| Year |
Citation |
Score |
| 2011 |
Feeney J, Birdsall B, Kovalevskaya NV, Smurnyy YD, Navarro Peran EM, Polshakov VI. NMR structures of apo L. casei dihydrofolate reductase and its complexes with trimethoprim and NADPH: contributions to positive cooperative binding from ligand-induced refolding, conformational changes, and interligand hydrophobic interactions. Biochemistry. 50: 3609-20. PMID 21410224 DOI: 10.1021/Bi200067T |
0.381 |
|
| 2007 |
Babon JJ, Morgan WD, Kelly G, Eccleston JF, Feeney J, Holder AA. Structural studies on Plasmodium vivax merozoite surface protein-1. Molecular and Biochemical Parasitology. 153: 31-40. PMID 17343930 DOI: 10.1016/J.Molbiopara.2007.01.015 |
0.314 |
|
| 2007 |
Kovalevskaya NV, Smurnyi ED, Birdsall B, Feeney J, Polshakov VI. Structural factors determining the binding selectivity of the antibacterial drug trimethoprim to dihydrofolate reductase Pharmaceutical Chemistry Journal. 41: 350-353. DOI: 10.1007/S11094-007-0079-1 |
0.378 |
|
| 2006 |
Polshakov VI, Birdsall B, Feeney J. Effects of co-operative ligand binding on protein amide NH hydrogen exchange. Journal of Molecular Biology. 356: 886-903. PMID 16405904 DOI: 10.1016/J.Jmb.2005.11.084 |
0.36 |
|
| 2006 |
Kovalevskaya N, Polshakov V, Birdsall B, Bradbury A, Frenkiel T, Feeney J. 1H, 15N and 13C resonance assignments of human dihydrofolate reductase in its complex with trimethoprim and NADPH Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr5981 |
0.377 |
|
| 2004 |
Martin SR, Biekofsky RR, Skinner MA, Guerrini R, Salvadori S, Feeney J, Bayley PM. Interaction of calmodulin with the phosphofructokinase target sequence. Febs Letters. 577: 284-8. PMID 15527800 DOI: 10.1016/J.Febslet.2004.10.023 |
0.314 |
|
| 2004 |
Biekofsky RR, Turjanski AG, Estrin DA, Feeney J, Pastore A. Ab initio study of NMR 15N chemical shift differences induced by Ca2+ binding to EF-hand proteins. Biochemistry. 43: 6554-64. PMID 15157088 DOI: 10.1021/Bi0497852 |
0.348 |
|
| 2003 |
Muskett FW, May FE, Westley BR, Feeney J. Solution structure of the disulfide-linked dimer of human intestinal trefoil factor (TFF3): the intermolecular orientation and interactions are markedly different from those of other dimeric trefoil proteins. Biochemistry. 42: 15139-47. PMID 14690424 DOI: 10.1021/Bi030182K |
0.339 |
|
| 2002 |
Biekofsky RR, Martin SR, McCormick JE, Masino L, Fefeu S, Bayley PM, Feeney J. Thermal stability of calmodulin and mutants studied by (1)H-(15)N HSQC NMR measurements of selectively labeled [(15)N]Ile proteins. Biochemistry. 41: 6850-9. PMID 12022890 DOI: 10.1021/Bi012187S |
0.345 |
|
| 2002 |
Polshakov VI, Biekofsky RR, Birdsall B, Feeney J. Towards understanding the origins of the different specificities of binding the reduced (NADPH) and oxidised (NADPH+) forms of nicotinamide adenine dinucleotide phosphate coenzyme to dihydrofolate reductase Journal of Molecular Structure. 602: 257-267. DOI: 10.1016/S0022-2860(01)00687-1 |
0.396 |
|
| 2001 |
Williams M, Polshakov V, Feeney J. 1H and 15N Chemical Shift Assignments for a Cys58Ser mutant of TFF1 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4933 |
0.347 |
|
| 2001 |
Williams M, Westley B, May F, Feeney J. 1H and 15N Chemical Shift Assignments for the homodimer of human TFF1 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4930 |
0.337 |
|
| 2000 |
Fefeu S, Biekofsky RR, McCormick JE, Martin SR, Bayley PM, Feeney J. Calcium-induced refolding of the calmodulin V136G mutant studied by NMR spectroscopy: evidence for interaction between the two globular domains. Biochemistry. 39: 15920-31. PMID 11123919 DOI: 10.1021/Bi001772A |
0.305 |
|
| 2000 |
Morgan WD, Kragt A, Feeney J. Expression of deuterium-isotope-labelled protein in the yeast pichia pastoris for NMR studies. Journal of Biomolecular Nmr. 17: 337-47. PMID 11014598 DOI: 10.1023/A:1008313530207 |
0.346 |
|
| 2000 |
Birdsall B, Polshakov VI, Feeney J. NMR studies of ligand carboxylate group interactions with arginine residues in complexes of Lactobacillus casei dihydrofolate reductase with substrates and substrate analogues. Biochemistry. 39: 9819-25. PMID 10933799 DOI: 10.1021/Bi000728S |
0.419 |
|
| 2000 |
Feeney J. NMR Studies of Ligand Binding to Dihydrofolate Reductase. Angewandte Chemie (International Ed. in English). 39: 290-312. PMID 10649397 DOI: 10.1002/(Sici)1521-3773(20000117)39:2<290::Aid-Anie290>3.0.Co;2-1 |
0.378 |
|
| 2000 |
Feeney J. NMR-Untersuchungen zur Ligandenbindung an Dihydrofolat-Reduktase Angewandte Chemie. 112: 298-321. DOI: 10.1002/(Sici)1521-3757(20000117)112:2<298::Aid-Ange298>3.0.Co;2-W |
0.377 |
|
| 1999 |
Polshakov VI, Birdsall B, Feeney J. Characterization of rates of ring-flipping in trimethoprim in its ternary complexes with Lactobacillus casei dihydrofolate reductase and coenzyme analogues. Biochemistry. 38: 15962-9. PMID 10625463 DOI: 10.1021/Bi9915263 |
0.363 |
|
| 1999 |
Polshakov VI, Morgan WD, Birdsall B, Feeney J. Validation of a new restraint docking method for solution structure determinations of protein-ligand complexes. Journal of Biomolecular Nmr. 14: 115-22. PMID 10610140 DOI: 10.1023/A:1008379225053 |
0.342 |
|
| 1999 |
Biekofsky RR, Muskett FW, Schmidt JM, Martin SR, Browne JP, Bayley PM, Feeney J. NMR approaches for monitoring domain orientations in calcium-binding proteins in solution using partial replacement of Ca2+ by Tb3+. Febs Letters. 460: 519-26. PMID 10556528 DOI: 10.1016/S0014-5793(99)01410-6 |
0.32 |
|
| 1999 |
Morgan WD, Birdsall B, Frenkiel TA, Gradwell MG, Burghaus PA, Syed SE, Uthaipibull C, Holder AA, Feeney J. Solution structure of an EGF module pair from the Plasmodium falciparum merozoite surface protein 1. Journal of Molecular Biology. 289: 113-22. PMID 10339410 DOI: 10.1006/Jmbi.1999.2753 |
0.34 |
|
| 1999 |
Polshakov VI, Birdsall B, Frenkiel TA, Gargaro AR, Feeney J. Structure and dynamics in solution of the complex of Lactobacillus casei dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate. Protein Science : a Publication of the Protein Society. 8: 467-81. PMID 10091649 DOI: 10.1110/Ps.8.3.467 |
0.409 |
|
| 1999 |
Morgan WD, Birdsall B, Nieto PM, Gargaro AR, Feeney J. 1H/15N HSQC NMR studies of ligand carboxylate group interactions with arginine residues in complexes of brodimoprim analogues and Lactobacillus casei dihydrofolate reductase. Biochemistry. 38: 2127-34. PMID 10026296 DOI: 10.1021/Bi982359U |
0.434 |
|
| 1998 |
Muskett FW, Frenkiel TA, Feeney J, Freedman RB, Carr MD, Williamson RA. High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3. The Journal of Biological Chemistry. 273: 21736-43. PMID 9705310 DOI: 10.1074/Jbc.273.34.21736 |
0.358 |
|
| 1998 |
McIntosh PB, Frenkiel TA, Wollborn U, McCormick JE, Klempnauer KH, Feeney J, Carr MD. Solution structure of the B-Myb DNA-binding domain: a possible role for conformational instability of the protein in DNA binding and control of gene expression. Biochemistry. 37: 9619-29. PMID 9657674 DOI: 10.1021/Bi972861Z |
0.345 |
|
| 1998 |
Biekofsky RR, Martin SR, Browne JP, Bayley PM, Feeney J. Ca2+ coordination to backbone carbonyl oxygen atoms in calmodulin and other EF-hand proteins: 15N chemical shifts as probes for monitoring individual-site Ca2+ coordination. Biochemistry. 37: 7617-29. PMID 9585577 DOI: 10.1021/Bi9800449 |
0.347 |
|
| 1998 |
Gargaro AR, Soteriou A, Frenkiel TA, Bauer CJ, Birdsall B, Polshakov VI, Barsukov IL, Roberts GC, Feeney J. The solution structure of the complex of Lactobacillus casei dihydrofolate reductase with methotrexate. Journal of Molecular Biology. 277: 119-34. PMID 9514736 DOI: 10.1006/Jmbi.1997.1560 |
0.395 |
|
| 1997 |
Williamson RA, Carr MD, Frenkiel TA, Feeney J, Freedman RB. Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation. Biochemistry. 36: 13882-9. PMID 9374866 DOI: 10.1021/Bi9712091 |
0.329 |
|
| 1997 |
Polshakov VI, Williams MA, Gargaro AR, Frenkiel TA, Westley BR, Chadwick MP, May FE, Feeney J. High-resolution solution structure of human pNR-2/pS2: a single trefoil motif protein. Journal of Molecular Biology. 267: 418-32. PMID 9096235 DOI: 10.1006/Jmbi.1997.0896 |
0.353 |
|
| 1997 |
Nieto PM, Birdsall B, Morgan WD, Frenkiel TA, Gargaro AR, Feeney J. Correlated bond rotations in interactions of arginine residues with ligand carboxylate groups in protein ligand complexes. Febs Letters. 405: 16-20. PMID 9094416 DOI: 10.1016/S0014-5793(97)00147-6 |
0.362 |
|
| 1997 |
Birdsall B, Casarotto MG, Cheung HT, Basran J, Roberts GC, Feeney J. The influence of aspartate 26 on the tautomeric forms of folate bound to Lactobacillus casei dihydrofolate reductase. Febs Letters. 402: 157-61. PMID 9037186 DOI: 10.1016/S0014-5793(96)01519-0 |
0.38 |
|
| 1996 |
Gradwell MJ, Feeney J. Validation of the use of intermolecular NOE constraints for obtaining docked structures of protein-ligand complexes. Journal of Biomolecular Nmr. 7: 48-58. PMID 8720831 DOI: 10.1007/Bf00190456 |
0.344 |
|
| 1996 |
Gargaro AR, Frenkiel TA, Nieto PM, Birdsall B, Polshakov VI, Morgan WD, Feeney J. NMR detection of arginine-ligand interactions in complexes of Lactobacillus casei dihydrofolate reductase. European Journal of Biochemistry / Febs. 238: 435-9. PMID 8681955 DOI: 10.1111/J.1432-1033.1996.0435Z.X |
0.403 |
|
| 1996 |
Carr MD, Wollborn U, McIntosh PB, Frenkiel TA, McCormick JE, Bauer CJ, Klempnauer KH, Feeney J. Structure of the B-Myb DNA-binding domain in solution and evidence for multiple conformations in the region of repeat-2 involved in DNA binding: implications for sequence-specific DNA binding by Myb proteins. European Journal of Biochemistry / Febs. 235: 721-35. PMID 8654422 DOI: 10.1111/J.1432-1033.1996.00721.X |
0.343 |
|
| 1996 |
Gerothanassis IP, Barrie PJ, Birdsall B, Feeney J. 31P solid-state NMR measurements used to detect interactions between NADPH and water and to determine the ionisation state of NADPH in a protein-ligand complex subjected to low-level hydration. European Journal of Biochemistry / Febs. 235: 262-6. PMID 8631340 DOI: 10.1111/J.1432-1033.1996.00262.X |
0.356 |
|
| 1995 |
Polshakov VI, Frenkiel TA, Westley B, Chadwick M, May F, Carr MD, Feeney J. NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure. European Journal of Biochemistry / Febs. 233: 847-55. PMID 8521850 DOI: 10.1111/J.1432-1033.1995.847_3.X |
0.393 |
|
| 1995 |
Morgan WD, Birdsall B, Polshakov VI, Sali D, Kompis I, Feeney J. Solution structure of a brodimoprim analogue in its complex with Lactobacillus casei dihydrofolate reductase. Biochemistry. 34: 11690-702. PMID 7547901 DOI: 10.1021/Bi00037A006 |
0.42 |
|
| 1995 |
Polshakov VI, Frenkiel TA, Birdsall B, Soteriou A, Feeney J. Determination of stereospecific assignments, torsion-angle constraints, and rotamer populations in proteins using the program AngleSearch. Journal of Magnetic Resonance. Series B. 108: 31-43. PMID 7542984 DOI: 10.1006/Jmrb.1995.1099 |
0.332 |
|
| 1995 |
Polshakov VI, Birdsall B, Gradwell MJ, Feeney J. The use of PM3 SCF MO quantum mechanical calculations to refine NMR-determined structures of complexes of antifolate drugs with dihydrofolate reductase in solution Journal of Molecular Structure: Theochem. 357: 207-216. DOI: 10.1016/0166-1280(95)04294-1 |
0.375 |
|
| 1994 |
Carr MD, Bauer CJ, Gradwell MJ, Feeney J. Solution structure of a trefoil-motif-containing cell growth factor, porcine spasmolytic protein Proceedings of the National Academy of Sciences of the United States of America. 91: 2206-2210. PMID 8134374 DOI: 10.1073/Pnas.91.6.2206 |
0.332 |
|
| 1994 |
Curtis N, Moore S, Birdsall B, Bloxsidge J, Gibson CL, Jones JR, Feeney J. 3H-n.m.r. studies of multiple conformations and dynamic processes in complexes of folate and methotrexate with Lactobacillus casei dihydrofolate reductase Biochemical Journal. 303: Pt 2/-. PMID 7980397 DOI: 10.1042/Bj3030401 |
0.403 |
|
| 1994 |
Gerothanassis IP, Barrie PJ, Birdsall B, Feeney J. 31P-NMR studies of NADPH, NADP+ and the complex of NADPH and methotrexate with Lactobacillus casei dihydrofolate reductase in the solid state. European Journal of Biochemistry / Febs. 226: 211-8. PMID 7957250 DOI: 10.1111/J.1432-1033.1994.0T211.X |
0.36 |
|
| 1994 |
Thomas JA, Arnold JR, Basran J, Andrews J, Roberts GC, Birdsall B, Feeney J. Effects of substitution of Thr63 by alanine on the structure and function of Lactobacillus casei dihydrofolate reductase. Protein Engineering. 7: 783-92. PMID 7937709 |
0.307 |
|
| 1994 |
Martorell G, Gradwell MJ, Birdsall B, Bauer CJ, Frenkiel TA, Cheung HT, Polshakov VI, Kuyper L, Feeney J. Solution structure of bound trimethoprim in its complex with Lactobacillus casei dihydrofolate reductase. Biochemistry. 33: 12416-26. PMID 7918464 DOI: 10.1021/Bi00207A008 |
0.414 |
|
| 1993 |
Cheung HTA, Birdsall B, Frenkiel TA, Chau DD, Feeney J. 13C NMR determination of the tautomeric and ionization states of folate in its complexes with Lactobacillus casei dihydrofolate reductase Biochemistry. 32: 6846-6854. PMID 8334117 DOI: 10.1021/Bi00078A007 |
0.394 |
|
| 1993 |
Eccleston JF, Molloy DP, Hinds MG, King RW, Feeney J. Conformational differences between complexes of elongation factor Tu studied 19F-NMR spectroscopy. European Journal of Biochemistry / Febs. 218: 1041-7. PMID 8281922 DOI: 10.1111/J.1432-1033.1993.Tb18463.X |
0.387 |
|
| 1992 |
Gerothanassis IP, Birdsall B, Bauer CJ, Feeney J. 31P-NMR assignment and conformational study of NADPH bound to Lactobacillus casei dihydrofolate reductase based on two-dimensional 1H-31P-heteronuclear and 1H-detected 1H-31P-shift-correlation experiments European Journal of Biochemistry. 204: 173-177. PMID 1740127 DOI: 10.1111/J.1432-1033.1992.Tb16620.X |
0.406 |
|
| 1992 |
Gerothanassis IP, Birdsall B, Bauer CJ, Frenkiel TA, Feeney J. Nuclear magnetic resonance detection of bound water molecules in the active site of Lactobacillus casei dihydrofolate reductase in aqueous solution Journal of Molecular Biology. 226: 549-554. PMID 1640465 DOI: 10.1016/0022-2836(92)90967-O |
0.357 |
|
| 1992 |
Cheung HTA, Birdsall B, Feeney J. 13C NMR studies of complexes of Escherichia coli dihydrofolate reductase formed with methotrexate and with folic acid Febs Letters. 312: 147-151. PMID 1426244 DOI: 10.1016/0014-5793(92)80923-5 |
0.405 |
|
| 1992 |
Hinds MG, King RW, Feeney J. 19F n.m.r. studies of conformational changes accompanying cyclic AMP binding to 3-fluorophenylalanine-containing cyclic AMP receptor protein from Escherichia coli. The Biochemical Journal. 287: 627-32. PMID 1332679 DOI: 10.1042/Bj2870627 |
0.357 |
|
| 1992 |
Chai W, Hounsell EF, Cashmore GC, Rosankiewicz JR, Feeney J, Lawson AM. Characterisation by mass spectrometry and 1H-NMR of novel hexasaccharides among the acidic O-linked carbohydrate chains of bovine submaxillary mucin European Journal of Biochemistry. 207: 973-980. PMID 1323463 DOI: 10.1111/J.1432-1033.1992.Tb17132.X |
0.338 |
|
| 1992 |
Feeney J. Development of high resolution NMR spectroscopy as a structural tool Advanced Optical Technologies. 10309. DOI: 10.1117/12.2283718 |
0.301 |
|
| 1992 |
Lawson M, Hounsell EF, Stoll MS, Feeney J, Chai W, Rosankiewics JR, Feizi T. Characterisation of minor tetra- to hepta-saccharides O-linked to human meconium glycoproteins by t.l.c.-m.c. and H-n.m.r. spectroscopy Carbohydrate Research. 228: C1. DOI: 10.1016/0008-6215(92)84141-E |
0.308 |
|
| 1991 |
Carr MD, Birdsall B, Frenkiel TA, Bauer CJ, Jimenez-Barbero J, Polshakov VI, McCormick JE, Roberts GCK, Feeney J. Dihydrofolate reductase: Sequential resonance assignments using 2D and 3D NMR and secondary structure determination in solution Biochemistry. 30: 6330-6341. PMID 1905571 |
0.324 |
|
| 1991 |
Gerothanassis IP, Birdsall B, Feeney J. Hydrogen bonding effects on 31P NMR shielding in the pyrophosphate group of NADPH bound to L. casei dihydrofolate reductase Febs Letters. 291: 21-23. PMID 1657637 DOI: 10.1016/0014-5793(91)81094-O |
0.347 |
|
| 1991 |
Hinds MG, King RW, Feeney J. 19F NMR evidence for interactions between the c-AMP binding sites on the c-AMP receptor protein from E. coli. Febs Letters. 283: 127-30. PMID 1645291 DOI: 10.1016/0014-5793(91)80569-O |
0.352 |
|
| 1990 |
Feeney J. NMR studies of interactions of ligands with dihydrofolate reductase Biochemical Pharmacology. 40: 141-152. PMID 2196881 DOI: 10.1016/0006-2952(90)90189-R |
0.354 |
|
| 1990 |
Sixl F, King RW, Bracken M, Feeney J. 19F-n.m.r. studies of ligand binding to 5-fluorotryptophan- and 3-fluorotyrosine-containing cyclic AMP receptor protein from Escherichia coli Biochemical Journal. 266: 545-552. PMID 2156500 DOI: 10.1042/Bj2660545 |
0.355 |
|
| 1990 |
Birdsall B, Tendler SJ, Arnold JR, Feeney J, Griffin RJ, Carr MD, Thomas JA, Roberts GC, Stevens MF. NMR studies of multiple conformations in complexes of Lactobacillus casei dihydrofolate reductase with analogues of pyrimethamine. Biochemistry. 29: 9660-7. PMID 2125479 |
0.306 |
|
| 1990 |
Feeney J, Birdsall B, Ostler G, Carr MD, Kairi M. A novel method of preparing totally α-deuterated amino acids for selective incorporation into proteins. Application to assignment of 1H resonances of valine residues in dihydrofolate reductase Febs Letters. 272: 197-199. PMID 2121536 DOI: 10.1016/0014-5793(90)80483-Y |
0.305 |
|
| 1990 |
Birdsall B, Arnold JR, Jimenez-Barbero J, Frenkiel TA, Bauer CJ, Tendler SJ, Carr MD, Thomas JA, Roberts GC, Feeney J. The 1H-NMR assignments of the aromatic resonances in complexes of Lactobacillus casei dihydrofolate reductase and the origins of their chemical shifts. European Journal of Biochemistry / Febs. 191: 659-68. PMID 2118112 DOI: 10.1111/J.1432-1033.1990.Tb19172.X |
0.443 |
|
| 1989 |
Jimenez MA, Arnold JR, Andrews J, Thomas JA, Roberts GC, Birdsall B, Feeney J. Dihydrofolate reductase: control of the mode of substrate binding by aspartate 26. Protein Engineering. 2: 627-31. PMID 2813337 DOI: 10.1093/Protein/2.8.627 |
0.396 |
|
| 1989 |
Walker JW, Feeney J, Trentham DR. Photolabile precursors of inositol phosphates. Preparation and properties of 1-(2-nitrophenyl)ethyl esters of myo-inositol 1,4,5-trisphosphate. Biochemistry. 28: 3272-80. PMID 2787165 DOI: 10.1021/Bi00434A023 |
0.312 |
|
| 1989 |
Hounsell EF, Lawson AM, Stoll MS, Kane DP, Cashmore GC, Carruthers RA, Feeney J, Feizi T. Characterisation by mass spectrometry and 500-MHz proton nuclear magnetic resonance spectroscopy of penta- and hexasaccharide chains of human foetal gastrointestinal mucins (meconium glycoproteins). European Journal of Biochemistry / Febs. 186: 597-610. PMID 2606107 DOI: 10.1111/J.1432-1033.1989.Tb15250.X |
0.317 |
|
| 1989 |
Birdsall B, Feeney J, Tendler SJB, Hammond SJ, Roberts GCK. Dihydrofolate reductase: Multiple conformations and alternative modes of substrate binding Biochemistry. 28: 2297-2305. PMID 2524214 |
0.328 |
|
| 1989 |
Andrews J, Fierke CA, Birdsall B, Ostler G, Feeney J, Roberts GC, Benkovic SJ. A kinetic study of wild-type and mutant dihydrofolate reductases from Lactobacillus casei. Biochemistry. 28: 5743-50. PMID 2505841 DOI: 10.1021/Bi00440A007 |
0.311 |
|
| 1989 |
Birdsall B, Andrews J, Ostler G, Tendler SJB, Feeney J, Roberts GCK, Davies RW, Cheung HTA. NMR studies of differences in the conformations and dynamics of ligand complexes formed with mutant dihydrofolate reductases Biochemistry. 28: 1353-1362. PMID 2496755 DOI: 10.1021/Bi00429A062 |
0.411 |
|
| 1989 |
Bowden K, Hall AD, Birdsall B, Feeney J, Roberts GCK. Interactions between inhibitors of dihydrofolate reductase Biochemical Journal. 258: 335-342. PMID 2495789 DOI: 10.1042/Bj2580335 |
0.354 |
|
| 1989 |
Feeney J, Birdsall B, Akiboye J, Tendler SJB, Barbero JJ, Ostler G, Arnold JRP, Roberts GCK, Kühn A, Roth K. Optimising selective deuteration of proteins for 2D 1H NMR detection and assignment studies Application to the Phe residues of Lactobacillus casei dihydrofolate reductase Febs Letters. 248: 57-61. DOI: 10.1016/0014-5793(89)80431-4 |
0.37 |
|
| 1988 |
Hounsell EF, Lawson AM, Feeney J, Cashmore GC, Kane DP, Stoll M, Feizi T. Identification of a novel oligosaccharide backbone structure with a galactose residue monosubstituted at C-6 in human foetal gastrointestinal mucins. The Biochemical Journal. 256: 397-401. PMID 3223919 DOI: 10.1042/Bj2560397 |
0.338 |
|
| 1988 |
Tendler SJB, Griffin RJ, Birdsall B, Stevens MFG, Roberts GCK, Feeney J. Direct 19F NMR observation of the conformational selection of optically active rotamers of the antifolate compound fluoronitropyrimethamine bound to the enzyme dihydrofolate reductase Febs Letters. 240: 201-204. PMID 3142793 DOI: 10.1016/0014-5793(88)80368-5 |
0.395 |
|
| 1988 |
Searle MS, Forster MJ, Birdsall B, Roberts GC, Feeney J, Cheung HT, Kompis I, Geddes AJ. Dynamics of trimethoprim bound to dihydrofolate reductase. Proceedings of the National Academy of Sciences of the United States of America. 85: 3787-91. PMID 3131763 DOI: 10.1073/Pnas.85.11.3787 |
0.601 |
|
| 1988 |
Hounsell EF, Feeney J, Scudder P. 500 MHz 1H n.m.r. of oligosaccharides of N-acetyl-lactosamine-type released from human erythrocyte glycopeptides by endo-β-galactosidase Biochemical Journal. 250: 9-13. PMID 3128279 DOI: 10.1042/Bj2500009 |
0.317 |
|
| 1988 |
Hounsell EF, Jones NJ, Gooi HC, Feizi T, Donald ASR, Feeney J. 500-MHz 1H-n.m.r. and conformational studies of fucosyloligosaccharides recognised by monoclonal antibodies with specificities related to Lea, Leb, and SSEA-1 Carbohydrate Research. 178: 67-78. PMID 2908539 DOI: 10.1016/0008-6215(88)80102-2 |
0.339 |
|
| 1987 |
Hammond SJ, Birdsall B, Feeney J, Searle MS, Roberts GC, Cheung HT. Structural comparisons of complexes of methotrexate analogues with Lactobacillus casei dihydrofolate reductase by two-dimensional 1H NMR at 500 MHz. Biochemistry. 26: 8585-90. PMID 3126805 DOI: 10.1021/Bi00400A014 |
0.622 |
|
| 1987 |
Birdsall B, De Graw J, Feeney J, Hammond S, Searle MS, Roberts GC, Colwell WT, Crase J. 15N and 1H NMR evidence for multiple conformations of the complex of dihydrofolate reductase with its substrate, folate. Febs Letters. 217: 106-10. PMID 3109940 DOI: 10.1016/0014-5793(87)81252-8 |
0.635 |
|
| 1986 |
Hughes RC, Feeney J. Ricin-resistant mutants of baby-hamster-kidney cells deficient in alpha-mannosidase-II-catalyzed processing of asparagine-linked oligosaccharides. Febs Journal. 158: 227-237. PMID 3732270 DOI: 10.1111/J.1432-1033.1986.Tb09742.X |
0.324 |
|
| 1986 |
Cheung HT, Searle MS, Feeney J, Birdsall B, Roberts GC, Kompis I, Hammond SJ. Trimethoprim binding to Lactobacillus casei dihydrofolate reductase: a 13C NMR study using selectively 13C-enriched trimethoprim. Biochemistry. 25: 1925-31. PMID 3085709 DOI: 10.1021/Bi00356A014 |
0.612 |
|
| 1986 |
Searle MS, Hammond SJ, Birdsall B, Roberts GC, Feeney J, King RW, Griffiths DV. Identification of the 1H resonances of valine and leucine residues in dihydrofolate reductase by using a combination of selective deuteration and two-dimensional correlation spectroscopy. Febs Letters. 194: 165-70. PMID 3079708 DOI: 10.1016/0014-5793(86)80070-9 |
0.616 |
|
| 1986 |
Hammond SJ, Birdsall B, Searle MS, Roberts GC, Feeney J. Dihydrofolate reductase. 1H resonance assignments and coenzyme-induced conformational changes. Journal of Molecular Biology. 188: 81-97. PMID 3012098 DOI: 10.1016/0022-2836(86)90483-3 |
0.64 |
|
| 1986 |
Hounsell EF, Feeney J, Scudder P, Tang PW, Feizi T. 1H-NMR studies at 500 MHz of a neutral disaccharide and sulphated di-, tetra-, hexa- and larger oligosaccharides obtained by endo-beta-galactosidase treatment of keratan sulphate. European Journal of Biochemistry / Febs. 157: 375-84. PMID 2940089 DOI: 10.1111/J.1432-1033.1986.Tb09679.X |
0.374 |
|
| 1985 |
Bevan AW, Roberts GCK, Feeney J, Kuyper L. 1H and 15N NMR studies of protonation and hydrogen-bonding in the binding of trimethoprim to dihydrofolate reductase. European Biophysics Journal. 11: 211. PMID 2985375 DOI: 10.1007/Bf00261997 |
0.394 |
|
| 1985 |
Charlton PA, Young DW, Birdsall B, Feeney J, Roberts GCK. Stereochemistry of reduction of the vitamin folic acid by dihydrofolate reductase Journal of the Chemical Society-Perkin Transactions 1. 16: 1349-1353. DOI: 10.1039/P19850001349 |
0.303 |
|
| 1984 |
Hounsell EF, Wright DJ, Donald AS, Feeney J. A computerized approach to the analysis of oligosaccharide structure by high-resolution proton n.m.r. The Biochemical Journal. 223: 129-43. PMID 6497836 DOI: 10.1042/Bj2230129 |
0.363 |
|
| 1984 |
Birdsall B, Feeney J, Pascual C, Roberts GCK, Kompis I, Then RL, Mueller K, Kroehn A. A 1H NMR study of the interactions and conformations of rationally designed brodimoprim analogues in complexes with Lactobacillus casei dihydrofolate reductase. Journal of Medicinal Chemistry. 27: 1672-1676. PMID 6438320 DOI: 10.1021/Jm00378A025 |
0.392 |
|
| 1984 |
Birdsall B, Bevan AW, Pascual C, Roberts GC, Feeney J, Gronenborn A, Clore GM. Multinuclear NMR characterization of two coexisting conformational states of the Lactobacillus casei dihydrofolate reductase-trimethoprim-NADP+ complex. Biochemistry. 23: 4733-42. PMID 6437442 DOI: 10.1021/Bi00315A032 |
0.454 |
|
| 1984 |
Birdsall B, Feeney J, Griffiths DV, Hammond S, Kimber B, King RW, Roberts GC, Searle M. The combined use of selective deuteration and double resonance experiments in assigning the 1H resonances of valine and tyrosine residues of dihydrofolate reductase. Febs Letters. 175: 364-8. PMID 6434351 DOI: 10.1016/0014-5793(84)80769-3 |
0.589 |
|
| 1984 |
Clore GM, Gronenborn AM, Birdsall B, Feeney J, Roberts GC. 19F-n.m.r. studies of 3',5'-difluoromethotrexate binding to Lactobacillus casei dihydrofolate reductase. Molecular motion and coenzyme-induced conformational changes. The Biochemical Journal. 217: 659-66. PMID 6424648 DOI: 10.1042/Bj2170659 |
0.352 |
|
| 1983 |
Birdsall B, Gronenborn A, Hyde EI, Clore GM, Roberts GC, Feeney J, Burgen AS. Hydrogen-1, carbon-13, and phosphorus-31 nuclear magnetic resonance studies of the dihydrofolate reductase-nicotinamide adenine dinucleotide phosphate-folate complex: characterization of three coexisting conformational states. Biochemistry. 21: 5831-8. PMID 6817782 DOI: 10.1021/Bi00266A017 |
0.363 |
|
| 1982 |
Mansour TE, Morris PG, Feeney J, Roberts GC. A 31P-nmr study of the intact liver fluke Fasciola hepatica. Biochimica Et Biophysica Acta. 721: 336-40. PMID 7159598 DOI: 10.1016/0167-4889(82)90087-8 |
0.31 |
|
| 1982 |
Birdsall B, Gronenborn A, Clore GM, Roberts GC, Feeney J, Burgen AS. 13C NMR evidence for three slowly interconverting conformations of the dihydrofolate reductase-NADP+-folate complex. Biochemical and Biophysical Research Communications. 101: 1139-44. PMID 6796080 DOI: 10.1016/0006-291X(81)91566-7 |
0.351 |
|
| 1982 |
Rawson BJ, Feeney J, Kimber BJ, Greven HM. 1 H nuclear magnetic resonance studies of the conformations of adrenocorticotropic hormone ACTH(1–10) and related peptides in aqueous and trifluoroethanol solutions Journal of the Chemical Society-Perkin Transactions 1. 14: 1471-1477. DOI: 10.1039/P29820001471 |
0.388 |
|
| 1981 |
Birdsall B, Gronenborn A, Hyde EI, Roberts GC, Feeney J, Burgen AS. Demonstration and characterization of two co-existing conformations of an enzyme complex by n.m.r. Biochemical Society Transactions. 8: 637. PMID 7450269 DOI: 10.1042/Bst0080637 |
0.353 |
|
| 1981 |
Birdsall B, Burgen ASV, Hyde EI, Roberts GCK, Feeney J. Negative cooperativity between folinic acid and coenzyme in their binding to L. casei dihydrofolate reductase Biochemistry. 20: 7186-7195. PMID 6797469 DOI: 10.1021/Bi00528A021 |
0.376 |
|
| 1981 |
Gronenborn A, Birdsall B, Hyde EI, Roberts GC, Feeney J, Burgen AS. Effects of coenzyme binding on histidine residues of Lactobacillus casei dihydrofolate reductase. Biochemistry. 20: 1717-22. PMID 6784757 DOI: 10.1021/Bi00510A003 |
0.414 |
|
| 1981 |
Bongini A, Feeney J, Williamson MP, Williams DH. Assignment of the carbon-13 spectrum of vancomycin and its derivatives Journal of the Chemical Society-Perkin Transactions 1. 12: 201-206. DOI: 10.1039/P29810000201 |
0.349 |
|
| 1981 |
Gronenborn A, Birdsall B, Hyde EI, Roberts GCK, Feeney J, Burgen ASV. Direct observation by NMR of two coexisting conformations of an enzyme–ligand complex in solution Nature. 290: 273-274. DOI: 10.1038/290273A0 |
0.411 |
|
| 1981 |
Clore G, Roberts G, Gronenborn A, Birdsall B, Feeney J. Transfer-of-saturation NMR studies of protein-ligand complexes. Three-site exchange Journal of Magnetic Resonance (1969). 45: 151-161. DOI: 10.1016/0022-2364(81)90109-8 |
0.363 |
|
| 1980 |
Birdsall B, Feeney J, Roberts GCK, Burgen ASV. The use of saturation transfer NMR experiments to monitor the conformational selection accompanying ligand—protein interactions Febs Letters. 120: 107-109. PMID 6777193 DOI: 10.1016/0014-5793(80)81057-X |
0.321 |
|
| 1980 |
Hyde EI, Birdsall B, Roberts GCK, Feeney J, Burgen ASV. Phosphorus-31 nuclear magnetic resonance studies of the binding of oxidized coenzymes to Lactobacillus casei dihydrofolate reductase. Biochemistry. 19: 3746-3754. PMID 6773551 DOI: 10.1021/Bi00557A016 |
0.431 |
|
| 1980 |
Hyde EI, Birdsall B, Roberts GCK, Feeney J, Burgen ASV. Proton nuclear magnetic resonance saturation transfer studies of coenzyme binding to Lactobacillus casei dihydrofolate reductase. Biochemistry. 19: 3738-3746. PMID 6773550 DOI: 10.1021/Bi00557A015 |
0.411 |
|
| 1980 |
Wyeth P, Gronenborn A, Birdsall B, Roberts GC, Feeney J, Burgen AS. Histidine residues of Lactobacillus casei dihydrofolate reductase: paramagnetic relaxation and deuterium-exchange studies and partial assignments. Biochemistry. 19: 2608-15. PMID 6772202 DOI: 10.1021/Bi00553A012 |
0.355 |
|
| 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 |
0.376 |
|
| 1980 |
Convert O, Bongini A, Feeney J. A 1H nuclear magnetic resonance study of the interactions of vancomycin with N-acetyl-D-alanyl-D-alanine and related peptides Journal of the Chemical Society-Perkin Transactions 1. 11: 1262-1270. DOI: 10.1039/P29800001262 |
0.377 |
|
| 1980 |
Feeney J, Albrand JP, Boicelli CA, Charlton PA, Young DW. Conformational studies on 5-formyl-5,6,7,8-tetrahydrofolic acid (folinic acid) using 1H and 13C nuclear magnetic resonance measurements: two interconverting conformations Journal of the Chemical Society-Perkin Transactions 1. 11: 176-180. DOI: 10.1039/P29800000176 |
0.421 |
|
| 1980 |
Cayley PJ, Feeney J, Kimber BJ. 31P n.m.r. studies of complexes of NADPH and NADP+ with Escherichia coli dihydrofolate reductase International Journal of Biological Macromolecules. 2: 251-255. DOI: 10.1016/0141-8130(80)90084-7 |
0.376 |
|
| 1979 |
Degelaen J, Feeney J, Roberts GCK, Burgen ASV, Frère J, Ghuysen J. NMR evidence for the structure of the complex between penicillin and the DD-carboxypeptidase of Streptomyces R61. Febs Letters. 98: 53-56. PMID 428542 DOI: 10.1016/0014-5793(79)80150-7 |
0.331 |
|
| 1979 |
Kalman JR, Blake TJ, Williams DH, Feeney J, Roberts GCK. The conformations of triostin A in solution Journal of the Chemical Society-Perkin Transactions 1. 10: 1313-1321. DOI: 10.1039/P19790001313 |
0.366 |
|
| 1979 |
Albrand J, Birdsall B, Feeney J, Roberts G, Burgen A. The use of transferred nuclear Overhauser effects in the study of the conformations of small molecules bound to proteins International Journal of Biological Macromolecules. 1: 37-41. DOI: 10.1016/0141-8130(79)90008-4 |
0.373 |
|
| 1979 |
Feeney J, Batchelor J, Albrand J, Roberts G. The effects of intermediate exchange processes on the estimation of equilibrium constants by NMR Journal of Magnetic Resonance (1969). 33: 519-529. DOI: 10.1016/0022-2364(79)90163-X |
0.317 |
|
| 1978 |
Kimber BJ, Feeney J, Roberts GC, Birdsall B, Griffiths DV, Burgen AS, Sykes BD. Proximity of two tryptophan residues in dihydrofolate reductase determined by 19f NMR. Nature. 271: 184-5. PMID 622158 DOI: 10.1038/271184A0 |
0.402 |
|
| 1977 |
Birdsall B, Roberts GCK, Feeney J, Burgen ASV. 31P NMR studies of the binding of adenosine-2'-phosphate to Lactobacillus casei dihydrofolate reductase. Febs Letters. 80: 313-316. PMID 19299 DOI: 10.1016/0014-5793(77)80465-1 |
0.332 |
|
| 1977 |
Feeney J, Roberts GC, Birdsall B, Griffiths DV, King RW, Scudder P, Burgen A. 1H nuclear magnetic resonance studies of the tyrosine residues of selectively deuterated Lactobacillus casei dihydrofolate reductase. Proceedings of the Royal Society of London. Series B, Biological Sciences. 196: 267-90. PMID 16269 DOI: 10.1098/Rspb.1977.0041 |
0.429 |
|
| 1977 |
Birdsall B, Griffiths DV, Roberts GC, Feeney J, Burgen A. 1H nuclear magnetic resonance studies of Lactobacillus casei dihydrofolate reductase: effects of substrate and inhibitor binding on the histidine residues. Proceedings of the Royal Society of London. Series B, Biological Sciences. 196: 251-65. PMID 16268 DOI: 10.1098/Rspb.1977.0040 |
0.37 |
|
| 1977 |
Feeney J, Foster R, Piper EA. Nuclear magnetic resonance study of the conformations of atropine and scopolamine cations in aqueous solution Journal of the Chemical Society-Perkin Transactions 1. 9: 2016-2020. DOI: 10.1039/P29770002016 |
0.399 |
|
| 1977 |
Boicelli CA, Bradbury AF, Feeney J. Nuclear magnetic resonance conformational studies of the Cα–Cβ fragments of oxytocin, oxytocinoic acid, and tocinoic acid in aqueous solution Journal of the Chemical Society-Perkin Transactions 1. 8: 477-482. DOI: 10.1039/P29770000477 |
0.385 |
|
| 1976 |
Griffiths DV, Feeney J, Roberts GC, Burgen AS. Preparation of selectively deuterated aromatic amino acids for use in 1H NMR studies of proteins. Biochimica Et Biophysica Acta. 446: 479-85. PMID 990287 DOI: 10.1016/0005-2795(76)90014-3 |
0.322 |
|
| 1975 |
Birdsall B, Birdsall NJM, Feeney J, Thornton J. A nuclear magnetic resonance investigation of the conformation of nicotinamide mononucleotide in aqueous solution. Journal of the American Chemical Society. 97: 2845-2850. PMID 1133337 DOI: 10.1021/Ja00843A039 |
0.322 |
|
| 1975 |
Burgen ASV, Roberts GCK, Feeney J. Binding of flexible ligands to macromolecules Nature. 253: 753-755. PMID 1113874 DOI: 10.1038/253753A0 |
0.365 |
|
| 1975 |
Feeney J, Birdsall B, Roberts GCK, Burgen ASV. 31P NMR studies of NADPH and NADP+ binding to L. casei dihydrofolate reductase Nature. 257: 564-566. PMID 241022 DOI: 10.1038/257564A0 |
0.395 |
|
| 1975 |
Hansen P, Feeney J, Roberts G. Long range 13C1H spin-spin coupling constants in amino acids. Conformational applications Journal of Magnetic Resonance (1969). 17: 249-261. DOI: 10.1016/0022-2364(75)90186-9 |
0.344 |
|
| 1975 |
BIRDSALL B, BIRDSALL NJM, FEENEY J, THORNTON J. ChemInform Abstract: A NUCLEAR MAGNETIC RESONANCE INVESTIGATION OF THE CONFORMATION OF NICOTINAMIDE MONONUCLEOTIDE IN AQUEOUS SOLUTION Chemischer Informationsdienst. 6. DOI: 10.1002/Chin.197530087 |
0.326 |
|
| 1974 |
Bradbury AF, Burgen ASV, Feeney J, Roberts GCK, Smyth DG. Unequivocal assignments of NH proton magnetic resonance bands in oxytocin using 2H- and 15N-substituted molecules Febs Letters. 42: 179-182. PMID 4855316 DOI: 10.1016/0014-5793(74)80780-5 |
0.351 |
|
| 1974 |
Roberts GCK, Feeney J, Burgen ASV, Yuferov V, Dann JG, Bjur R. Nuclear magnetic resonance studies of the binding of substrate analogs and coenzyme to dihydrofolate reductase from Lactobacillus casei. Biochemistry. 13: 5351-5357. PMID 4154775 DOI: 10.1021/Bi00723A015 |
0.331 |
|
| 1974 |
Feeney J, Hansen PE, Roberts GCK. Use of 13C-1H spin-coupling constants in the determination of side-chain conformations of amino-acids Journal of the Chemical Society, Chemical Communications. 465-466. DOI: 10.1039/C39740000465 |
0.336 |
|
| 1974 |
Feeney J, Partington P, Roberts G. The assignment of carbon-13 resonances from carbonyl groups in peptides Journal of Magnetic Resonance (1969). 13: 268-274. DOI: 10.1016/0022-2364(74)90021-3 |
0.39 |
|
| 1973 |
Feeney J, Burgen SV, Grell E. Cyanide binding to carbonic anhydrase. A 13 C-nuclear-magnetic-resonance study. European Journal of Biochemistry / Febs. 34: 107-11. PMID 4633799 DOI: 10.1111/J.1432-1033.1973.Tb02735.X |
0.388 |
|
| 1973 |
Birdsall B, Feeney J, Partington P. Ionisation, self association, and proton exchange studies of nicotinamide in aqueous solution using nuclear magnetic resonance spectroscopy Journal of the Chemical Society-Perkin Transactions 1. 5: 2145-2151. DOI: 10.1039/P29730002145 |
0.375 |
|
| 1973 |
Wessels PL, Feeney J, Gregory H, Gormley JJ. High resolution nuclear magnetic resonance studies of the conformation of luteinizing hormone releasing hormone (LH-RH) and its component peptides Journal of the Chemical Society-Perkin Transactions 1. 4: 1691-1698. DOI: 10.1039/P29730001691 |
0.376 |
|
| 1973 |
Feeney J, Partington P. Pseudo INDOR nuclear magnetic resonance spectra using double resonance difference spectroscopy and the Fourier transform technique Journal of the Chemical Society, Chemical Communications. 611-612. DOI: 10.1039/C39730000611 |
0.317 |
|
| 1972 |
Birdsall NJM, Feeney J, Lee AG, Levine YK, Metcalfe JC. Dipalmitoyl-lecithin: assignment of the 1H and 13C nuclear magnetic resonance spectra, and conformational studies Journal of the Chemical Society-Perkin Transactions 1. 1441-1445. DOI: 10.1039/P29720001441 |
0.436 |
|
| 1972 |
Feeney J, Roberts GCK, Brown JP, Burgen ASV, Gregory H. Conformational study of some component peptides of pentagastrin Journal of the Chemical Society-Perkin Transactions 1. 601-604. DOI: 10.1039/P29720000601 |
0.389 |
|
| 1972 |
BIRDSALL NJM, FEENEY J, LEE AG, METCALFE JC, LEVINE YK. ChemInform Abstract: DIPALMITOYLLECITHIN, ZUORDNUNG DER (1)H- UND (13)C-NMR-SPEKTREN UND UNTERSUCHUNG DER KONFORM. Chemischer Informationsdienst. 3. DOI: 10.1002/Chin.197245099 |
0.347 |
|
| 1971 |
Feeney J, Roberts GCK, Rockey JH, Burgen ASV. Conformational studies of oxytocin and lysine vasopressin in aqueous solution using high resolution NMR spectroscopy. Nature. 232: 108-110. PMID 5284945 DOI: 10.1038/Newbio232108A0 |
0.381 |
|
| 1971 |
Metcalfe JC, Birdsall NJM, Feeney J, Lee AG, Levine YK, Partington P. 13 C NMR Spectra of Lecithin Vesicles and Erythrocyte Membranes Nature. 233: 199-201. PMID 4939181 DOI: 10.1038/233199A0 |
0.402 |
|
| 1968 |
Feeney J, Sutcliffe L. Long range coupling involving alkoxy protons in vinyl ethers Spectrochimica Acta Part a: Molecular Spectroscopy. 24: 1135-1137. DOI: 10.1016/0584-8539(68)80133-3 |
0.47 |
|
| 1966 |
Feeney J, Sutcliffe L, Walker S. Calculations of chemical shifts Molecular Physics. 11: 145-152. DOI: 10.1080/00268976600100971 |
0.495 |
|
| 1966 |
Feeney J, Sutcliffe LH, Walker SM. Calculations of chemical shifts Molecular Physics. 11: 137-143. DOI: 10.1080/00268976600100961 |
0.495 |
|
| 1966 |
Feeney J, Sutcliffe L, Walker S. Calculations of chemical shifts Molecular Physics. 11: 129-135. DOI: 10.1080/00268976600100951 |
0.495 |
|
| 1966 |
Feeney J, Sutcliffe L, Walker S. Calculations of chemical shifts Molecular Physics. 11: 117-128. DOI: 10.1080/00268976600100941 |
0.495 |
|
| 1966 |
Feeney J, Sutcliffe LH, Walker SM. Coupling constants in fluorinated cyclic compounds. Part 2.—Fluorocyclopentenes and perfluorocyclohexadiene-1,3 Trans. Faraday Soc.. 62: 2969-2979. DOI: 10.1039/TF9666202969 |
0.451 |
|
| 1966 |
Feeney J, Sutcliffe LH, Walker SM. Coupling constants of fluorinated cyclic compounds. Part 1.—1,2,4-trichloroheptafluorocyclohexene Trans. Faraday Soc.. 62: 2650-2654. DOI: 10.1039/TF9666202650 |
0.452 |
|
| 1965 |
Boden N, Feeney J, Sutcliffe L. The 19F resonance spectrum of perfluorovinylsulphur pentafluoride Spectrochimica Acta. 21: 627-632. DOI: 10.1016/0371-1951(65)80018-2 |
0.474 |
|
| 1964 |
Boden N, Emsley JW, Feeney J, Sutcliffe LH. The n.m.r. spectrum and configuration of decafluorobiphenyl Molecular Physics. 8: 467-471. DOI: 10.1080/00268976400100511 |
0.477 |
|
| 1964 |
Boden N, Emsley JW, Feeney J, Sutcliffe LH. The effects of π-electron distribution and intramolecular electric fields on the 19f n.m.r. shielding in substituted perfluorobenzenes Molecular Physics. 8: 133-149. DOI: 10.1080/00268976400100171 |
0.466 |
|
| 1963 |
Boden N, Emsley JW, Feeney J, Sutcliffe LH. N.M.R. spectra of some aliphatic sulphur pentafluorides Transactions of the Faraday Society. 59: 620-629. DOI: 10.1039/TF9635900620 |
0.492 |
|
| 1961 |
Feeney J, Sutcliffe LH. CONFORMATION OF FLUORINATED CYCLOHEXANES The Journal of Physical Chemistry. 65: 1894-1895. DOI: 10.1021/j100827a502 |
0.514 |
|
| 1960 |
Feeney J, Sutcliffe LH. The nuclear magnetic resonance spectra of some fluorinated cyclohexanes Transactions of the Faraday Society. 56: 1559. DOI: 10.1039/TF9605601559 |
0.498 |
|
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