Year |
Citation |
Score |
2006 |
Frank DJ, Martin SR, Gruender BN, Lee YS, Simonette RA, Bayley PM, Miller KG, Beckingham KM. Androcam is a tissue-specific light chain for myosin VI in the Drosophila testis. The Journal of Biological Chemistry. 281: 24728-36. PMID 16790438 DOI: 10.1074/Jbc.M602094200 |
0.336 |
|
2004 |
Wang B, Martin SR, Newman RA, Hamilton SL, Shea MA, Bayley PM, Beckingham KM. Biochemical properties of V91G calmodulin: A calmodulin point mutation that deregulates muscle contraction in Drosophila. Protein Science : a Publication of the Protein Society. 13: 3285-97. PMID 15557269 DOI: 10.1110/Ps.04928204 |
0.322 |
|
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 |
0.333 |
|
2004 |
Martin SR, Bayley PM. Calmodulin bridging of IQ motifs in myosin-V. Febs Letters. 567: 166-70. PMID 15178316 DOI: 10.1016/J.Febslet.2004.04.053 |
0.354 |
|
2004 |
Haire LF, Whyte SM, Vasisht N, Gill AC, Verma C, Dodson EJ, Dodson GG, Bayley PM. The crystal structure of the globular domain of sheep prion protein. Journal of Molecular Biology. 336: 1175-83. PMID 15037077 DOI: 10.1016/J.Jmb.2003.12.059 |
0.325 |
|
2003 |
Bayley P, Martin S, Browne P, Royer C. Time-resolved fluorescence anisotropy studies show domain-specific interactions of calmodulin with IQ target sequences of myosin V. European Biophysics Journal : Ebj. 32: 122-7. PMID 12734700 DOI: 10.1007/S00249-002-0274-7 |
0.368 |
|
2003 |
Whyte SM, Sylvester ID, Martin SR, Gill AC, Wopfner F, Schätzl HM, Dodson GG, Bayley PM. Stability and conformational properties of doppel, a prion-like protein, and its single-disulphide mutant. The Biochemical Journal. 373: 485-94. PMID 12665426 DOI: 10.1042/Bj20021911 |
0.341 |
|
2003 |
Kleinjung J, Fraternali F, Martin SR, Bayley PM. Thermal unfolding simulations of apo-calmodulin using leap-dynamics. Proteins. 50: 648-56. PMID 12577271 DOI: 10.1002/Prot.10331 |
0.313 |
|
2002 |
Rabl CR, Martin SR, Neumann E, Bayley PM. Temperature jump kinetic study of the stability of apo-calmodulin. Biophysical Chemistry. 101: 553-64. PMID 12488026 DOI: 10.1016/S0301-4622(02)00150-3 |
0.311 |
|
2002 |
Clapperton JA, Martin SR, Smerdon SJ, Gamblin SJ, Bayley PM. Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: studies of the kinase activation mechanism. Biochemistry. 41: 14669-79. PMID 12475216 DOI: 10.1021/Bi026660T |
0.376 |
|
2002 |
Martin SR, Bayley PM. Regulatory implications of a novel mode of interaction of calmodulin with a double IQ-motif target sequence from murine dilute myosin V. Protein Science : a Publication of the Protein Society. 11: 2909-23. PMID 12441389 DOI: 10.1110/Ps.0210402 |
0.382 |
|
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 |
0.374 |
|
2001 |
Feeny J, Birdsall B, Bradbury AF, Biekofsky RR, Bayley PM. Calmodulin tagging provides a general method of using lanthanide induced magnetic field orientation to observe residual dipolar couplings in proteins in solution. Journal of Biomolecular Nmr. 21: 41-8. PMID 11693567 DOI: 10.1023/A:1011924017938 |
0.335 |
|
2000 |
Martin SR, Masino L, Bayley PM. Enhancement by Mg2+ of domain specificity in Ca2+-dependent interactions of calmodulin with target sequences. Protein Science : a Publication of the Protein Society. 9: 2477-88. PMID 11206069 DOI: 10.1110/Ps.9.12.2477 |
0.345 |
|
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 |
0.371 |
|
2000 |
Masino L, Martin SR, Bayley PM. Ligand binding and thermodynamic stability of a multidomain protein, calmodulin. Protein Science : a Publication of the Protein Society. 9: 1519-29. PMID 10975573 DOI: 10.1110/Ps.9.8.1519 |
0.373 |
|
2000 |
Kleinjung J, Bayley P, Fraternali F. Leap-dynamics: efficient sampling of conformational space of proteins and peptides in solution. Febs Letters. 470: 257-62. PMID 10745078 DOI: 10.1016/S0014-5793(00)01295-3 |
0.314 |
|
1999 |
Martin SR, Lu AQ, Xiao J, Kleinjung J, Beckingham K, Bayley PM. Conformational and metal-binding properties of androcam, a testis-specific, calmodulin-related protein from Drosophila. Protein Science : a Publication of the Protein Society. 8: 2444-54. PMID 10595548 DOI: 10.1110/Ps.8.11.2444 |
0.364 |
|
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 |
0.335 |
|
1999 |
Erent M, Pagakis S, Browne JP, Bayley P. Association of calmodulin with cytoskeletal structures at different stages of HeLa cell division, visualized by a calmodulin-EGFP fusion protein. Molecular Cell Biology Research Communications : McBrc. 1: 209-15. PMID 10425228 DOI: 10.1006/Mcbr.1999.0137 |
0.318 |
|
1999 |
Vandecandelaere A, Brune M, Webb MR, Martin SR, Bayley PM. Phosphate release during microtubule assembly: what stabilizes growing microtubules? Biochemistry. 38: 8179-88. PMID 10387063 DOI: 10.1021/Bi9830765 |
0.36 |
|
1998 |
Barth A, Martin SR, Bayley PM. Resolution of Trp near UV CD spectra of calmodulin-domain peptide complexes into the 1La and 1Lb component spectra. Biopolymers. 45: 493-501. PMID 9577230 DOI: 10.1002/(Sici)1097-0282(199806)45:7<493::Aid-Bip3>3.0.Co;2-J |
0.309 |
|
1998 |
Barth A, Martin SR, Bayley PM. Specificity and symmetry in the interaction of calmodulin domains with the skeletal muscle myosin light chain kinase target sequence. The Journal of Biological Chemistry. 273: 2174-83. PMID 9442059 DOI: 10.1074/Jbc.273.4.2174 |
0.359 |
|
1998 |
Bayley P. Biophysical studies of the cytoskeleton: Editorial European Biophysics Journal. 27: 429-430. DOI: 10.1007/S002490050152 |
0.313 |
|
1997 |
Browne JP, Strom M, Martin SR, Bayley PM. The role of beta-sheet interactions in domain stability, folding, and target recognition reactions of calmodulin. Biochemistry. 36: 9550-61. PMID 9236001 DOI: 10.1021/Bi970460D |
0.396 |
|
1997 |
Utton MA, Vandecandelaere A, Wagner U, Reynolds CH, Gibb GM, Miller CC, Bayley PM, Anderton BH. Phosphorylation of tau by glycogen synthase kinase 3beta affects the ability of tau to promote microtubule self-assembly. The Biochemical Journal. 323: 741-7. PMID 9169608 DOI: 10.1042/Bj3230741 |
0.3 |
|
1997 |
Brown SE, Martin SR, Bayley PM. Kinetic control of the dissociation pathway of calmodulin-peptide complexes. The Journal of Biological Chemistry. 272: 3389-97. PMID 9013581 DOI: 10.1074/Jbc.272.6.3389 |
0.323 |
|
1996 |
Vandecandelaere A, Pedrotti B, Utton MA, Calvert RA, Bayley PM. Differences in the regulation of microtubule dynamics by microtubule-associated proteins MAP1B and MAP2. Cell Motility and the Cytoskeleton. 35: 134-46. PMID 8894283 DOI: 10.1002/(Sici)1097-0169(1996)35:2<134::Aid-Cm6>3.0.Co;2-A |
0.309 |
|
1996 |
Bayley PM, Findlay WA, Martin SR. Target recognition by calmodulin: dissecting the kinetics and affinity of interaction using short peptide sequences. Protein Science : a Publication of the Protein Society. 5: 1215-28. PMID 8819155 DOI: 10.1002/Pro.5560050701 |
0.374 |
|
1996 |
Martin SR, Bayley PM, Brown SE, Porumb T, Zhang M, Ikura M. Spectroscopic characterization of a high-affinity calmodulin-target peptide hybrid molecule. Biochemistry. 35: 3508-17. PMID 8639501 DOI: 10.1021/Bi952522A |
0.382 |
|
1995 |
Findlay WA, Gradwell MJ, Bayley PM. Role of the N-terminal region of the skeletal muscle myosin light chain kinase target sequence in its interaction with calmodulin. Protein Science : a Publication of the Protein Society. 4: 2375-82. PMID 8563635 DOI: 10.1002/Pro.5560041116 |
0.365 |
|
1995 |
Findlay WA, Martin SR, Beckingham K, Bayley PM. Recovery of native structure by calcium binding site mutants of calmodulin upon binding of sk-MLCK target peptides. Biochemistry. 34: 2087-94. PMID 7857920 DOI: 10.1021/Bi00007A001 |
0.367 |
|
1995 |
Vandecandelaere A, Martin SR, Bayley PM. Regulation of microtubule dynamic instability by tubulin-GDP. Biochemistry. 34: 1332-43. PMID 7827081 DOI: 10.1021/Bi00004A028 |
0.342 |
|
1995 |
Findlay WA, Martin SR, Bayley PM. Investigating calmodulin-target sequence interactions using mutant proteins and synthetic target peptides Techniques in Protein Chemistry. 6: 401-408. DOI: 10.1016/S1080-8914(06)80049-9 |
0.35 |
|
1993 |
Martin SR, Schilstra MJ, Bayley PM. Dynamic instability of microtubules: Monte Carlo simulation and application to different types of microtubule lattice. Biophysical Journal. 65: 578-96. PMID 8218889 DOI: 10.1016/S0006-3495(93)81091-9 |
0.362 |
|
1992 |
Martin SR, Maune JF, Beckingham K, Bayley PM. Stopped-flow studies of calcium dissociation from calcium-binding-site mutants of Drosophila melanogaster calmodulin. European Journal of Biochemistry / Febs. 205: 1107-14. PMID 1576994 DOI: 10.1111/J.1432-1033.1992.Tb16879.X |
0.374 |
|
1992 |
Török K, Lane AN, Martin SR, Janot JM, Bayley PM. Effects of calcium binding on the internal dynamic properties of bovine brain calmodulin, studied by NMR and optical spectroscopy. Biochemistry. 31: 3452-62. PMID 1554727 DOI: 10.1021/Bi00128A020 |
0.343 |
|
1992 |
Maune JF, Beckingham K, Martin SR, Bayley PM. Circular dichroism studies on calcium binding to two series of Ca2+ binding site mutants of Drosophila melanogaster calmodulin. Biochemistry. 31: 7779-86. PMID 1510964 DOI: 10.1021/Bi00149A006 |
0.365 |
|
1991 |
Janot JM, Beeby A, Bayley PM, Phillips D. The time resolved fluorescence and anisotropy of subtilisins BPN' and Carlsberg. Biophysical Chemistry. 41: 277-87. PMID 17014795 DOI: 10.1016/0301-4622(91)85042-O |
0.346 |
|
1991 |
Martin SR, Schilstra MJ, Bayley PM. Opposite-end behaviour of dynamic microtubules. Biochimica Et Biophysica Acta. 1073: 555-61. PMID 2015279 DOI: 10.1016/0304-4165(91)90230-E |
0.347 |
|
1991 |
Bayley PM, Martin SR. Microtubule dynamic instability: some possible physical mechanisms and their implications. Biochemical Society Transactions. 19: 1023-8. PMID 1794459 DOI: 10.1042/Bst0191023 |
0.343 |
|
1991 |
Schilstra MJ, Bayley PM, Martin SR. The effect of solution composition on microtubule dynamic instability. The Biochemical Journal. 277: 839-47. PMID 1678598 DOI: 10.1042/Bj2770839 |
0.339 |
|
1990 |
Martin SR, Linse S, Johansson C, Bayley PM, Forsén S. Protein surface charges and Ca2+ binding to individual sites in calbindin D9k: stopped-flow studies. Biochemistry. 29: 4188-93. PMID 2193686 DOI: 10.1021/Bi00469A023 |
0.37 |
|
1989 |
Forsén S, Akke M, Brodin P, Bayley P, Drakenberg T, Grundström T, Johansson C, Linse S, Martin S, Thulin E. Neutralization of surface charges markedly affects the properties of bovine calbindin D9k. Advances in Experimental Medicine and Biology. 255: 185-94. PMID 2618856 DOI: 10.1007/978-1-4684-5679-0_20 |
0.364 |
|
1989 |
Bayley P, Schilstra M, Martin S. A lateral cap model of microtubule dynamic instability. Febs Letters. 259: 181-4. PMID 2599106 DOI: 10.1016/0014-5793(89)81523-6 |
0.333 |
|
1989 |
Bayley PM, Janot JM, Martin SR. Subtilisin enzymes: A note on time-resolved fluorescence and circular dichroism properties Febs Letters. 250: 389-394. DOI: 10.1016/0014-5793(89)80762-8 |
0.308 |
|
1988 |
Wendt B, Hofmann T, Martin SR, Bayley P, Brodin P, Grundström T, Thulin E, Linse S, Forsén S. Effect of amino acid substitutions and deletions on the thermal stability, the pH stability and unfolding by urea of bovine calbindin D9k. European Journal of Biochemistry / Febs. 175: 439-45. PMID 3409879 DOI: 10.1111/J.1432-1033.1988.Tb14214.X |
0.372 |
|
1988 |
Favilla R, Martin SR, Bayley PM. Fluorescence stopped-flow studies on the binding of 1,N6-etheno-NAD to bovine liver glutamate dehydrogenase. Biochimica Et Biophysica Acta. 955: 321-9. PMID 3401491 DOI: 10.1016/0167-4838(88)90211-7 |
0.331 |
|
1988 |
Forsén S, Linse S, Thulin E, Lindegård B, Martin SR, Bayley PM, Brodin P, Grundström T. Kinetics of calcium binding to calbindin mutants. European Journal of Biochemistry / Febs. 177: 47-52. PMID 3181158 DOI: 10.1111/J.1432-1033.1988.Tb14343.X-I2 |
0.385 |
|
1988 |
Gal V, Martin S, Bayley P. Fast disassembly of microtubules induced by Mg2+ or Ca2+. Biochemical and Biophysical Research Communications. 155: 1464-70. PMID 3178822 DOI: 10.1016/S0006-291X(88)81306-8 |
0.347 |
|
1988 |
Bayley P, Martin S, Jones G. The conformation of calmodulin: a substantial environmentally sensitive helical transition in Ca4-calmodulin with potential mechanistic function. Febs Letters. 238: 61-6. PMID 3169255 DOI: 10.1016/0014-5793(88)80225-4 |
0.339 |
|
1987 |
Schilstra MJ, Martin SR, Bayley PM. On the relationship between nucleotide hydrolysis and microtubule assembly: studies with a GTP-regenerating system. Biochemical and Biophysical Research Communications. 147: 588-95. PMID 3632688 DOI: 10.1016/0006-291X(87)90971-5 |
0.324 |
|
1987 |
Martin SR, Bayley PM. Effects of GDP on microtubules at steady state. Biophysical Chemistry. 27: 67-76. PMID 3607239 DOI: 10.1016/0301-4622(87)80047-9 |
0.375 |
|
1987 |
Martin SR, Butler FM, Clark DC, Zhou JM, Bayley PM. Magnesium ion effects on microtubule nucleation in vitro. Biochimica Et Biophysica Acta. 914: 96-100. PMID 3607064 DOI: 10.1016/0167-4838(87)90166-X |
0.337 |
|
1987 |
Martin SR, Schilstra MJ, Bayley PM. Dynamic properties of microtubules at steady state of polymerisation. Biochemical and Biophysical Research Communications. 149: 461-7. PMID 3426585 DOI: 10.1016/0006-291X(87)90390-1 |
0.335 |
|
1986 |
Martin SR, Linse S, Bayley PM, Forsén S. Kinetics of cadmium and terbium dissociation from calmodulin and its tryptic fragments. European Journal of Biochemistry / Febs. 161: 595-601. PMID 3792310 DOI: 10.1111/J.1432-1033.1986.Tb10483.X |
0.317 |
|
1986 |
Bayley PM, Butler FM, Manser EJ. Control of nucleation in microtubule self-assembly. Febs Letters. 205: 230-4. PMID 3743775 DOI: 10.1016/0014-5793(86)80903-6 |
0.313 |
|
1986 |
Bayley PM, Martin SR. Inhibition of microtubule elongation by GDP. Biochemical and Biophysical Research Communications. 137: 351-8. PMID 3718509 DOI: 10.1016/0006-291X(86)91217-9 |
0.362 |
|
1986 |
Favilla R, Mazzini A, Cavatorta F, Bayley PM. The binding of 1,N6-ethenoNAD to bovine liver glutamate dehydrogenase: studies using the time-correlated single photon counting fluorescence technique. Biochimica Et Biophysica Acta. 870: 41-9. PMID 3484973 DOI: 10.1016/0167-4838(86)90006-3 |
0.335 |
|
1985 |
Martin SR, Andersson Teleman A, Bayley PM, Drakenberg T, Forsen S. Kinetics of calcium dissociation from calmodulin and its tryptic fragments. A stopped-flow fluorescence study using Quin 2 reveals a two-domain structure. European Journal of Biochemistry / Febs. 151: 543-50. PMID 4029146 DOI: 10.1111/J.1432-1033.1985.Tb09137.X |
0.387 |
|
1985 |
Bayley PM, Butler FM, Clark DC, Manser EJ, Martin SR. The assembly of microtubule protein in vitro. The kinetic role in microtubule elongation of oligomeric fragments containing microtubule-associated proteins. The Biochemical Journal. 227: 439-55. PMID 4004773 DOI: 10.1042/Bj2270439 |
0.346 |
|
1985 |
Bayley PM, Manser EJ. Assembly of microtubules from nucleotide-depleted tubulin. Nature. 318: 683-5. PMID 3001532 DOI: 10.1038/318683A0 |
0.393 |
|
1985 |
Manser EJ, Bayley PM. Incorporation of GDP-tubulin during elongation of microtubules in vitro. Biochemical and Biophysical Research Communications. 131: 386-94. PMID 2994659 DOI: 10.1016/0006-291X(85)91814-5 |
0.336 |
|
1984 |
Bayley P, Ahlström P, Martin SR, Forsen S. The kinetics of calcium binding to calmodulin: Quin 2 and ANS stopped-flow fluorescence studies. Biochemical and Biophysical Research Communications. 120: 185-91. PMID 6712688 DOI: 10.1016/0006-291X(84)91431-1 |
0.347 |
|
1983 |
Woody RW, Clark DC, Roberts GC, Martin SR, Bayley PM. Molecular flexibility in microtubule proteins: proton nuclear magnetic resonance characterization. Biochemistry. 22: 2186-92. PMID 6860659 DOI: 10.1021/Bi00278A020 |
0.348 |
|
1983 |
Bayley PM, Clark DC, Martin SR. Conformational properties of microtubule protein: their relation to the self-assembly process in vitro. Biopolymers. 22: 87-91. PMID 6673776 DOI: 10.1002/Bip.360220114 |
0.353 |
|
1982 |
Palmer GR, Clark DC, Bayley PM, Sattelle DB. A quasi-elastic laser light scattering study of tubulin and microtubule protein from bovine brain. Journal of Molecular Biology. 160: 641-58. PMID 7175941 DOI: 10.1016/0022-2836(82)90320-5 |
0.301 |
|
1982 |
Delabar JM, Martin SR, Bayley PM. The binding of NADH and NADPH to bovine-liver glutamate dehydrogenase. Spectroscopic characterisation. European Journal of Biochemistry / Febs. 127: 367-74. PMID 7140774 DOI: 10.1111/J.1432-1033.1982.Tb06881.X |
0.324 |
|
1982 |
Martin SR, Clark DC, Bayley PM. Interactions of tubulin and microtubule-associated proteins. Conformation and stability of oligomeric species from glycerol-cycled microtubule protein of bovine brain Biochemical Journal. 203: 643-652. PMID 7115306 DOI: 10.1042/Bj2030643 |
0.372 |
|
1982 |
Woody RW, Roberts GC, Clark DC, Bayley PM. 1H NMR evidence for flexibility in microtubule-associated proteins and microtubule protein oligomers. Febs Letters. 141: 181-4. PMID 7095148 DOI: 10.1016/0014-5793(82)80042-2 |
0.323 |
|
1982 |
Bayley PM, Charlwood PA, Clark DC, Martin SR. Oligomeric species in glycerol-cycled bovine-brain microtubule protein. Analytical ultracentrifugal characterisation. European Journal of Biochemistry / Febs. 121: 579-85. PMID 7056259 DOI: 10.1111/J.1432-1033.1982.Tb05826.X |
0.345 |
|
1982 |
Favilla R, Bayley PM. The reaction of bovine glutamate dehydrogenase with periodate-oxidised ADP. European Journal of Biochemistry / Febs. 125: 209-14. PMID 6286311 DOI: 10.1111/J.1432-1033.1982.Tb06670.X |
0.318 |
|
1981 |
Clark DC, Martin SR, Bayley PM. Conformation and assembly characteristics of tubulin and microtubule protein from bovine brain. Biochemistry. 20: 1924-32. PMID 7225366 DOI: 10.1021/Bi00510A031 |
0.379 |
|
1980 |
Clark DC, Martin SR, Bayley PM. A study of tubulin dimer conformation by near-UV circular dichroism. Biochemical and Biophysical Research Communications. 97: 628-34. PMID 7470116 DOI: 10.1016/0006-291X(80)90310-1 |
0.391 |
|
1980 |
Bayley PM, O'Neill KT. The binding of oxidised coenzyme to bovine-liver glutamate dehydrogenase studied by circular-difference spectroscopy. European Journal of Biochemistry / Febs. 112: 521-31. PMID 7460936 DOI: 10.1111/J.1432-1033.1980.Tb06115.X |
0.346 |
|
1980 |
Eccleston JF, Bayley PM. Circular dichroic spectra of 6-thioguanosine nucleotides and their complexes with myosin subfragment 1. Biochemistry. 19: 5050-6. PMID 7459323 DOI: 10.1021/Bi00563A018 |
0.353 |
|
1977 |
Thornton JM, Bayley PM. Conformational energy calculations for dinucleotide molecules: a study of the nucleotide coenzyme nicotinamide adenine dinucleotide (NAD+). Biopolymers. 16: 1971-86. PMID 198038 DOI: 10.1002/Bip.1977.360160911 |
0.462 |
|
1976 |
Thornton JM, Bayley PM. Conformational energy calculations for dinucleotide molecules. A systematic study of dinucleotide conformation, with application to diadenosine pyrophosphate. Biopolymers. 15: 955-75. PMID 177120 DOI: 10.1002/Bip.1976.360150511 |
0.482 |
|
1975 |
Thornton JM, Bayley PM. Conformational energy calculations for dinucleotide molecules. A study of the component mononucleotide adenosine 3'-monophosphate. The Biochemical Journal. 149: 585-96. PMID 1200996 DOI: 10.1042/Bj1490585 |
0.476 |
|
1975 |
Bayley PM, Harris HE. Conformational properties of pig-heart cytoplasmic aspartate aminotransferase. Circular-dichroism and absorption-spectroscopic study of dicarboxylate binding. European Journal of Biochemistry / Febs. 56: 455-65. PMID 1175635 DOI: 10.1111/J.1432-1033.1975.Tb02252.X |
0.364 |
|
1975 |
Bayley P, Anson M. Stopped-flow circular dichroism: a rapid kinetic study of the binding of a sulphonamide drug to bovine carbonic anhydrase. Biochemical and Biophysical Research Communications. 62: 717-22. PMID 804309 DOI: 10.1016/0006-291X(75)90458-1 |
0.305 |
|
1974 |
Bayley P, Debenham P. The effect of lanthanide ions on the conformation of adenine mononucleotides and dinucleotides. European Journal of Biochemistry / Febs. 43: 561-8. PMID 4364861 DOI: 10.1111/J.1432-1033.1974.Tb03443.X |
0.346 |
|
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