| Year |
Citation |
Score |
| 2020 |
Bradley JM, Pullin J, Moore GR, Svistunenko DA, Hemmings AM, Le Brun NE. Routes of iron entry into, and exit from, the catalytic ferroxidase sites of the prokaryotic ferritin SynFtn. Dalton Transactions (Cambridge, England : 2003). PMID 31930254 DOI: 10.1039/c9dt03570b |
0.364 |
|
| 2019 |
Deacon OM, White RW, Moore GR, Wilson MT, Worrall JAR. Comparison of the structural dynamic and mitochondrial electron-transfer properties of the proapoptotic human cytochrome c variants, G41S, Y48H and A51V. Journal of Inorganic Biochemistry. 203: 110924. PMID 31760234 DOI: 10.1016/J.Jinorgbio.2019.110924 |
0.352 |
|
| 2019 |
Huang Y, Soliakov A, Le Brun AP, Macdonald CJ, Johnson C, Solovyova A, Waller H, Moore GR, Lakey JH. Helix N-Cap residues drive the acid unfolding that is essential in the action of the toxin Colicin A. Biochemistry. PMID 31686499 DOI: 10.1021/Acs.Biochem.9B00705 |
0.343 |
|
| 2018 |
Deacon OM, Svistunenko DA, Moore GR, Wilson MT, Worrall JAR. Naturally occurring disease-related mutations in the 40-57 Ω-loop of human cytochrome c control triggering of the alkaline isomerisation. Biochemistry. PMID 29949346 DOI: 10.1021/Acs.Biochem.8B00520 |
0.382 |
|
| 2017 |
Deacon OM, Karsisiotis AI, Moreno Chicano T, Hough MA, Macdonald CJ, Blumenschein T, Wilson MT, Moore GR, Worrall JAR. Heightened dynamics of the oxidized Y48H variant of human cytochrome c increases its peroxidatic activity. Biochemistry. PMID 29083920 DOI: 10.1021/Acs.Biochem.7B00890 |
0.421 |
|
| 2017 |
Johnson CL, Solovyova AS, Hecht O, Macdonald C, Waller H, Grossmann JG, Moore GR, Lakey JH. The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N. Biophysical Journal. 113: 1673-1684. PMID 29045862 DOI: 10.1016/J.Bpj.2017.08.030 |
0.342 |
|
| 2017 |
Bradley JM, Svistunenko DA, Moore GR, Le Brun NE. Tyr25, Tyr58 and Trp133 of Escherichia coli bacterioferritin transfer electrons between iron in the central cavity and the ferroxidase centre. Metallomics : Integrated Biometal Science. PMID 28914315 DOI: 10.1039/C7Mt00187H |
0.371 |
|
| 2017 |
Bradley JM, Moore GR, Le Brun NE. Diversity of Fe(2+) entry and oxidation in ferritins. Current Opinion in Chemical Biology. 37: 122-128. PMID 28314217 DOI: 10.1016/J.Cbpa.2017.02.027 |
0.327 |
|
| 2017 |
Karsisiotis AI, Deacon OM, Macdonald C, Blumenschein TM, Moore GR, Worrall JA. Near-complete backbone resonance assignments of acid-denatured human cytochrome c in dimethylsulfoxide: a prelude to studying interactions with phospholipids. Biomolecular Nmr Assignments. PMID 28260216 DOI: 10.1007/S12104-017-9740-0 |
0.398 |
|
| 2017 |
Ioannis Karsisiotis A, Deacon OM, Wilson MT, Macdonald C, Blumenschein TM, Moore GR, Worrall JA. The G41S Variant of Human Cytochrome C Enhances Apoptosis via Increased Dynamics Biophysical Journal. 112: 32a-33a. DOI: 10.1016/J.Bpj.2016.11.210 |
0.396 |
|
| 2016 |
Karsisiotis AI, Deacon OM, Wilson MT, Macdonald C, Blumenschein TM, Moore GR, Worrall JA. Increased dynamics in the 40-57 Ω-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation. Scientific Reports. 6: 30447. PMID 27461282 DOI: 10.1038/Srep30447 |
0.395 |
|
| 2016 |
Bradley JM, Le Brun NE, Moore GR. Ferritins: furnishing proteins with iron. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 26825805 DOI: 10.1007/S00775-016-1336-0 |
0.37 |
|
| 2015 |
Bradley JM, Svistunenko DA, Lawson TL, Hemmings AM, Moore GR, Le Brun NE. Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin. Angewandte Chemie (Weinheim An Der Bergstrasse, Germany). 127: 14976-14980. PMID 27478271 DOI: 10.1002/Ange.201507486 |
0.357 |
|
| 2015 |
Pfaffen S, Bradley JM, Abdulqadir R, Firme MR, Moore GR, Le Brun NE, Murphy ME. A Diatom Ferritin Optimized for Iron Oxidation but not Iron Storage. The Journal of Biological Chemistry. PMID 26396187 DOI: 10.1074/Jbc.M115.669713 |
0.348 |
|
| 2015 |
Karsisiotis AI, Deacon OM, Rajagopal BS, Macdonald C, Blumenschein TM, Moore GR, Worrall JA. Backbone resonance assignments of ferric human cytochrome c and the pro-apoptotic G41S mutant in the ferric and ferrous states. Biomolecular Nmr Assignments. PMID 26123826 DOI: 10.1007/S12104-015-9621-3 |
0.371 |
|
| 2015 |
Wong SG, Grigg JC, Le Brun NE, Moore GR, Murphy ME, Mauk AG. The B-type channel is a major route for iron entry into the ferroxidase center and central cavity of bacterioferritin. The Journal of Biological Chemistry. 290: 3732-9. PMID 25512375 DOI: 10.1074/Jbc.M114.623082 |
0.345 |
|
| 2015 |
Çelen E, Kiliç MA, Moore GR. The role of Escherichia coli bacterioferritin in stressed induced conditions Iufs Journal of Biology. 74: 35-42. DOI: 10.18478/Iufsjb.70302 |
0.325 |
|
| 2014 |
Bradley JM, Moore GR, Le Brun NE. Mechanisms of iron mineralization in ferritins: one size does not fit all. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 19: 775-85. PMID 24748222 DOI: 10.1007/S00775-014-1136-3 |
0.357 |
|
| 2013 |
Figueiredo AM, Sardinha J, Moore GR, Cabrita EJ. Protein destabilisation in ionic liquids: the role of preferential interactions in denaturation. Physical Chemistry Chemical Physics : Pccp. 15: 19632-43. PMID 24132185 DOI: 10.1039/C3Cp53395F |
0.627 |
|
| 2013 |
Figueiredo AM, Whittaker SB, Knowling SE, Radford SE, Moore GR. Conformational dynamics is more important than helical propensity for the folding of the all α-helical protein Im7. Protein Science : a Publication of the Protein Society. 22: 1722-38. PMID 24123274 DOI: 10.1002/Pro.2372 |
0.649 |
|
| 2012 |
Hecht O, Macdonald C, Moore GR. Intrinsically disordered proteins: lessons from colicins. Biochemical Society Transactions. 40: 1534-8. PMID 23176512 DOI: 10.1042/Bst20120198 |
0.365 |
|
| 2012 |
Li C, Zhang Y, Vankemmelbeke M, Hecht O, Aleanizy FS, Macdonald C, Moore GR, James R, Penfold CN. Structural evidence that colicin A protein binds to a novel binding site of TolA protein in Escherichia coli periplasm. The Journal of Biological Chemistry. 287: 19048-57. PMID 22493500 DOI: 10.1074/Jbc.M112.342246 |
0.387 |
|
| 2012 |
Wong SG, Abdulqadir R, Le Brun NE, Moore GR, Mauk AG. Fe-haem bound to Escherichia coli bacterioferritin accelerates iron core formation by an electron transfer mechanism. The Biochemical Journal. 444: 553-60. PMID 22458666 DOI: 10.1042/Bj20112200 |
0.357 |
|
| 2012 |
Figueiredo AM, Moore GR, Whittaker SB. Understanding how small helical proteins fold: conformational dynamics of Im proteins relevant to their folding landscapes. Biochemical Society Transactions. 40: 424-8. PMID 22435824 DOI: 10.1042/Bst20110739 |
0.642 |
|
| 2012 |
Huang Y, Le Brun A, Soliakov A, MacDonald C, Moore G, Lakey JH. Helix N-Cap Asp are the pH Trigger for Colicin a Membrane Insertion Biophysical Journal. 102: 656a. DOI: 10.1016/J.Bpj.2011.11.3575 |
0.333 |
|
| 2011 |
Whittaker SB, Clayden NJ, Moore GR. NMR characterisation of the relationship between frustration and the excited state of Im7. Journal of Molecular Biology. 414: 511-29. PMID 22019474 DOI: 10.1016/J.Jmb.2011.09.038 |
0.618 |
|
| 2011 |
Yasmin S, Andrews SC, Moore GR, Le Brun NE. A new role for heme, facilitating release of iron from the bacterioferritin iron biomineral. The Journal of Biological Chemistry. 286: 3473-83. PMID 21106523 DOI: 10.1074/Jbc.M110.175034 |
0.313 |
|
| 2010 |
Meenan NA, Sharma A, Fleishman SJ, Macdonald CJ, Morel B, Boetzel R, Moore GR, Baker D, Kleanthous C. The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. Proceedings of the National Academy of Sciences of the United States of America. 107: 10080-5. PMID 20479265 DOI: 10.1073/Pnas.0910756107 |
0.367 |
|
| 2010 |
Hecht O, Zhang Y, Li C, Penfold CN, James R, Moore GR. Characterisation of the interaction of colicin A with its co-receptor TolA. Febs Letters. 584: 2249-52. PMID 20433837 DOI: 10.1016/J.Febslet.2010.04.061 |
0.393 |
|
| 2010 |
Le Brun NE, Crow A, Murphy ME, Mauk AG, Moore GR. Iron core mineralisation in prokaryotic ferritins. Biochimica Et Biophysica Acta. 1800: 732-44. PMID 20388533 DOI: 10.1016/J.Bbagen.2010.04.002 |
0.323 |
|
| 2009 |
Lawson TL, Crow A, Lewin A, Yasmin S, Moore GR, Le Brun NE. Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy. Biochemistry. 48: 9031-9. PMID 19705876 DOI: 10.1021/Bi900869X |
0.359 |
|
| 2009 |
Bonsor DA, Hecht O, Vankemmelbeke M, Sharma A, Krachler AM, Housden NG, Lilly KJ, James R, Moore GR, Kleanthous C. Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins. The Embo Journal. 28: 2846-57. PMID 19696740 DOI: 10.1038/Emboj.2009.224 |
0.342 |
|
| 2009 |
Knowling SE, Figueiredo AM, Whittaker SB, Moore GR, Radford SE. Amino acid insertion reveals a necessary three-helical intermediate in the folding pathway of the colicin E7 immunity protein Im7. Journal of Molecular Biology. 392: 1074-86. PMID 19651139 DOI: 10.1016/J.Jmb.2009.07.085 |
0.663 |
|
| 2009 |
Crow A, Lewin A, Hecht O, Carlsson Möller M, Moore GR, Hederstedt L, Le Brun NE. Crystal structure and biophysical properties of Bacillus subtilis BdbD. An oxidizing thiol:disulfide oxidoreductase containing a novel metal site. The Journal of Biological Chemistry. 284: 23719-33. PMID 19535335 DOI: 10.1074/Jbc.M109.005785 |
0.346 |
|
| 2009 |
Vankemmelbeke M, Zhang Y, Moore GR, Kleanthous C, Penfold CN, James R. Energy-dependent immunity protein release during tol-dependent nuclease colicin translocation. The Journal of Biological Chemistry. 284: 18932-41. PMID 19458090 DOI: 10.1074/Jbc.M806149200 |
0.301 |
|
| 2009 |
Wong SG, Tom-Yew SA, Lewin A, Le Brun NE, Moore GR, Murphy ME, Mauk AG. Structural and mechanistic studies of a stabilized subunit dimer variant of Escherichia coli bacterioferritin identify residues required for core formation. The Journal of Biological Chemistry. 284: 18873-81. PMID 19439409 DOI: 10.1074/Jbc.M901747200 |
0.408 |
|
| 2009 |
Crow A, Lawson TL, Lewin A, Moore GR, Le Brun NE. Structural basis for iron mineralization by bacterioferritin. Journal of the American Chemical Society. 131: 6808-13. PMID 19391621 DOI: 10.1021/Ja8093444 |
0.38 |
|
| 2009 |
Hecht O, Ridley H, Lakey JH, Moore GR. A common interaction for the entry of colicin N and filamentous phage into Escherichia coli. Journal of Molecular Biology. 388: 880-93. PMID 19306883 DOI: 10.1016/J.Jmb.2009.03.035 |
0.357 |
|
| 2009 |
Figueiredo A, Whittaker S, Spronk C, Knowling S, Radford S, Moore G. Nmr Structure Of A Mutant Colicin E7 Immunity Protein Im7 With An Extended Helix Iii Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2K0D/Pdb |
0.643 |
|
| 2008 |
Hecht O, Ridley H, Boetzel R, Lewin A, Cull N, Chalton DA, Lakey JH, Moore GR. Self-recognition by an intrinsically disordered protein. Febs Letters. 582: 2673-7. PMID 18573254 DOI: 10.1016/J.Febslet.2008.06.022 |
0.313 |
|
| 2008 |
Spiro S, Kilic MA, Lewin A, Dobbin-Namiranian S, Thomson AJ, Moore GR. Interactions of heme and other metal ion complexes with the bacterial Fe-uptake regulatory protein and with bacterioferritin Iron Metabolism: Inorganic Biochemistry and Regulatory Mechanisms. 211-226. DOI: 10.1002/9783527613700.ch14 |
0.434 |
|
| 2007 |
Botër M, Amigues B, Peart J, Breuer C, Kadota Y, Casais C, Moore G, Kleanthous C, Ochsenbein F, Shirasu K, Guerois R. Structural and functional analysis of SGT1 reveals that its interaction with HSP90 is required for the accumulation of Rx, an R protein involved in plant immunity Plant Cell. 19: 3791-3804. PMID 18032631 DOI: 10.1105/Tpc.107.050427 |
0.308 |
|
| 2007 |
Heise CT, Le Duff CS, Boter M, Casais C, Airey JE, Leech AP, Amigues B, Guerois R, Moore GR, Shirasu K, Kleanthous C. Biochemical characterization of RAR1 cysteine- and histidine-rich domains (CHORDs): a novel class of zinc-dependent protein-protein interaction modules. Biochemistry. 46: 1612-23. PMID 17279625 DOI: 10.1021/Bi062174K |
0.392 |
|
| 2007 |
White GF, Ottignon L, Georgiou T, Kleanthous C, Moore GR, Thomson AJ, Oganesyan VS. Analysis of nitroxide spin label motion in a protein-protein complex using multiple frequency EPR spectroscopy. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 185: 191-203. PMID 17218133 DOI: 10.1016/J.Jmr.2006.12.009 |
0.576 |
|
| 2007 |
Whittaker SB, Spence GR, Günter Grossmann J, Radford SE, Moore GR. NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7. Journal of Molecular Biology. 366: 1001-15. PMID 17188712 DOI: 10.1016/J.Jmb.2006.11.012 |
0.408 |
|
| 2006 |
Le Duff CS, Whittaker SB, Radford SE, Moore GR. Characterisation of the conformational properties of urea-unfolded Im7: implications for the early stages of protein folding. Journal of Molecular Biology. 364: 824-35. PMID 17045607 DOI: 10.1016/J.Jmb.2006.09.037 |
0.397 |
|
| 2006 |
Bai E, Rosell FI, Lige B, Mauk MR, Lelj-Garolla B, Moore GR, Mauk AG. Functional characterization of the dimerization domain of the ferric uptake regulator (Fur) of Pseudomonas aeruginosa. The Biochemical Journal. 400: 385-92. PMID 16928194 DOI: 10.1042/Bj20061168 |
0.365 |
|
| 2006 |
Loftus SR, Walker D, Maté MJ, Bonsor DA, James R, Moore GR, Kleanthous C. Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9. Proceedings of the National Academy of Sciences of the United States of America. 103: 12353-8. PMID 16894158 DOI: 10.1073/Pnas.0603433103 |
0.359 |
|
| 2006 |
Mosbahi K, Walker D, James R, Moore GR, Kleanthous C. Global structural rearrangement of the cell penetrating ribonuclease colicin E3 on interaction with phospholipid membranes. Protein Science : a Publication of the Protein Society. 15: 620-7. PMID 16452623 DOI: 10.1110/Ps.051890306 |
0.341 |
|
| 2006 |
Gsponer J, Hopearuoho H, Whittaker SB, Spence GR, Moore GR, Paci E, Radford SE, Vendruscolo M. Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7. Proceedings of the National Academy of Sciences of the United States of America. 103: 99-104. PMID 16371468 DOI: 10.1073/Pnas.0508667102 |
0.346 |
|
| 2005 |
Lewin A, Moore GR, Le Brun NE. Formation of protein-coated iron minerals. Dalton Transactions (Cambridge, England : 2003). 3597-610. PMID 16258608 DOI: 10.1039/B506071K |
0.378 |
|
| 2005 |
Hands SL, Holland LE, Vankemmelbeke M, Fraser L, Macdonald CJ, Moore GR, James R, Penfold CN. Interactions of TolB with the translocation domain of colicin E9 require an extended TolB box. Journal of Bacteriology. 187: 6733-41. PMID 16166536 DOI: 10.1128/Jb.187.19.6733-6741.2005 |
0.345 |
|
| 2005 |
Housden NG, Loftus SR, Moore GR, James R, Kleanthous C. Cell entry mechanism of enzymatic bacterial colicins: porin recruitment and the thermodynamics of receptor binding. Proceedings of the National Academy of Sciences of the United States of America. 102: 13849-54. PMID 16166265 DOI: 10.1073/Pnas.0503567102 |
0.36 |
|
| 2005 |
Tozawa K, Macdonald CJ, Penfold CN, James R, Kleanthous C, Clayden NJ, Moore GR. Clusters in an intrinsically disordered protein create a protein-binding site: the TolB-binding region of colicin E9. Biochemistry. 44: 11496-507. PMID 16114886 DOI: 10.1021/Bi0503596 |
0.65 |
|
| 2005 |
Vankemmelbeke M, Healy B, Moore GR, Kleanthous C, Penfold CN, James R. Rapid detection of colicin E9-induced DNA damage using Escherichia coli cells carrying SOS promoter-lux fusions. Journal of Bacteriology. 187: 4900-7. PMID 15995205 DOI: 10.1128/Jb.187.14.4900-4907.2005 |
0.304 |
|
| 2005 |
Mauk MR, Rosell FI, Lelj-Garolla B, Moore GR, Mauk AG. Metal ion binding to human hemopexin. Biochemistry. 44: 1864-71. PMID 15697212 DOI: 10.1016/S0162-0134(03)80488-9 |
0.33 |
|
| 2004 |
Macdonald CJ, Tozawa K, Collins ES, Penfold CN, James R, Kleanthous C, Clayden NJ, Moore GR. Characterisation of a mobile protein-binding epitope in the translocation domain of colicin E9. Journal of Biomolecular Nmr. 30: 81-96. PMID 15452437 DOI: 10.1023/B:Jnmr.0000042963.71790.19 |
0.657 |
|
| 2004 |
Penfold CN, Healy B, Housden NG, Boetzel R, Vankemmelbeke M, Moore GR, Kleanthous C, James R. Flexibility in the receptor-binding domain of the enzymatic colicin E9 is required for toxicity against Escherichia coli cells. Journal of Bacteriology. 186: 4520-7. PMID 15231784 DOI: 10.1128/Jb.186.14.4520-4527.2004 |
0.359 |
|
| 2004 |
van den Bremer ET, Keeble AH, Jiskoot W, Spelbrink RE, Maier CS, van Hoek A, Visser AJ, James R, Moore GR, Kleanthous C, Heck AJ. Distinct conformational stability and functional activity of four highly homologous endonuclease colicins. Protein Science : a Publication of the Protein Society. 13: 1391-401. PMID 15096639 DOI: 10.1110/Ps.03508204 |
0.387 |
|
| 2004 |
Mosbahi K, Walker D, Lea E, Moore GR, James R, Kleanthous C. Destabilization of the colicin E9 Endonuclease domain by interaction with negatively charged phospholipids: implications for colicin translocation into bacteria. The Journal of Biological Chemistry. 279: 22145-51. PMID 15044477 DOI: 10.1074/Jbc.M400402200 |
0.395 |
|
| 2004 |
Gorski SA, Le Duff CS, Capaldi AP, Kalverda AP, Beddard GS, Moore GR, Radford SE. Equilibrium hydrogen exchange reveals extensive hydrogen bonded secondary structure in the on-pathway intermediate of Im7. Journal of Molecular Biology. 337: 183-93. PMID 15001361 DOI: 10.1016/J.Jmb.2004.01.004 |
0.366 |
|
| 2004 |
Malone SA, Lewin A, Kilic MA, Svistunenko DA, Cooper CE, Wilson MT, Le Brun NE, Spiro S, Moore GR. Protein-template-driven formation of polynuclear iron species. Journal of the American Chemical Society. 126: 496-504. PMID 14719947 DOI: 10.1021/Ja036483Z |
0.377 |
|
| 2004 |
Aitken-Rogers H, Singleton C, Lewin A, Taylor-Gee A, Moore GR, Le Brun NE. Effect of phosphate on bacterioferritin-catalysed iron(II) oxidation. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 161-70. PMID 14673713 DOI: 10.1007/S00775-003-0504-1 |
0.35 |
|
| 2003 |
Baaghil S, Lewin A, Moore GR, Le Brun NE. Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center. Biochemistry. 42: 14047-56. PMID 14636073 DOI: 10.1021/Bi035253U |
0.364 |
|
| 2003 |
Kilic MA, Spiro S, Moore GR. Stability of a 24-meric homopolymer: comparative studies of assembly-defective mutants of Rhodobacter capsulatus bacterioferritin and the native protein. Protein Science : a Publication of the Protein Society. 12: 1663-74. PMID 12876316 DOI: 10.1110/Ps.0301903 |
0.356 |
|
| 2003 |
Walker D, Moore GR, James R, Kleanthous C. Thermodynamic consequences of bipartite immunity protein binding to the ribosomal ribonuclease colicin E3. Biochemistry. 42: 4161-71. PMID 12680770 DOI: 10.1021/Bi0273720 |
0.373 |
|
| 2003 |
Anderluh G, Hong Q, Boetzel R, MacDonald C, Moore GR, Virden R, Lakey JH. Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA. The Journal of Biological Chemistry. 278: 21860-8. PMID 12679333 DOI: 10.1074/Jbc.M300411200 |
0.391 |
|
| 2003 |
Boetzel R, Collins ES, Clayden NJ, Kleanthous C, James R, Moore GR. Structural dynamics of the receptor-binding domain of colicin E9. Faraday Discussions. 122: 145-62; discussion 1. PMID 12555855 DOI: 10.1039/B201127A |
0.647 |
|
| 2002 |
Lewin AC, Doughty PA, Flegg L, Moore GR, Spiro S. The ferric uptake regulator of Pseudomonas aeruginosa has no essential cysteine residues and does not contain a structural zinc ion. Microbiology (Reading, England). 148: 2449-56. PMID 12177338 DOI: 10.1099/00221287-148-8-2449 |
0.385 |
|
| 2002 |
Keeble AH, Hemmings AM, James R, Moore GR, Kleanthous C. Multistep binding of transition metals to the H-N-H endonuclease toxin colicin E9. Biochemistry. 41: 10234-44. PMID 12162738 DOI: 10.1021/Bi020174O |
0.354 |
|
| 2002 |
Walker DC, Georgiou T, Pommer AJ, Walker D, Moore GR, Kleanthous C, James R. Mutagenic scan of the H-N-H motif of colicin E9: implications for the mechanistic enzymology of colicins, homing enzymes and apoptotic endonucleases. Nucleic Acids Research. 30: 3225-34. PMID 12136104 DOI: 10.1093/Nar/Gkf420 |
0.323 |
|
| 2002 |
van den Bremer ET, Jiskoot W, James R, Moore GR, Kleanthous C, Heck AJ, Maier CS. Probing metal ion binding and conformational properties of the colicin E9 endonuclease by electrospray ionization time-of-flight mass spectrometry. Protein Science : a Publication of the Protein Society. 11: 1738-52. PMID 12070327 DOI: 10.1110/Ps.0200502 |
0.33 |
|
| 2002 |
Collins ES, Whittaker SB, Tozawa K, MacDonald C, Boetzel R, Penfold CN, Reilly A, Clayden NJ, Osborne MJ, Hemmings AM, Kleanthous C, James R, Moore GR. Structural dynamics of the membrane translocation domain of colicin E9 and its interaction with TolB. Journal of Molecular Biology. 318: 787-804. PMID 12054823 DOI: 10.1016/S0022-2836(02)00036-0 |
0.64 |
|
| 2002 |
McEwan AG, Lewin A, Davy SL, Boetzel R, Leech A, Walker D, Wood T, Moore GR. PrrC from Rhodobacter sphaeroides, a homologue of eukaryotic Sco proteins, is a copper-binding protein and may have a thiol-disulfide oxidoreductase activity. Febs Letters. 518: 10-6. PMID 11997009 DOI: 10.1016/S0014-5793(02)02532-2 |
0.38 |
|
| 2002 |
Baaghil S, Thomson AJ, Moore GR, Le Brun NE. Studies of copper(II)-binding to bacterioferritin and its effect on iron(II) oxidation Dalton Transactions. 811-818. DOI: 10.1039/B107288A |
0.606 |
|
| 2002 |
Lewin A, Hill JP, Boetzel R, Georgiou T, James R, Kleanthous C, Moore GR. Site-specific labeling of proteins with cyclen-bound transition metal ions Inorganica Chimica Acta. 331: 123-130. DOI: 10.1016/S0020-1693(01)00766-6 |
0.377 |
|
| 2002 |
Schmitt W, Jordan PA, Henderson RK, Moore GR, Anson CE, Powell AK. Synthesis, structures and properties of hydrolytic Al(III) aggregates and Fe(III) analogues formed with iminodiacetate-based chelating ligands Coordination Chemistry Reviews. 228: 115-126. DOI: 10.1016/S0010-8545(02)00110-8 |
0.314 |
|
| 2001 |
Pommer AJ, Cal S, Keeble AH, Walker D, Evans SJ, Kühlmann UC, Cooper A, Connolly BA, Hemmings AM, Moore GR, James R, Kleanthous C. Mechanism and cleavage specificity of the H-N-H endonuclease colicin E9. Journal of Molecular Biology. 314: 735-49. PMID 11733993 DOI: 10.1006/Jmbi.2001.5189 |
0.323 |
|
| 2001 |
Pidcock E, Moore GR. Structural characteristics of protein binding sites for calcium and lanthanide ions. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 6: 479-89. PMID 11472012 DOI: 10.1007/S007750100214 |
0.351 |
|
| 2000 |
Penfold CN, Garinot-Schneider C, Hemmings AM, Moore GR, Kleanthous C, James R. A 76-residue polypeptide of colicin E9 confers receptor specificity and inhibits the growth of vitamin B12-dependent Escherichia coli 113/3 cells. Molecular Microbiology. 38: 639-49. PMID 11069686 DOI: 10.1046/J.1365-2958.2000.02160.X |
0.346 |
|
| 2000 |
Boetzel R, Czisch M, Kaptein R, Hemmings AM, James R, Kleanthous C, Moore GR. NMR investigation of the interaction of the inhibitor protein Im9 with its partner DNase. Protein Science : a Publication of the Protein Society. 9: 1709-18. PMID 11045617 DOI: 10.1110/Ps.9.9.1709 |
0.443 |
|
| 2000 |
Hannan JP, Busch JL, Breton J, James R, Thomson AJ, Moore GR, Davy SL. Characterisation of oxidised 7Fe dicluster ferredoxins with NMR spectroscopy. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 5: 432-47. PMID 10968614 DOI: 10.1007/Pl00021445 |
0.6 |
|
| 2000 |
Kühlmann UC, Pommer AJ, Moore GR, James R, Kleanthous C. Specificity in protein-protein interactions: the structural basis for dual recognition in endonuclease colicin-immunity protein complexes. Journal of Molecular Biology. 301: 1163-78. PMID 10966813 DOI: 10.1006/Jmbi.2000.3945 |
0.391 |
|
| 2000 |
Hannan JP, Whittaker SB, Hemmings AM, James R, Kleanthous C, Moore GR. NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9. Journal of Inorganic Biochemistry. 79: 365-70. PMID 10830890 DOI: 10.1016/S0162-0134(99)00235-4 |
0.4 |
|
| 2000 |
Whittaker SB, Czisch M, Wechselberger R, Kaptein R, Hemmings AM, James R, Kleanthous C, Moore GR. Slow conformational dynamics of an endonuclease persist in its complex with its natural protein inhibitor. Protein Science : a Publication of the Protein Society. 9: 713-20. PMID 10794413 DOI: 10.1110/Ps.9.4.713 |
0.423 |
|
| 2000 |
Yang X, Le Brun NE, Thomson AJ, Moore GR, Chasteen ND. The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin. Biochemistry. 39: 4915-23. PMID 10769150 DOI: 10.1021/Bi992631F |
0.578 |
|
| 2000 |
Hannan JP, Busch JL, James R, Thomson AJ, Moore GR, Davy SL. Slow formation of [3Fe-4S](1+) clusters in mutant forms of Desulfovibrio africanus ferredoxin III. Febs Letters. 468: 161-5. PMID 10692579 DOI: 10.1016/S0014-5793(00)01210-2 |
0.598 |
|
| 2000 |
Busch JL, Breton JL, Davy SL, James R, Moore GR, Armstrong FA, Thomson AJ. Ferredoxin III of Desulfovibrio africanus: sequencing of the native gene and characterization of a histidine-tagged form. The Biochemical Journal. 346: 375-84. PMID 10677356 DOI: 10.1042/Bj3460375 |
0.62 |
|
| 1999 |
Whittaker SB, Boetzel R, MacDonald C, Lian LY, James R, Kleanthous C, Moore GR. Assignment of 1H, 13C and 15N signals of the DNase domain of colicin E9. Journal of Biomolecular Nmr. 14: 201-2. PMID 10610142 DOI: 10.1023/A:1008394407597 |
0.315 |
|
| 1999 |
Pommer AJ, Kühlmann UC, Cooper A, Hemmings AM, Moore GR, James R, Kleanthous C. Homing in on the role of transition metals in the HNH motif of colicin endonucleases. The Journal of Biological Chemistry. 274: 27153-60. PMID 10480931 DOI: 10.1074/Jbc.274.38.27153 |
0.312 |
|
| 1999 |
Hannan JP, Whittaker SB, Davy SL, Kühlmann UC, Pommer AJ, Hemmings AM, James R, Kleanthous C, Moore GR. NMR study of Ni2+ binding to the H-N-H endonuclease domain of colicin E9. Protein Science : a Publication of the Protein Society. 8: 1711-3. PMID 10452617 DOI: 10.1110/Ps.8.8.1711 |
0.362 |
|
| 1999 |
Kühlmann UC, Kleanthous C, James R, Moore GR, Hemmings AM. Preliminary X-ray crystallographic analysis of the complex between the DNAase domain of colicin E9 and its cognate immunity protein. Acta Crystallographica. Section D, Biological Crystallography. 55: 256-9. PMID 10089452 DOI: 10.1107/S0108444998002590 |
0.301 |
|
| 1999 |
Kleanthous C, Kühlmann UC, Pommer AJ, Ferguson N, Radford SE, Moore GR, James R, Hemmings AM. Structural and mechanistic basis of immunity toward endonuclease colicins. Nature Structural Biology. 6: 243-52. PMID 10074943 DOI: 10.1038/6683 |
0.335 |
|
| 1998 |
Boetzel R, Czisch M, MacDonald CJ, Kaptein R, Hemmings AM, James R, Kleanthous C, Moore GR. Assignment of 1H, 13C and 15N signals of the inhibitor protein Im9 bound to the DNase domain of colicin E9. Journal of Biomolecular Nmr. 12: 567-8. PMID 9917143 DOI: 10.1023/A:1008397523780 |
0.358 |
|
| 1998 |
Whittaker SB, Boetzel R, MacDonald C, Lian LY, Pommer AJ, Reilly A, James R, Kleanthous C, Moore GR. NMR detection of slow conformational dynamics in an endonuclease toxin. Journal of Biomolecular Nmr. 12: 145-59. PMID 9729794 DOI: 10.1023/A:1008272928173 |
0.427 |
|
| 1998 |
Li W, Hamill SJ, Hemmings AM, Moore GR, James R, Kleanthous C. Dual recognition and the role of specificity-determining residues in colicin E9 DNase-immunity protein interactions. Biochemistry. 37: 11771-9. PMID 9718299 DOI: 10.1021/Bi9808621 |
0.372 |
|
| 1998 |
Dennis CA, Videler H, Pauptit RA, Wallis R, James R, Moore GR, Kleanthous C. A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificity. The Biochemical Journal. 333: 183-91. PMID 9639578 DOI: 10.1042/Bj3330183 |
0.393 |
|
| 1998 |
Kleanthous C, Hemmings AM, Moore GR, James R. Immunity proteins and their specificity for endonuclease colicins: telling right from wrong in protein-protein recognition. Molecular Microbiology. 28: 227-33. PMID 9622349 DOI: 10.1046/J.1365-2958.1998.00811.X |
0.359 |
|
| 1998 |
Moore GR, Cox MC, Crowe D, Osborne MJ, Rosell FI, Bujons J, Barker PD, Mauk MR, Mauk AG. N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation. The Biochemical Journal. 332: 439-49. PMID 9601073 |
0.311 |
|
| 1998 |
Davy SL, Osborne MJ, Moore GR. Determination of the structure of oxidised Desulfovibrio africanus ferredoxin I by 1H NMR spectroscopy and comparison of its solution structure with its crystal structure. Journal of Molecular Biology. 277: 683-706. PMID 9533888 DOI: 10.1006/Jmbi.1998.1631 |
0.352 |
|
| 1998 |
Wallis R, Leung KY, Osborne MJ, James R, Moore GR, Kleanthous C. Specificity in protein-protein recognition: conserved Im9 residues are the major determinants of stability in the colicin E9 DNase-Im9 complex. Biochemistry. 37: 476-85. PMID 9425068 DOI: 10.1021/Bi971884A |
0.399 |
|
| 1998 |
Costa C, Moore GR. The effect of surface charge on the reduction potential and heme propionate ionization of a monoheme cytochrome: Spectroscopic and potentiometric studies of trifluoroacetylated cytochrome c551 from Pseudomonas aeruginosa Inorganica Chimica Acta. 275: 256-262. DOI: 10.1016/S0020-1693(97)06070-2 |
0.311 |
|
| 1997 |
Garinot-Schneider C, Penfold CN, Moore GR, Kleanthous C, James R. Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9. Microbiology (Reading, England). 143: 2931-8. PMID 9308177 DOI: 10.1099/00221287-143-9-2931 |
0.346 |
|
| 1997 |
Osborne MJ, Crowe D, Davy SL, Macdonald C, Moore GR. NMR of paramagnetic proteins. Methods in Molecular Biology (Clifton, N.J.). 60: 233-69. PMID 9276250 DOI: 10.1385/0-89603-309-0:233 |
0.367 |
|
| 1997 |
Li W, Dennis CA, Moore GR, James R, Kleanthous C. Protein-protein interaction specificity of Im9 for the endonuclease toxin colicin E9 defined by homologue-scanning mutagenesis. The Journal of Biological Chemistry. 272: 22253-8. PMID 9268373 DOI: 10.1074/Jbc.272.35.22253 |
0.397 |
|
| 1997 |
Osborne MJ, Wallis R, Leung KY, Williams G, Lian LY, James R, Kleanthous C, Moore GR. Identification of critical residues in the colicin E9 DNase binding region of the Im9 protein. The Biochemical Journal. 323: 823-31. PMID 9169618 DOI: 10.1042/Bj3230823 |
0.431 |
|
| 1997 |
Thomson AJ, Le Brun NE, Keech A, Andrews SC, Moore GR. Pumping iron: does bacterioferritin contain a redox-driven iron pump? Biochemical Society Transactions. 25: 96-101. PMID 9056851 DOI: 10.1042/Bst0250096 |
0.563 |
|
| 1997 |
Keech AM, Le Brun NE, Wilson MT, Andrews SC, Moore GR, Thomson AJ. Spectroscopic studies of cobalt(II) binding to Escherichia coli bacterioferritin. The Journal of Biological Chemistry. 272: 422-9. PMID 8995278 DOI: 10.1074/Jbc.272.1.422 |
0.596 |
|
| 1997 |
McKnight J, White N, Moore GR. Effect of copper(II) on the aerobic oxidative uptake of iron(II) by horse spleen apoferritin Journal of the Chemical Society-Dalton Transactions. 4043-4046. DOI: 10.1039/A704456I |
0.337 |
|
| 1996 |
Le Brun NE, Keech AM, Mauk MR, Mauk AG, Andrews SC, Thomson AJ, Moore GR. Charge compensated binding of divalent metals to bacterioferritin: H+ release associated with cobalt(II) and zinc(II) binding at dinuclear metal sites. Febs Letters. 397: 159-63. PMID 8955338 DOI: 10.1016/S0014-5793(96)01172-6 |
0.604 |
|
| 1996 |
Osborne MJ, Breeze AL, Lian LY, Reilly A, James R, Kleanthous C, Moore GR. Three-dimensional solution structure and 13C nuclear magnetic resonance assignments of the colicin E9 immunity protein Im9. Biochemistry. 35: 9505-12. PMID 8755730 DOI: 10.1021/Bi960401K |
0.414 |
|
| 1996 |
Garinot-Schneider C, Pommer AJ, Moore GR, Kleanthous C, James R. Identification of putative active-site residues in the DNase domain of colicin E9 by random mutagenesis. Journal of Molecular Biology. 260: 731-42. PMID 8709151 DOI: 10.1006/Jmbi.1996.0433 |
0.353 |
|
| 1996 |
Penfold CN, Ringeling PL, Davy SL, Moore GR, McEwan AG, Spiro S. Isolation, characterisation and expression of the bacterioferritin gene of Rhodobacter capsulatus. Fems Microbiology Letters. 139: 143-8. PMID 8674981 DOI: 10.1111/J.1574-6968.1996.Tb08194.X |
0.323 |
|
| 1996 |
Jordan PA, Clayden NJ, Heath SL, Moore GR, Powell AK, Tapparo A. Defining speciation profiles of Al3+ complexed with small organic ligands: The Al3+-heidi system Coordination Chemistry Reviews. 149: 281-309. DOI: 10.1016/S0010-8545(96)90032-6 |
0.587 |
|
| 1995 |
Mauk AG, Mauk MR, Moore GR, Northrup SH. Experimental and theoretical analysis of the interaction between cytochrome c and cytochrome b5. Journal of Bioenergetics and Biomembranes. 27: 311-30. PMID 8847345 DOI: 10.1007/Bf02110101 |
0.35 |
|
| 1995 |
Cox MC, Le Brun N, Thomson AJ, Smith A, Morgan WT, Moore GR. MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domain. Biochimica Et Biophysica Acta. 1253: 215-23. PMID 8519805 DOI: 10.1016/0167-4838(95)00163-4 |
0.645 |
|
| 1995 |
Davy SL, Osborne MJ, Breton J, Moore GR, Thomson AJ, Bertini I, Luchinat C. Determination of the [Fe4S4]Cys4 cluster geometry of Desulfovibrio africanus ferredoxin I by 1H NMR spectroscopy. Febs Letters. 363: 199-204. PMID 7729544 DOI: 10.1016/0014-5793(95)00317-3 |
0.601 |
|
| 1995 |
Wallis R, Leung KY, Pommer AJ, Videler H, Moore GR, James R, Kleanthous C. Protein-protein interactions in colicin E9 DNase-immunity protein complexes. 2. Cognate and noncognate interactions that span the millimolar to femtomolar affinity range. Biochemistry. 34: 13751-9. PMID 7577967 DOI: 10.1021/Bi00042A005 |
0.36 |
|
| 1995 |
Wallis R, Moore GR, James R, Kleanthous C. Protein-protein interactions in colicin E9 DNase-immunity protein complexes. 1. Diffusion-controlled association and femtomolar binding for the cognate complex. Biochemistry. 34: 13743-50. PMID 7577966 DOI: 10.1021/Bi00042A004 |
0.345 |
|
| 1995 |
Andrews SC, Le Brun NE, Barynin V, Thomson AJ, Moore GR, Guest JR, Harrison PM. Site-directed replacement of the coaxial heme ligands of bacterioferritin generates heme-free variants. The Journal of Biological Chemistry. 270: 23268-74. PMID 7559480 DOI: 10.1074/jbc.270.40.23268 |
0.597 |
|
| 1995 |
Le Brun NE, Moore GR, Thomson AJ. Magnetic circular dichroism spectroscopy of the iron cores of ferritin and bacterioferritin Molecular Physics. 85: 1061-1068. DOI: 10.1080/00268979500101661 |
0.607 |
|
| 1995 |
Le Brun NE, Andrews SC, Guest JR, Harrison PM, Moore GR, Thomson AJ. Identification of the ferroxidase centre of Escherichia coli bacterioferritin Biochemical Journal. 312: 385-392. DOI: 10.1042/Bj3120385 |
0.586 |
|
| 1995 |
Heath SL, Jordan PA, Johnson ID, Moore GR, Powell AK, Helliwell M. Comparative X-ray and 27Al NMR spectroscopic studies of the speciation of aluminum in aqueous systems: Al(III) complexes of N(CH2CO2H)2(CH2CH2OH) Journal of Inorganic Biochemistry. 59: 785-794. DOI: 10.1016/0162-0134(94)00064-H |
0.313 |
|
| 1995 |
Barcel� F, Otero Are�n C, Moore G. Isolation and preliminary characterization of ferritin from clover seeds Biometals. 8. DOI: 10.1007/Bf00156157 |
0.334 |
|
| 1994 |
Wallis R, Reilly A, Barnes K, Abell C, Campbell DG, Moore GR, James R, Kleanthous C. Tandem overproduction and characterisation of the nuclease domain of colicin E9 and its cognate inhibitor protein Im9. European Journal of Biochemistry / Febs. 220: 447-54. PMID 8125102 DOI: 10.1111/J.1432-1033.1994.Tb18642.X |
0.376 |
|
| 1994 |
Ringeling PL, Davy SL, Monkara FA, Hunt C, Dickson DP, McEwan AG, Moore GR. Iron metabolism in Rhodobacter capsulatus. Characterisation of bacterioferritin and formation of non-haem iron particles in intact cells. European Journal of Biochemistry / Febs. 223: 847-55. PMID 8055962 DOI: 10.1111/J.1432-1033.1994.Tb19061.X |
0.35 |
|
| 1994 |
Moore GR, Kadir FH, al-Massad FK, Le Brun NE, Thomson AJ, Greenwood C, Keen JN, Findlay JB. Structural heterogeneity of Pseudomonas aeruginosa bacterioferritin. The Biochemical Journal. 304: 493-7. PMID 7998985 DOI: 10.1042/Bj3040493 |
0.543 |
|
| 1994 |
Davy SL, Breton J, Osborne MJ, Thomson AJ, Thurgood AP, Lian LY, Pétillot Y, Hatchikian C, Moore GR. MCD and 1H-NMR spectroscopic studies of Desulfovibrio africanus ferredoxin I: revised amino-acid sequence and identification of secondary structure. Biochimica Et Biophysica Acta. 1209: 33-9. PMID 7947979 DOI: 10.1016/0167-4838(94)90133-3 |
0.626 |
|
| 1994 |
Osborne MJ, Lian LY, Wallis R, Reilly A, James R, Kleanthous C, Moore GR. Sequential assignments and identification of secondary structure elements of the colicin E9 immunity protein in solution by homonuclear and heteronuclear NMR. Biochemistry. 33: 12347-55. PMID 7918457 DOI: 10.1021/Bi00207A001 |
0.378 |
|
| 1993 |
Cheesman MR, le Brun NE, Kadir FH, Thomson AJ, Moore GR, Andrews SC, Guest JR, Harrison PM, Smith JM, Yewdall SJ. Haem and non-haem iron sites in Escherichia coli bacterioferritin: spectroscopic and model building studies. The Biochemical Journal. 292: 47-56. PMID 8389131 DOI: 10.1042/bj2920047 |
0.634 |
|
| 1993 |
Le Brun NE, Cheesman MR, Thomson AJ, Moore GR, Andrews SC, Guest JR, Harrison PM. An EPR investigation of non-haem iron sites in Escherichia coli bacterioferritin and their interaction with phosphate. A study using nitric oxide as a spin probe. Febs Letters. 323: 261-6. PMID 8388809 DOI: 10.1016/0014-5793(93)81353-2 |
0.63 |
|
| 1993 |
Davies AM, Guillemette JG, Smith M, Greenwood C, Thurgood AG, Mauk AG, Moore GR. Redesign of the interior hydrophilic region of mitochondrial cytochrome c by site-directed mutagenesis. Biochemistry. 32: 5431-5. PMID 8388720 DOI: 10.1021/Bi00071A019 |
0.409 |
|
| 1993 |
Le Brun NE, Wilson MT, Andrews SC, Guest JR, Harrison PM, Thomson AJ, Moore GR. Kinetic and structural characterization of an intermediate in the biomineralization of bacterioferritin. Febs Letters. 333: 197-202. PMID 8224163 DOI: 10.1016/0014-5793(93)80404-I |
0.617 |
|
| 1992 |
Wallis R, Reilly A, Rowe A, Moore GR, James R, Kleanthous C. In vivo and in vitro characterization of overproduced colicin E9 immunity protein. European Journal of Biochemistry / Febs. 207: 687-95. PMID 1633820 DOI: 10.1111/J.1432-1033.1992.Tb17096.X |
0.359 |
|
| 1992 |
Brunt CE, Cox MC, Thurgood AG, Moore GR, Reid GA, Chapman SK. Isolation and characterization of the cytochrome domain of flavocytochrome b2 expressed independently in Escherichia coli. The Biochemical Journal. 283: 87-90. PMID 1567382 DOI: 10.1042/Bj2830087 |
0.316 |
|
| 1992 |
Wallis R, Moore GR, Kleanthous C, James R. Molecular analysis of the protein-protein interaction between the E9 immunity protein and colicin E9. European Journal of Biochemistry / Febs. 210: 923-30. PMID 1483475 DOI: 10.1111/J.1432-1033.1992.Tb17496.X |
0.367 |
|
| 1992 |
el-Thaher TS, Bailey GS, Wilson MT, Osborne M, Moore GR. A 1H-NMR study of the interactions between rat tissue kallikrein and two peptide inhibitors. Biochimica Et Biophysica Acta. 1160: 235-8. PMID 1445951 DOI: 10.1016/0167-4838(92)90013-4 |
0.301 |
|
| 1992 |
Moore GR, Kadir FH, al-Massad F. Haem binding to ferritin and possible mechanisms of physiological iron uptake and release by ferritin. Journal of Inorganic Biochemistry. 47: 175-81. PMID 1431879 DOI: 10.1016/0162-0134(92)84063-S |
0.326 |
|
| 1992 |
Moore GR, Cheesman MR, Kadir FH, Thomson AJ, Yewdall SJ, Harrison PM. Spectroscopic identification of the haem axial ligands of haemoferritin and location of possible haem-binding sites in ferritin by molecular modelling. The Biochemical Journal. 287: 457-60. PMID 1332674 DOI: 10.1042/Bj2870457 |
0.583 |
|
| 1992 |
Cheesman MR, Kadir FH, al-Basseet J, al-Massad F, Farrar J, Greenwood C, Thomson AJ, Moore GR. E.p.r. and magnetic circular dichroism spectroscopic characterization of bacterioferritin from Pseudomonas aeruginosa and Azotobacter vinelandii. The Biochemical Journal. 286: 361-7. PMID 1326939 DOI: 10.1042/Bj2860361 |
0.588 |
|
| 1992 |
Cox MC, Rogers MS, Cheesman M, Jones GD, Thomson AJ, Wilson MT, Moore GR. Spectroscopic identification of the haem ligands of cellobiose oxidase. Febs Letters. 307: 233-6. PMID 1322830 DOI: 10.1016/0014-5793(92)80774-B |
0.584 |
|
| 1992 |
Monkara F, Bingham SJ, Kadir FH, McEwan AG, Thomson AJ, Thurgood AG, Moore GR. Spectroscopic studies of Rhodobacter capsulatus cytochrome c' in the isolated state and in intact cells. Biochimica Et Biophysica Acta. 1100: 184-8. PMID 1319208 DOI: 10.1016/0005-2728(92)90080-L |
0.637 |
|
| 1991 |
Kadir FH, Read NM, Dickson DP, Greenwood C, Thompson A, Moore GR. Mössbauer spectroscopic studies of iron in Pseudomonas aeruginosa. Journal of Inorganic Biochemistry. 43: 753-8. PMID 1779230 DOI: 10.1016/0162-0134(91)80046-K |
0.311 |
|
| 1991 |
Thurgood AG, Davies AM, Greenwood C, Mauk AG, Smith M, Guillemette JG, Moore GR. NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted. European Journal of Biochemistry / Febs. 202: 339-47. PMID 1662130 DOI: 10.1111/J.1432-1033.1991.Tb16381.X |
0.411 |
|
| 1991 |
Thurgood AG, Pielak GJ, Cutler RL, Davies AM, Greenwood C, Mauk AG, Smith M, Williamson DJ, Moore GR. Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c. Febs Letters. 284: 173-7. PMID 1647980 DOI: 10.1016/0014-5793(91)80678-V |
0.556 |
|
| 1991 |
Rogers M, Wilson M, Cheesman M, Thomson A, Cox M, Moore G. Spectroscopic investigations reveal his/met ligation for the b-haem of the flavo-haem enzyme cellobiose oxidase Journal of Inorganic Biochemistry. 43: 347. DOI: 10.1016/0162-0134(91)84334-6 |
0.555 |
|
| 1991 |
Kadir F, Le Brun N, Cheesman M, Thomson A, Moore G. Spectroscopic studies of haem binding to horse spleen ferritin Journal of Inorganic Biochemistry. 43: 128. DOI: 10.1016/0162-0134(91)84122-P |
0.554 |
|
| 1991 |
Cox M, Osborne M, Thurgood A, Moore G. Structural characterisation of interprotein complexes involving cytochrome C Journal of Inorganic Biochemistry. 43: 106. DOI: 10.1016/0162-0134(91)84102-F |
0.336 |
|
| 1991 |
Cook MJ, Cracknell SJ, Moore GR, Osborne MJ, Williamson DJ. Solution phase1H and13C-NMR studies of some 1,4,8,11,15,18,22,25-octa-alkylphthalocyanines Magnetic Resonance in Chemistry. 29: 1053-1060. DOI: 10.1002/Mrc.1260291014 |
0.352 |
|
| 1991 |
Rigby SEJ, Burch AM, Moore GR. 1H NMR determination of the ionization constant of a carboxylic acid group of a haem protein in mixed aqueous-organic solvents using the super WEFT sequence Magnetic Resonance in Chemistry. 29: 1036-1039. DOI: 10.1002/Mrc.1260291011 |
0.356 |
|
| 1990 |
Kadir FH, Moore GR. Haem binding to horse spleen ferritin. Febs Letters. 276: 81-4. PMID 2265717 DOI: 10.1016/0014-5793(90)80512-H |
0.371 |
|
| 1990 |
Cheesman MR, Thomson AJ, Greenwood C, Moore GR, Kadir F. Bis-methionine axial ligation of haem in bacterioferritin from Pseudomonas aeruginosa. Nature. 346: 771-3. PMID 2167456 DOI: 10.1038/346771A0 |
0.653 |
|
| 1990 |
Kadir FH, Moore GR. Bacterial ferritin contains 24 haem groups. Febs Letters. 271: 141-3. PMID 2121527 DOI: 10.1016/0014-5793(90)80391-U |
0.332 |
|
| 1989 |
Rigby SE, Alleyne TA, Wilson MT, Moore GR. A 1H NMR study of bovine cytochrome oxidase. Paramagnetically shifted resonances of haem a. Febs Letters. 257: 155-8. PMID 2553487 DOI: 10.1016/0014-5793(89)81809-5 |
0.381 |
|
| 1989 |
Cutler RL, Davies AM, Creighton S, Warshel A, Moore GR, Smith M, Mauk AG. Role of arginine-38 in regulation of the cytochrome c oxidation-reduction equilibrium. Biochemistry. 28: 3188-97. PMID 2545252 DOI: 10.1021/Bi00434A012 |
0.397 |
|
| 1988 |
Rigby SE, Moore GR, Gray JC, Gadsby PM, George SJ, Thomson AJ. N.m.r., e.p.r. and magnetic-c.d. studies of cytochrome f. Identity of the haem axial ligands. The Biochemical Journal. 256: 571-7. PMID 3223931 DOI: 10.1042/Bj2560571 |
0.562 |
|
| 1988 |
Pielak GJ, Boyd J, Moore GR, Williams RJ. Proton-NMR studies show that the Thr-102 mutant of yeast iso-1-cytochrome c is a typical member of the eukaryotic cytochrome c family. European Journal of Biochemistry / Febs. 177: 167-77. PMID 2846294 DOI: 10.1111/J.1432-1033.1988.Tb14359.X-I2 |
0.67 |
|
| 1988 |
Arean CO, Moore GR, Williams G, Williams RJ. Ion binding to cytochrome c. European Journal of Biochemistry / Febs. 173: 607-15. PMID 2836194 DOI: 10.1111/J.1432-1033.1988.Tb14042.X |
0.508 |
|
| 1988 |
Rogers NK, Moore GR. On the energetics of conformational changes and pH dependent redox behaviour of electron transfer proteins. Febs Letters. 228: 69-73. PMID 2830136 DOI: 10.1016/0014-5793(88)80587-8 |
0.332 |
|
| 1988 |
Burch AM, Rigby SEJ, Funk W, Macgillivray RTA, Mauk AG, Mauk M, Moore GR. A 13C nuclear-magnetic-resonance investigation of the interaction between cytochrome c and cytochrome b5 Biochemical Society Transactions. 16: 844-845. DOI: 10.1042/Bst0160844A |
0.34 |
|
| 1988 |
DAVIES AM, CUTLER RL, SMITH M, MAUK AG, THURGOOD AGP, MOORE GR. Structure of yeast iso-1-cytochrome c in which arginine-38 is replaced by alanine-38 Biochemical Society Transactions. 16: 844-844. DOI: 10.1042/Bst0160844 |
0.352 |
|
| 1987 |
Hartshorn RT, Mauk AG, Mauk MR, Moore GR. NMR study of the interaction between cytochrome b5 and cytochrome c. Observation of a ternary complex formed by the two proteins and [Cr(en)3]3+. Febs Letters. 213: 391-5. PMID 3030818 DOI: 10.1016/0014-5793(87)81528-4 |
0.363 |
|
| 1987 |
Pielak GJ, Concar DW, Moore GR, Williams RJ. The structure of cytochrome c and its relation to recent studies of long-range electron transfer. Protein Engineering. 1: 83-8. PMID 2853357 DOI: 10.1093/Protein/1.2.83 |
0.584 |
|
| 1986 |
Moore GR, Pettigrew GW, Rogers NK. Factors influencing redox potentials of electron transfer proteins. Proceedings of the National Academy of Sciences of the United States of America. 83: 4998-9. PMID 3460080 DOI: 10.1073/Pnas.83.14.4998 |
0.339 |
|
| 1986 |
Moore GR, Mann S, Bannister JV. Isolation and properties of the complex nonheme-iron-containing cytochrome b557 (bacterioferritin) from Pseudomonas aeruginosa. Journal of Inorganic Biochemistry. 28: 329-36. PMID 3100721 DOI: 10.1016/0162-0134(86)80097-6 |
0.499 |
|
| 1986 |
St Pierre TG, Bell SH, Dickson DP, Mann S, Webb J, Moore GR, Williams RJ. Mössbauer spectroscopic studies of the cores of human, limpet and bacterial ferritins. Biochimica Et Biophysica Acta. 870: 127-34. PMID 3081032 DOI: 10.1016/0167-4838(86)90015-4 |
0.522 |
|
| 1986 |
Concar DW, Hill HA, Moore GR, Whitford D, Williams RJ. The modulation of cytochrome c electron self-exchange by site-specific chemical modification and anion binding. Febs Letters. 206: 15-9. PMID 3019766 DOI: 10.1016/0014-5793(86)81331-X |
0.623 |
|
| 1986 |
Moore GR. 1H NMR studies of bacterial class I cytochromes c Journal of Inorganic Biochemistry. 28: 355-362. DOI: 10.1016/0162-0134(86)80100-3 |
0.399 |
|
| 1985 |
Williams G, Clayden NJ, Moore GR, Williams RJ. Comparison of the solution and crystal structures of mitochondrial cytochrome c. Analysis of paramagnetic shifts in the nuclear magnetic resonance spectrum of ferricytochrome c. Journal of Molecular Biology. 183: 447-60. PMID 2991533 DOI: 10.1016/0022-2836(85)90013-0 |
0.674 |
|
| 1985 |
Moore GR, Robinson MN, Williams G, Williams RJ. Solution structure of mitochondrial cytochrome c. II. 1H nuclear magnetic resonance of ferrocytochrome c. Journal of Molecular Biology. 183: 429-46. PMID 2991532 DOI: 10.1016/0022-2836(85)90012-9 |
0.442 |
|
| 1985 |
Williams G, Moore GR, Porteous R, Robinson MN, Soffe N, Williams RJ. Solution structure of mitochondrial cytochrome c. I. 1H nuclear magnetic resonance of ferricytochrome c. Journal of Molecular Biology. 183: 409-28. PMID 2991531 DOI: 10.1016/0022-2836(85)90011-7 |
0.529 |
|
| 1985 |
Rogers NK, Moore GR, Sternberg MJ. Electrostatic interactions in globular proteins: calculation of the pH dependence of the redox potential of cytochrome c551. Journal of Molecular Biology. 182: 613-6. PMID 2989537 DOI: 10.1016/0022-2836(85)90248-7 |
0.346 |
|
| 1985 |
Moore GR, Williams RJ, Peterson J, Thomson AJ, Mathews FS. A spectroscopic investigation of the structure and redox properties of Escherichia coli cytochrome b-562. Biochimica Et Biophysica Acta. 829: 83-96. PMID 2986699 DOI: 10.1016/0167-4838(85)90071-8 |
0.645 |
|
| 1985 |
Williams G, Moore GR, Williams RJP. Biological Electron Transfer: The Structure, Dynamics and Reactivity of Cytochromec Comments On Inorganic Chemistry. 4: 55-98. DOI: 10.1080/02603598508072253 |
0.366 |
|
| 1985 |
Moore GR. 1H-NMR studies of the haem and coordinated methionine of Class I and Class II cytochromes c Biochimica Et Biophysica Acta (Bba) - Protein Structure and Molecular Enzymology. 829: 425-429. DOI: 10.1016/0167-4838(85)90253-5 |
0.362 |
|
| 1984 |
Moore GR, Williams RJ. Protein antigenicity and protein mobility. Nature. 312: 706. PMID 6514006 |
0.365 |
|
| 1984 |
Leitch FA, Moore GR, Pettigrew GW. Structural basis for the variation of pH-dependent redox potentials of Pseudomonas cytochromes c-551. Biochemistry. 23: 1831-8. PMID 6326813 DOI: 10.1021/Bi00303A039 |
0.348 |
|
| 1984 |
Williams G, Moore GR. Reactions of mitochondrial cytochrome c with iron-polyaminocarboxylate complexes. Journal of Inorganic Biochemistry. 22: 1-10. PMID 6092533 DOI: 10.1016/0162-0134(84)85058-8 |
0.393 |
|
| 1984 |
Moura JG, Moore GR, Williams RJ, Probst I, Legall J, Xavier AV. Nuclear-magnetic-resonance studies of Desulfuromonas acetoxidans cytochrome c551.5 (c7). European Journal of Biochemistry / Febs. 144: 433-40. PMID 6092073 |
0.65 |
|
| 1984 |
Ragg E, Moore GR. Association constants for metal hexacyanide binding to cytochrome c. Journal of Inorganic Biochemistry. 21: 253-61. PMID 6088687 DOI: 10.1016/0162-0134(84)83008-1 |
0.34 |
|
| 1984 |
Moore GR, Williams G. Assignment of 1H-NMR resonances of the heme and axial histidine ligand of mitochondrial cytochrome c Biochimica Et Biophysica Acta (Bba) - Protein Structure and Molecular Enzymology. 788: 147-150. DOI: 10.1016/0167-4838(84)90307-8 |
0.355 |
|
| 1983 |
Moore GR, Ratcliffe RG, Williams RJ. NMR and the biochemist. Essays in Biochemistry. 19: 142-95. PMID 6389121 |
0.383 |
|
| 1983 |
Moore GR. Control of redox properties of cytochrome c by special electrostatic interactions. Febs Letters. 161: 171-5. PMID 6311622 DOI: 10.1016/0014-5793(83)81001-1 |
0.337 |
|
| 1983 |
Robinson MN, Boswell AP, Huang ZX, Eley CG, Moore GR. The conformation of eukaryotic cytochrome c around residues 39, 57, 59 and 74. The Biochemical Journal. 213: 687-700. PMID 6311172 DOI: 10.1042/Bj2130687 |
0.423 |
|
| 1983 |
Boswell AP, Moore GR, Williams RJ, Harris DE, Wallace CJ, Bocieck S, Welti D. Ionization of tyrosine and lysine residues in native and modified horse cytochrome c. The Biochemical Journal. 213: 679-86. PMID 6311171 DOI: 10.1042/Bj2130679 |
0.521 |
|
| 1983 |
Clayden NJ, Moore GR, Williams RJP, Baldwin JE, Crossley MJ. Nuclear magnetic resonance study of metal complexes of the 'capped' porphyrins Journal of the Chemical Society, Perkin Transactions 2. 1863-1868. DOI: 10.1039/P29830001863 |
0.618 |
|
| 1982 |
Moore GR, Huang ZX, Eley CG, Barker HA, Williams G, Robinson MN, Williams RJ. Electron transfer in biology. The function of cytochrome c. Faraday Discussions of the Chemical Society. 74: 311-29. PMID 6305705 DOI: 10.1039/Dc9827400311 |
0.489 |
|
| 1982 |
Williams G, Eley CG, Moore GR, Robinson MN, Williams RJ. The reaction of cytochrome c with [Fe(EDTA)(H2O)]-. Febs Letters. 150: 293-9. PMID 6297974 DOI: 10.1016/0014-5793(82)80754-0 |
0.453 |
|
| 1982 |
Moura JJ, Santos H, Moura I, LeGall J, Moore GR, Williams RJ, Xavier AV. NMR redox studies of Desulfovibrio vulgaris Cytochrome c3. Electron transfer mechanisms. European Journal of Biochemistry / Febs. 127: 151-5. PMID 6291937 DOI: 10.1111/J.1432-1033.1982.Tb06849.X |
0.614 |
|
| 1982 |
Eley CG, Moore GR, Williams RJ, Neupert W, Boon PJ, Brinkhof HH, Nivard RJ, Tesser GI. Structural role of the tyrosine residues of cytochrome c. The Biochemical Journal. 205: 153-65. PMID 6289807 DOI: 10.1042/Bj2050153 |
0.539 |
|
| 1982 |
Eley CG, Moore GR, Williams G, Williams RJ. 1H NMR studies of the electron exchange between cytochrome c and iron hexacyanides. Definition of the iron hexacyanide binding sites on cytochrome c. European Journal of Biochemistry / Febs. 124: 295-303. PMID 6284504 DOI: 10.1111/J.1432-1033.1982.Tb06591.X |
0.533 |
|
| 1982 |
Boswell AP, Eley CG, Moore GR, Robinson MN, Williams G, Williams RJ, Neupert WJ, Hennig B. 1H NMR studies of eukaryotic cytochrome c. Resonance assignments and iron-hexacyanide-mediated electron exchange. European Journal of Biochemistry / Febs. 124: 289-94. PMID 6284503 DOI: 10.1111/J.1432-1033.1982.Tb06590.X |
0.482 |
|
| 1982 |
Boswell AP, Moore GR, Williams RJ. The binding of platinum complexes to tuna cytochrome c. The Biochemical Journal. 201: 523-6. PMID 6284122 DOI: 10.1042/Bj2010523 |
0.53 |
|
| 1982 |
Moore GR, McClune GJ, Clayden NJ, Williams RJ, Alsaadi BM, Angström J, Ambler RP, van Beeumen J, Tempst P, Bartsch RG, Meyer TE, Kamen MD. Metal coordination centres of class II cytochromes c. European Journal of Biochemistry / Febs. 123: 73-80. PMID 6279397 DOI: 10.1111/J.1432-1033.1982.Tb06500.X |
0.65 |
|
| 1982 |
Clayden NJ, Moore GR, Williams RJP, Baldwin JE, Crossley MJ. Metalation shifts in the nuclear magnetic resonance spectra of ‘capped’ porphyrins Journal of the Chemical Society-Perkin Transactions 1. 14: 1693-1698. DOI: 10.1039/P29820001693 |
0.382 |
|
| 1982 |
Ångström J, Moore GR, Williams RJ. The magnetic susceptibility of ferricytochrome c Biochimica Et Biophysica Acta (Bba) - Protein Structure and Molecular Enzymology. 703: 87-94. DOI: 10.1016/0167-4838(82)90014-0 |
0.477 |
|
| 1981 |
Boswell AP, Moore GR, Williams RJ, Wallace CJ, Boon PJ, Nivard RJ, Tesser GI. Structural studies of eukaryotic cytochrome c modified at methionine-65. The Biochemical Journal. 193: 493-502. PMID 6272709 DOI: 10.1042/Bj1930493 |
0.523 |
|
| 1981 |
Emptage MH, Xavier AV, Wood JM, Alsaadi BM, Moore GR, Pitt RC, Williams RJ, Ambler RP, Bartsch RG. Nuclear magnetic resonance studies of Rhodospirillum rubrum cytochrome c'. Biochemistry. 20: 58-64. PMID 6258631 DOI: 10.1021/Bi00504A010 |
0.673 |
|
| 1980 |
Boswell AP, Moore GR, Williams RJ, Chien JC, Dickinson LC. Nuclear magnetic resonance studies of the phenylalanine residues of eukaryotic cytochrome c. Journal of Inorganic Biochemistry. 13: 347-52. PMID 6257839 DOI: 10.1016/S0162-0134(00)80254-8 |
0.463 |
|
| 1980 |
Boswell AP, Moore GR, Williams RJ. Nuclear-magnetic-resonance studies of the methanol-induced denaturation of ferricytochrome c and ferrocytochrome c. Biochemical Society Transactions. 8: 638-9. PMID 6256242 DOI: 10.1042/Bst0080638 |
0.403 |
|
| 1980 |
Boswell AP, McClune GJ, Moore GR, Williams RJ, Pettigrew GW, Inubishi T, Yonetani T, Harris DE. Nuclear-magnetic-resonance study of the interaction of cytochrome c with cytochrome c peroxidase. Biochemical Society Transactions. 8: 637-8. PMID 6256241 |
0.415 |
|
| 1980 |
Moore GR, Pettigrew GW, Pitt RC, Williams RJ. pH dependence of the redox potential of Pseudomonas aeruginosa cytochrome c-551. Biochimica Et Biophysica Acta. 590: 261-71. PMID 6245686 DOI: 10.1016/0005-2728(80)90030-4 |
0.472 |
|
| 1980 |
Moore GR, Williams RJ. The solution structures of tuna and horse cytochromes c. European Journal of Biochemistry / Febs. 103: 533-41. PMID 6244162 DOI: 10.1111/J.1432-1033.1980.Tb05977.X |
0.467 |
|
| 1980 |
Moore GR, Williams RJ. The stability of ferricytochrome c. Temperature dependence of its NMR spectrum. European Journal of Biochemistry / Febs. 103: 523-32. PMID 6244161 DOI: 10.1111/J.1432-1033.1980.Tb05976.X |
0.452 |
|
| 1980 |
Moore GR, Williams RJ. Nuclear-magnetic-resonance studies of ferrocytochrome c. pH and temperature dependence. European Journal of Biochemistry / Febs. 103: 513-21. PMID 6244160 DOI: 10.1111/J.1432-1033.1980.Tb05975.X |
0.441 |
|
| 1980 |
Moore GR, Williams RJ. Nuclear-magnetic-resonance studies of eukaryotic cytochrome c. Assignment of resonances of aliphatic amino acids. European Journal of Biochemistry / Febs. 103: 503-12. PMID 6244159 |
0.437 |
|
| 1980 |
Moore GR, Williams RJ. Nuclear-magnetic-resonance studies of eukaryotic cytochrome c. Assignment of resonances of aromatic amino acids. European Journal of Biochemistry / Febs. 103: 493-502. PMID 6244158 DOI: 10.1111/J.1432-1033.1980.Tb05973.X |
0.44 |
|
| 1980 |
Moore GR, Williams RJ. Comparison of the structures of various eukaryotic ferricytochromes c and ferrocytochromes and their antigenic differences. European Journal of Biochemistry / Febs. 103: 543-50. PMID 6153614 DOI: 10.1111/J.1432-1033.1980.Tb05978.X |
0.472 |
|
| 1980 |
Moore GR, Williams RJ, Chien JC, Dickson L. Nuclear magnetic resonance studies of metal substituted horse cytochrome c Journal of Inorganic Biochemistry. 12: 1-15. DOI: 10.1016/S0162-0134(00)80039-2 |
0.484 |
|
| 1978 |
Moura JJ, Xavier AV, Cookson DJ, Moore GR, Williams RJ, Fauque G, Bruschi M, Le Gall J. Electron-transfer mechanisms in multihaem cytochromes [proceedings]. Biochemical Society Transactions. 6: 1285-7. PMID 744410 DOI: 10.1042/bst0061285 |
0.541 |
|
| 1978 |
Cookson DJ, Moore GR, Pitt RC, Williams RJ, Campbell ID, Ambler RP, Bruschi M, LeGall J. Structural homology of cytochromes c. European Journal of Biochemistry / Febs. 83: 261-75. PMID 203462 DOI: 10.1111/J.1432-1033.1978.Tb12091.X |
0.471 |
|
| 1977 |
Moore GR, Williams RJ. Structural basis for the variation in redox potential of cytochromes. Febs Letters. 79: 229-32. PMID 891938 DOI: 10.1016/0014-5793(77)80793-X |
0.414 |
|
| 1977 |
Moura JJ, Xavier AV, Cookson DJ, Moore GR, Williams RJ. Redox states of cytochrome c3 in the absence and presence of ferredoxin. Febs Letters. 81: 275-80. PMID 200473 DOI: 10.1016/0014-5793(77)80534-6 |
0.619 |
|
| 1977 |
Moore GR, Pitt RC, Williams RJ. Nuclear-magnetic-resonance studies of Pseudomonas aeruginosa cytochrome c-551. European Journal of Biochemistry / Febs. 77: 53-60. PMID 198212 DOI: 10.1111/J.1432-1033.1977.Tb11640.X |
0.451 |
|
| 1976 |
Campbell ID, Dobson CM, Moore GR, Perkins SJ, Williams RJ. Temperature dependent molecular motion of a tyrosine residue of ferrocytochrome C. Febs Letters. 70: 96-100. PMID 186328 DOI: 10.1016/0014-5793(76)80734-X |
0.608 |
|
| 1975 |
Dobson CM, Moore GR, Williams RJ. Assignment of aromatic amino acid PMR resonances of horse ferricytochrome c. Febs Letters. 51: 60-5. PMID 235463 DOI: 10.1016/0014-5793(75)80854-4 |
0.557 |
|
| 1975 |
Moore GR, Williams RJ. Assignment of aromatic amino acid PMR resonances of horse ferrocytochrome C. Febs Letters. 53: 334-8. PMID 165969 DOI: 10.1016/0014-5793(75)80049-4 |
0.396 |
|
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