP) site. Journal of Biomolecular Structure & Dynamics. 5: 219-47. PMID 2856028 DOI: 10.1080/07391102.1987.10506391 |
0.72 |
|
| 1986 |
Heerschap A, Walters JA, Mellema JR, Hilbers CW. Study of the interaction between uncharged yeast tRNAPhe and elongation factor Tu from Bacillus stearothermophilis. Biochemistry. 25: 2707-13. PMID 3636156 |
0.54 |
|
| 1986 |
van de Ven FJM, Hilbers CW. Residue-specific assignments of resonances in the 1H nuclear magnetic resonance spectrum of ribosomal protein E-L30 by systematic application of two-dimensional fourier transform nuclear magnetic resonance methods Journal of Molecular Biology. 192: 389-417. PMID 3550102 DOI: 10.1016/0022-2836(86)90372-4 |
0.325 |
|
| 1986 |
Heerschap A, Walters JA, Hilbers CW. Influence of the polyamines spermine and spermidine on yeast tRNAPhe as revealed from its imino proton NMR spectrum. Nucleic Acids Research. 14: 983-98. PMID 3511448 DOI: 10.1093/Nar/14.2.983 |
0.526 |
|
| 1986 |
Haasnoot CA, Hilbers CW, van der Marel GA, van Boom JH, Singh UC, Pattabiraman N, Kollman PA. On loop folding in nucleic acid hairpin-type structures. Journal of Biomolecular Structure & Dynamics. 3: 843-57. PMID 2482747 DOI: 10.1080/07391102.1986.10508468 |
0.783 |
|
| 1985 |
Hilbers CW, Haasnoot CAG, de Bruin SH, Joordens JJM, Van Der Marel GA, Van Boom JH. Hairpin formation in synthetic oligonucleotides Biochimie. 67: 685-695. PMID 4084598 DOI: 10.1016/S0300-9084(85)80156-5 |
0.53 |
|
| 1985 |
Heerschap A, Walters JA, Hilbers CW. Interactions of some naturally occurring cations with phenylalanine and initiator tRNA from yeast as reflected by their thermal stability. Biophysical Chemistry. 22: 205-17. PMID 3902111 DOI: 10.1016/0301-4622(85)80044-2 |
0.443 |
|
| 1985 |
Heerschap A, Mellema JR, Janssen HG, Walters JA, Haasnoot CA, Hilbers CW. Imino-proton resonances of yeast tRNAPhe studied by two-dimensional nuclear Overhauser enhancement spectroscopy. European Journal of Biochemistry / Febs. 149: 649-55. PMID 2988955 DOI: 10.1111/J.1432-1033.1985.Tb08973.X |
0.607 |
|
| 1984 |
Tibanyenda N, De Bruin SH, Haasnoot CA, van der Marel GA, van Boom JH, Hilbers CW. The effect of single base-pair mismatches on the duplex stability of d(T-A-T-T-A-A-T-A-T-C-A-A-G-T-T-G) . d(C-A-A-C-T-T-G-A-T-A-T-T-A-A-T-A) European Journal of Biochemistry. 139: 19-27. PMID 6698006 DOI: 10.1111/J.1432-1033.1984.TB07970.X |
0.749 |
|
| 1984 |
Haasnoot CA, Pandit UK, Kruk C, Hilbers CW. Complete assignment of the 500 MHz 1H-NMR spectra of bleomycin A2 in H2O and D2O solution by means of two-dimensional NMR spectroscopy. Journal of Biomolecular Structure & Dynamics. 2: 449-67. PMID 6086066 DOI: 10.1080/07391102.1984.10507579 |
0.75 |
|
| 1983 |
Alma NCM, Harmsen BJM, Van Boom JH, Van Der Marel G, Hilbers CW. A 500-MHz proton nuclear magnetic resonance study of the structure and structural alterations of gene-5 protein-oligo(deoxyadenylic acid) complexes Biochemistry. 22: 2104-2115. PMID 6602628 DOI: 10.1021/BI00278A010 |
0.527 |
|
| 1983 |
van Boom JH, van der Marel GA, Westerink H, van Boeckel CA, Mellema JR, Altona C, Hilbers CW, Haasnoot CA, de Bruin SH, Berendsen RG. Synthesis and conformational analysis of synthetic DNA fragments. Cold Spring Harbor Symposia On Quantitative Biology. 47: 403-9. PMID 6574853 |
0.761 |
|
| 1983 |
Hilbers CW, Heerschap A, Haasnoot CA, Walters JA. The solution structure of yeast tRNAPhe as studied by nuclear Overhauser effects in NMR. Journal of Biomolecular Structure & Dynamics. 1: 183-207. PMID 6401111 DOI: 10.1080/07391102.1983.10507434 |
0.779 |
|
| 1983 |
Haasnoot CA, de Bruin SH, Berendsen RG, Janssen HG, Binnendijk TJ, Hilbers CW, van der Marel GA, van Boom JH. Structure, kinetics and thermodynamics of DNA hairpin fragments in solution. Journal of Biomolecular Structure & Dynamics. 1: 115-29. PMID 6401107 DOI: 10.1080/07391102.1983.10507429 |
0.791 |
|
| 1983 |
van de Ven FJ, de Bruin SH, Hilbers CW. 500-MHz 1H-NMR studies of ribosomal proteins isolated from 70-S ribosomes of Escherichia coli European Journal of Biochemistry. 134: 429-438. PMID 6349991 DOI: 10.1111/J.1432-1033.1983.Tb07585.X |
0.354 |
|
| 1983 |
Heerschap A, Haasnoot CA, Hilbers CW. Nuclear magnetic resonance studies on yeast tRNAPhe. III. Assignments of the iminoproton resonances of the tertiary structure by means of nuclear Overhauser effect experiments at 500 MHz. Nucleic Acids Research. 11: 4501-20. PMID 6346269 DOI: 10.1093/Nar/11.13.4501 |
0.597 |
|
| 1983 |
Heerschap A, Haasnoot CA, Hilbers CW. Nuclear magnetic resonance studies on yeast tRNAPhe. II. Assignment of the iminoproton resonances of the anticodon and T stem by means of nuclear Overhauser effect experiments at 500 MHz. Nucleic Acids Research. 11: 4483-99. PMID 6346268 DOI: 10.1093/Nar/11.13.4483 |
0.584 |
|
| 1983 |
Heus HA, van Kimmenade JM, van Knippenberg PH, Haasnoot CA, de Bruin SH, Hilbers CW. High-resolution proton magnetic resonance studies of the 3'-terminal colicin fragment of 16 S ribosomal RNA from Escherichia coli. Assignment of iminoproton resonances by nuclear Overhauser effect experiments and the influence of adenine dimethylation on the hairpin conformation. Journal of Molecular Biology. 170: 939-56. PMID 6315954 DOI: 10.1016/S0022-2836(83)80197-1 |
0.341 |
|
| 1983 |
Haasnoot CAG, Heerschap A, Hilbers CW. Nuclear overhauser effect measurements involving the imino protons of yeast tRNAPhe using two-dimensional proton NMR spectroscopy Journal of the American Chemical Society. 105: 5483-5484. DOI: 10.1021/Ja00354A053 |
0.4 |
|
| 1982 |
Alma NC, Harmsen BJ, van Boom JH, van der Marel G, Hilbers CW. 1H NMR studies of the binding of bacteriophage-M13-encoded gene-5 protein to oligo(deoxyadenylic acid)s of varying length. European Journal of Biochemistry. 122: 319-26. PMID 6977447 DOI: 10.1111/J.1432-1033.1982.TB05883.X |
0.567 |
|
| 1982 |
Heerschap A, Haasnoot CA, Hilbers CW. Nuclear magnetic resonance studies on yeast tRNAPhe I. Assignment of the iminoproton resonances of the acceptor and D stem by means of Nuclear Overhauser Effect experiments at 500 MHz. Nucleic Acids Research. 10: 6981-7000. PMID 6757870 |
0.495 |
|
| 1981 |
Salemink PJ, Raué HA, Heerschap A, Planta RJ, Hilbers CW. Hydrogen-1 and phosphorus-31 nuclear magnetic resonance study of the solution structure of Bacillus licheniformis 5S ribonucleic acid. Biochemistry. 20: 265-72. PMID 7470483 DOI: 10.1021/Bi00505A006 |
0.632 |
|
| 1981 |
Zuiderweg ER, Hamers LF, Rollema HS, de Bruin SH, Hilbers CW. 31P NMR study of the kinetics of binding of myo-inositol hexakisphosphate to human hemoglobin. Observation of fast-exchange kinetics in high-affinity systems. European Journal of Biochemistry / Febs. 118: 95-104. PMID 7285916 |
0.592 |
|
| 1981 |
Zuiderweg ER, Hamers LF, de Bruin SH, Hilbers CW. Equilibrium aspects of the binding of myo-inositol hexakisphosphate to human hemoglobin as studied by 31P NMR and pH-stat techniques. European Journal of Biochemistry / Febs. 118: 85-94. PMID 7285915 DOI: 10.1111/J.1432-1033.1981.Tb05489.X |
0.62 |
|
| 1981 |
Salemink PJ, Reijerse EJ, Mollevanger LC, Hilbers CW. Conformational changes of yeast tRNAphe as monitored by 31P NMR European Journal of Biochemistry. 115: 635-641. PMID 7238525 DOI: 10.1111/J.1432-1033.1981.Tb06249.X |
0.501 |
|
| 1981 |
Alma NCM, Harmsen BJM, Hull WE, Van Der Marel G, Van Boom JH, Hilbers CW. Double-resonance experiments at 500 MHz on gene-5 protein and its complex with octadeoxyriboadenylic acid Biochemistry. 20: 4419-4428. PMID 6974567 DOI: 10.1021/BI00518A029 |
0.565 |
|
| 1981 |
Alma NCM, Harmsen BJM, Hilbers CW, Van der Marel G, Van Boom JH. 500 MHz 1H NMR study of the role of lysines and arginines in the binding of gene-5 protein to oligoadenylic acids Febs Letters. 135: 15-20. PMID 6797840 DOI: 10.1016/0014-5793(81)80934-9 |
0.458 |
|
| 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. |
0.403 |
|
| 1980 |
Geerdes HA, Van Boom JH, Hilbers CW. Codon-anticodon interaction in tRNAPhe. II. A nuclear magnetic resonance study of the binding of the codon UUC Journal of Molecular Biology. 142: 219-230. PMID 7003160 DOI: 10.1016/0022-2836(80)90046-7 |
0.443 |
|
| 1980 |
Garssen GJ, Tesser GI, Schoenmakers JG, Hilbers CW. NMR studies of the interaction of gene-V protein of bacteriophage M13 with oligonucleotides. Biochimica Et Biophysica Acta. 607: 361-71. PMID 6966158 DOI: 10.1016/0005-2787(80)90088-X |
0.379 |
|
| 1980 |
Geerdes HA, Van Boom JH, Hilbers CW. Nuclear magnetic resonance studies of codon-anticodon interaction in tRNAPhe. I. Effect of binding complementary tetra and pentanucleotides to the anticodon Journal of Molecular Biology. 142: 195-217. PMID 6160254 DOI: 10.1016/0022-2836(80)90045-5 |
0.453 |
|
| 1979 |
Salemink PJ, Swarthof T, Hilbers CW. Studies of yeast phenylalanine-accepting transfer ribonucleic acid backbone structure in solution by phosphorus-31 nuclear magnetic resonance spectroscopy. Biochemistry. 18: 3477-85. PMID 383144 DOI: 10.1021/BI00583A007 |
0.382 |
|
| 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 |
0.518 |
|
| 1978 |
Geerdes HAM, Van Boom JH, Hilbers CW. Codon-anticodon interaction in Yeast tRNAPhe an 1H NMR study Febs Letters. 88: 27-32. PMID 346374 DOI: 10.1016/0014-5793(78)80599-7 |
0.522 |
|
| 1977 |
Garssen GJ, Hilbers CW, Schoenmakers JG, van Boom JH. Studies on DNA unwinding. Proton and phosphorus nuclear-magnetic-resonance studies of gene V protein from bacteriophage M13, interacting with d(pC-G-C-G). European Journal of Biochemistry / Febs. 81: 453-63. PMID 598376 DOI: 10.1111/J.1432-1033.1977.Tb11970.X |
0.477 |
|
| 1977 |
Salemink PJM, Yamane T, Hilbers CW. Demonstration of a tertiary interaction in solution between the extra arm and the D-stem in two different transfer RNA's by NMR Nucleic Acids Research. 4: 3727-3741. PMID 339202 |
0.336 |
|
| 1977 |
Geerdes HAM, Hilbers CW. The iminoproton NMR spectrum of yeast tRNA(Phe) predicted from crystal coordinates Nucleic Acids Research. 4: 207-221. PMID 325518 DOI: 10.1093/Nar/4.1.207 |
0.408 |
|
| 1977 |
Baan RA, Hilbers CW, Van Charldorp R, Van Leerdam E, Van Knippenberg PH, Bosch L. High-resolution proton magnetic resonance study of the secondary structure of the 3'-terminal 49-nucleotide fragment of 16S rRNA from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 74: 1028-31. PMID 322143 DOI: 10.1073/Pnas.74.3.1028 |
0.349 |
|
| 1976 |
Bina-Stein M, Crothers DM, Hilbers CW, Shulman RG. Physical studies of denatured tRNA2Glu from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 73: 2216-20. PMID 781670 DOI: 10.1073/Pnas.73.7.2216 |
0.557 |
|
| 1976 |
Robillard GT, Hilbers CW, Reid BR, Gangloff J, Dirheimer G, Shulman RG. A study of secondary and tertiary solution structure of yeast tRNA(Asp) by nuclear magnetic resonance. Assignment of G.U ring NH and hydrogen-bonded base pair proton resonances. Biochemistry. 15: 1883-8. PMID 773428 DOI: 10.1021/Bi00654A014 |
0.681 |
|
| 1976 |
Hilbers CW, Robillard GT, Shulman RG, Blake RD, Webb PK, Fresco R, Riesner D. Thermal unfolding of yeast glycine transfer RNA Biochemistry. 15: 1874-1882. PMID 773427 DOI: 10.1021/Bi00654A013 |
0.637 |
|
| 1975 |
Reid BR, Ribeiro NS, Gould G, Robillard G, Hilbers CW, Shulman RG. Tertiary hydrogen bonds in the solution structure of transfer RNA. Proceedings of the National Academy of Sciences of the United States of America. 72: 2049-53. PMID 1094451 DOI: 10.1073/pnas.72.6.2049 |
0.684 |
|
| 1975 |
Patel DJ, Hilbers CW. Proton nuclear magnetic resonance investigations of fraying in double-stranded d-ApTpGpCpApT in H2O solution Biochemistry. 14: 2651-2656. PMID 238568 DOI: 10.1021/Bi00683A014 |
0.322 |
|
| 1974 |
Hilbers CW, Shulman RG, Yamane T, Steitz JA. High resolution proton NMR study of an isolated fragment of R17 bacteriophage mRNA. Nature. 248: 225-6. PMID 4819416 DOI: 10.1038/248225A0 |
0.557 |
|
| 1974 |
Crothers DM, Cole PE, Hilbers CW, Shulman RG. The molecular mechanism of thermal unfolding of Escherichia coli formylmethionine transfer RNA. Journal of Molecular Biology. 87: 63-88. PMID 4610153 DOI: 10.1016/0022-2836(74)90560-9 |
0.503 |
|
| 1974 |
Hilbers CW, Shulman RG. Assignment of the hydrogen bonded proton resonances in (Escherichia coli) tRNAGlu by sequential melting. Proceedings of the National Academy of Sciences of the United States of America. 71: 3239-42. PMID 4606251 |
0.537 |
|
| 1973 |
Hilbers CW, Shulman RG, Kim SH. High resolution NMR study of the melting of yeast tRNA Phe. Biochemical and Biophysical Research Communications. 55: 953-60. PMID 4586623 DOI: 10.1016/0006-291X(73)91235-7 |
0.471 |
|
| 1973 |
Shulman RG, Hilbers CW. Ring-current shifts in the 300 MHz nuclear magnetic resonance spectra of six purified transfer RNA molecules. Journal of Molecular Biology. 78: 57-69. PMID 4581295 |
0.483 |
|
| 1973 |
Shulman RG, Hilbers CW, Wong YP, Wong KL, Lightfoot DR, Reid BR, Kearns DR. Determination of secondary and tertiary structural features of transfer RNA molecules in solution by nuclear magnetic resonance. Proceedings of the National Academy of Sciences of the United States of America. 70: 2042-5. PMID 4579011 DOI: 10.1073/Pnas.70.7.2042 |
0.581 |
|
| 1973 |
Crothers DM, Hilbers CW, Shulman RG. Nuclear magnetic resonance study of hydrogen-bonded ring protons in Watson-Crick base pairs. Proceedings of the National Academy of Sciences of the United States of America. 70: 2899-901. PMID 4517943 DOI: 10.1073/Pnas.70.10.2899 |
0.522 |
|
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