Year |
Citation |
Score |
2002 |
Perutz MF, Finch JT, Berriman J, Lesk A. Amyloid fibers are water-filled nanotubes. Proceedings of the National Academy of Sciences of the United States of America. 99: 5591-5. PMID 11960014 DOI: 10.1073/Pnas.042681399 |
0.313 |
|
2000 |
Perutz M. Paul Sigler (1934-2000) Cell. 101: 23-24. PMID 10778852 DOI: 10.1016/S0092-8674(02)71111-2 |
0.349 |
|
1999 |
Chen YW, Stott K, Perutz MF. Crystal structure of a dimeric chymotrypsin inhibitor 2 mutant containing an inserted glutamine repeat. Proceedings of the National Academy of Sciences of the United States of America. 96: 1257-61. PMID 9990011 DOI: 10.1073/pnas.96.4.1257 |
0.316 |
|
1998 |
Bettati S, Mozzarelli A, Perutz MF. Allosteric mechanism of haemoglobin: rupture of salt-bridges raises the oxygen affinity of the T-structure. Journal of Molecular Biology. 281: 581-5. PMID 9710531 DOI: 10.1006/jmbi.1998.1983 |
0.354 |
|
1998 |
Perutz MF, Wilkinson AJ, Paoli M, Dodson GG. The stereochemical mechanism of the cooperative effects in hemoglobin revisited. Annual Review of Biophysics and Biomolecular Structure. 27: 1-34. PMID 9646860 DOI: 10.1146/annurev.biophys.27.1.1 |
0.312 |
|
1995 |
Perutz MF. Polar zippers: their role in human disease. Pharmaceutica Acta Helvetiae. 69: 213-24. PMID 7651965 DOI: 10.1016/0031-6865(95)00003-R |
0.342 |
|
1994 |
Perutz MF, Shih DT, Williamson D. The chloride effect in human haemoglobin. A new kind of allosteric mechanism. Journal of Molecular Biology. 239: 555-60. PMID 8006967 DOI: 10.1006/jmbi.1994.1394 |
0.3 |
|
1993 |
Shih DT, Luisi BF, Miyazaki G, Perutz MF, Nagai K. A mutagenic study of the allosteric linkage of His(HC3)146 beta in haemoglobin. Journal of Molecular Biology. 230: 1291-6. PMID 8487305 DOI: 10.1006/jmbi.1993.1242 |
0.547 |
|
1993 |
Perutz MF, Fermi G, Poyart C, Pagnier J, Kister J. A novel allosteric mechanism in haemoglobin. Structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin. Journal of Molecular Biology. 233: 536-45. PMID 8411160 DOI: 10.1006/jmbi.1993.1530 |
0.313 |
|
1992 |
Camardella L, Caruso C, D'Avino R, di Prisco G, Rutigliano B, Tamburrini M, Fermi G, Perutz MF. Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative. Journal of Molecular Biology. 224: 449-60. PMID 1560461 DOI: 10.1016/0022-2836(92)91007-C |
0.375 |
|
1992 |
Fermi G, Perutz MF, Williamson D, Stein P, Shih DT. Structure-function relationships in the low-affinity mutant haemoglobin Aalborg (Gly74 (E18)beta----Arg). Journal of Molecular Biology. 226: 883-8. PMID 1507231 DOI: 10.1016/0022-2836(92)90638-Z |
0.322 |
|
1992 |
Eisenberg D, Perutz MF, Buckingham AD, Graf L, Thornton J, Blow DM, Fersht AR, Karplus M, Johnson LN, Rippmann F, Dodson GG, Edwards PN, Halling P, Wüthrich K, Symons MCR, et al. General discussion Faraday Discussions. 93: 107-129. DOI: 10.1039/FD9929300107 |
0.484 |
|
1990 |
Huang Y, Pagnier J, Magne P, Baklouti F, Kister J, Delaunay J, Poyart C, Fermi G, Perutz MF. Structure and function of hemoglobin variants at an internal hydrophobic site: consequences of mutations at the beta 27 (B9) position. Biochemistry. 29: 7020-3. PMID 2223757 DOI: 10.1021/Bi00482A010 |
0.312 |
|
1990 |
Perutz MF. Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide. Annual Review of Physiology. 52: 1-25. PMID 2184753 DOI: 10.1146/annurev.ph.52.030190.000245 |
0.31 |
|
1988 |
Perutz MF, Fermi G, Fogg J, Rahbar S. Indirect allosteric effects of a neutral mutation. Structure of deoxyhaemoglobin north Chicago (ProC2(36)beta----Ser). Journal of Molecular Biology. 201: 459-61. PMID 3418705 DOI: 10.1016/0022-2836(88)90154-4 |
0.326 |
|
1988 |
Levitt M, Perutz MF. Aromatic rings act as hydrogen bond acceptors. Journal of Molecular Biology. 201: 751-4. PMID 3172202 DOI: 10.1016/0022-2836(88)90471-8 |
0.417 |
|
1987 |
Perutz MF, Fermi G, Luisi B, Shaanan B, Liddington RC. Stereochemistry of cooperative mechanisms in hemoglobin. Cold Spring Harbor Symposia On Quantitative Biology. 52: 555-65. PMID 3454276 DOI: 10.1021/Ar00141A001 |
0.491 |
|
1984 |
Fermi G, Perutz MF, Shaanan B, Fourme R. The crystal structure of human deoxyhaemoglobin at 1.74 A resolution. Journal of Molecular Biology. 175: 159-74. PMID 6726807 DOI: 10.1016/0022-2836(84)90472-8 |
0.354 |
|
1983 |
Abraham DJ, Perutz MF, Phillips SE. Physiological and x-ray studies of potential antisickling agents. Proceedings of the National Academy of Sciences of the United States of America. 80: 324-8. PMID 6572894 DOI: 10.1073/Pnas.80.2.324 |
0.308 |
|
1982 |
Perutz MF. Nature of the iron-oxygen bond and control of oxygen affinity of the haem by the structure of the globin in haemoglobin. Advances in Experimental Medicine and Biology. 148: 31-48. PMID 7124526 DOI: 10.1007/978-1-4615-9281-5_4 |
0.322 |
|
1982 |
Fermi G, Perutz MF, Dickinson LC, Chien JC. Structure of human deoxy cobalt haemoglobin. Journal of Molecular Biology. 155: 495-505. PMID 7086900 DOI: 10.1016/0022-2836(82)90483-1 |
0.349 |
|
1981 |
Phillips SE, Hall D, Perutz MF. Structure of deoxyhaemoglobin Zürich (HisE7(63 beta) - greater than Arg). Journal of Molecular Biology. 150: 137-41. PMID 7299818 DOI: 10.1016/0022-2836(81)90329-6 |
0.324 |
|
1980 |
Perutz MF, Kilmartin JV, Nishikura K, Fogg JH, Butler PJ, Rollema HS. Identification of residues contributing to the Bohr effect of human haemoglobin. Journal of Molecular Biology. 138: 649-68. PMID 7411620 DOI: 10.1016/S0022-2836(80)80022-2 |
0.61 |
|
1980 |
Kilmartin JV, Fogg JH, Perutz MF. Role of C-terminal histidine in the alkaline Bohr effect of human hemoglobin. Biochemistry. 19: 3189-83. PMID 7407039 |
0.598 |
|
1980 |
Perutz MF. Stereochemical mechanism of oxygen transport by haemoglobin. Proceedings of the Royal Society of London. Series B, Biological Sciences. 208: 135-62. PMID 6105654 DOI: 10.1098/rspb.1980.0047 |
0.327 |
|
1978 |
Tucker PW, Phillips SE, Perutz MF, Houtchens R, Caughey WS. Structure of haemoglobins Zürich (his e7(63)beta leads to arg) and Sydney (val e11(67)beta leads to ala) and the role of the distal residues in ligand binding. Progress in Clinical and Biological Research. 21: 3-16. PMID 662894 |
0.449 |
|
1978 |
Tucker PW, Phillips SE, Perutz MF, Houtchens R, Caughey WS. Structure of hemoglobins Zürich [His E7(63)beta replaced by Arg] and Sydney [Val E11(67)beta replaced by Ala] and role of the distal residues in ligand binding. Proceedings of the National Academy of Sciences of the United States of America. 75: 1076-80. PMID 274697 |
0.457 |
|
1977 |
Fermi G, Perutz MF. Structure of human fluoromethaemoglobin with inositol hexaphosphate. Journal of Molecular Biology. 114: 421-31. PMID 909092 DOI: 10.1016/0022-2836(77)90259-5 |
0.342 |
|
1977 |
Frier JA, Perutz MF. Structure of human foetal deoxyhaemoglobin. Journal of Molecular Biology. 112: 97-112. PMID 881729 DOI: 10.1016/S0022-2836(77)80158-7 |
0.388 |
|
1977 |
Ladner RC, Heidner EJ, Perutz MF. The structure of horse methaemoglobin at 2-0 A resolution. Journal of Molecular Biology. 114: 385-414. PMID 561852 DOI: 10.1016/0022-2836(77)90256-X |
0.351 |
|
1977 |
Tucker PW, Perutz MF. Mechanism of charge compensation and impairment of co-operative functions in haemoglobin Tacoma (Arg B12(30)beta leads to Ser). Journal of Molecular Biology. 114: 415-20. PMID 20512 |
0.421 |
|
1976 |
Perutz MF, Kilmartin JV, Nagai K, Szabo A, Simon SR. Influence of globin structures on the state of the heme. Ferrous low spin derivatives Biochemistry. 15: 378-387. PMID 1247524 DOI: 10.1021/Bi00647A022 |
0.643 |
|
1976 |
Asakura T, Adachi K, Wiley JS, Fung LW, Ho C, Kilmartin JV, Perutz MF. Structure and function of haemoglobin Philly (Tyr C1 (35) β→Phe) Journal of Molecular Biology. 104: 185-195. PMID 957431 DOI: 10.1016/0022-2836(76)90008-5 |
0.642 |
|
1976 |
Heidner EJ, Ladner RC, Perutz MF. Structure of horse carbonmonoxyhaemoglobin Journal of Molecular Biology. 104: 707-722. PMID 950675 DOI: 10.1016/0022-2836(76)90130-3 |
0.35 |
|
1975 |
Perutz MF, Raidt H. Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2 Nature. 255: 256-259. PMID 1143325 DOI: 10.1038/255256a0 |
0.312 |
|
1974 |
Arnone A, Perutz MF. Structure of inositol hexaphosphate human deoxyhaemoglobin complex Nature. 249: 34-36. PMID 4364353 DOI: 10.1038/249034a0 |
0.344 |
|
1973 |
Anderson NL, Perutz MF, Stamatoyannopoulos G. Site of the amino acid substitution in haemoglobin Seattle (α(A)2 β(70 Asp)2) Nature New Biol.. 243: 274-275. PMID 4515494 DOI: 10.1038/NEWBIO243274A0 |
0.318 |
|
1972 |
Hewitt JA, Kilmartin JV, Eyck LF, Perutz MF. Noncooperativity of the dimer in the reaction of hemoglobin with oxygen (human-dissociation-equilibrium-sulfhydryl-absorption-x-ray analysis) Proceedings of the National Academy of Sciences of the United States of America. 69: 203-207. PMID 4500548 DOI: 10.1073/Pnas.69.1.203 |
0.67 |
|
1972 |
Crick FHC, Kendrew JC, Hodgkin A, Keynes RD, Perutz MF, Wilkins M, Curran PF, Edelman I, Hutchinson F, Rosenblith WA, Soloman AA, Tobias C, Watson J, Monier R, Buchthal F, et al. Aharon katzir katchalsky Nature. 237: 357. DOI: 10.1038/237357A0 |
0.705 |
|
1971 |
Perutz MF, Pulsinelli P, Eyck LT, Kilmartin JV, Shibata S, Iuchi I, Miyaji T, Hamilton HB. Haemoglobin Hiroshima and the mechanism of the alkaline Bohr effect Nature: New Biology. 232: 147-149. PMID 5285571 DOI: 10.1038/Newbio232147A0 |
0.648 |
|
1971 |
Greer J, Perutz MF. Three dimensional structure of haemoglobin Rainier Nature: New Biology. 230: 261-264. PMID 5280664 DOI: 10.1038/Newbio230261A0 |
0.306 |
|
1971 |
Morimoto H, Lehmann H, Perutz MF. Molecular pathology of human haemoglobin: Stereochemical interpretation of abnormal oxygen affinities [15] Nature. 232: 408-413. PMID 4938842 DOI: 10.1038/232408a0 |
0.547 |
|
1970 |
Bolton W, Perutz MF. Three dimensional fourier synthesis of horse deoxyhaemoglobin at 2.8 å resolution Nature. 228: 551-552. PMID 5472471 DOI: 10.1038/228551a0 |
0.331 |
|
1969 |
Perutz MF, Muirhead H, Mazzarella L, Crowther RA, Greer J, Kilmartin JV. Identification of Residues responsible for the Alkaline Bohr Effect in Haemoglobin Nature. 222: 1240-1243. PMID 5789657 DOI: 10.1038/2221240a0 |
0.733 |
|
1969 |
Perutz MF. The Croonian Lecture, 1968. The haemoglobin molecule Proceedings of the Royal Society of London. Series B. Biological Sciences. 173: 113-140. PMID 4389425 DOI: 10.1098/Rspb.1969.0043 |
0.366 |
|
1969 |
Crick FHC, Kendrew JC, Perutz MF, Sanger F, Monod J, Jacob F, Lwoff A. International conferences Nature. 224: 93-94. DOI: 10.1038/224093a0 |
0.699 |
|
1968 |
Perutz MF, Lehmann H. Molecular pathology of human haemoglobin. Nature. 219: 902-9. PMID 5691676 DOI: 10.1038/219902A0 |
0.536 |
|
1968 |
Perutz MF, Muirhead H, Cox JM, Goaman LCG. Three-dimensional fourier synthesis of horse oxyhaemoglobin at 2.8 Å resolution: The atomic model Nature. 219: 131-139. PMID 5659637 DOI: 10.1038/219131a0 |
0.653 |
|
1968 |
Perutz MF, Miurhead H, Cox JM, Goaman LC, Mathews FS, McGandy EL, Webb LE. Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: (1) x-ray analysis. Nature. 219: 29-32. PMID 5659617 DOI: 10.1038/219029a0 |
0.326 |
|
1968 |
Bolton W, Cox JM, Perutz MF. Structure and function of haemoglobin. IV. A three-dimensional Fourier synthesis of horse deoxyhaemoglobin at 5.5 Å resolution Journal of Molecular Biology. 33: 283-297. PMID 5646648 DOI: 10.1016/0022-2836(68)90294-5 |
0.379 |
|
1968 |
Muirhead H, Cox J, Mazzarella L, Perutz MF. A comparison of the structures of horse oxy- and human deoxyhaemoglobin Journal De Chimie Physique. 65: 188-189. DOI: 10.1051/JCP/1968650188 |
0.637 |
|
1967 |
Muirhead H, Cox JM, Mazzarella L, Perutz MF. Structure and function of haemoglobin. 3. A three-dimensional fourier synthesis of human deoxyhaemoglobin at 5.5 Angstrom resolution Journal of Molecular Biology. 28: 117-156. PMID 6051747 |
0.6 |
|
1966 |
Perutz MF, Mathews FS. An X-ray study of azide methaemoglobin Journal of Molecular Biology. 21: 199-202. PMID 5969763 DOI: 10.1016/0022-2836(66)90088-X |
0.324 |
|
1965 |
Perutz M, Kendrew J, Watson H. Structure and function of haemoglobin Journal of Molecular Biology. 13: 669-678. DOI: 10.1016/S0022-2836(65)80134-6 |
0.768 |
|
1964 |
Perutz MF, Bolton W, Diamond R, Muirhead H, Watson HC. Structure of hæmoglobin : AAn X-ray examination of reduced horse æhmoglobin Nature. 203: 687-690. DOI: 10.1038/203687a0 |
0.641 |
|
1963 |
Muirhead H, Perutz MF. Structure of Reduced Human Hemoglobin Cold Spring Harbor Symposia On Quantitative Biology. 28: 451-459. DOI: 10.1101/SQB.1963.028.01.061 |
0.636 |
|
1963 |
Muirhead H, Perutz MF. Structure of hæemoglobin: A three-dimensional fourier synthesis of reduced human haemoglobin at 5.5 Å resolution Nature. 199: 633-638. DOI: 10.1038/199633a0 |
0.637 |
|
1962 |
Cullis AF, Muirhead H, Perutz MF, Rossmann MG, North ACT. The structure of haemoglobin. IX. A three-dimensional Fourier synthesis at 5.5 Å resolution: description of the structure Proceedings of the Royal Society a: Mathematical, Physical and Engineering Sciences. 265: 161-187. DOI: 10.1098/Rspa.1962.0002 |
0.715 |
|
1961 |
Cullis AF, Muirhead H, Perutz MF, Rossmann MG, North ACT. The Structure of Haemoglobin. VIII. A Three-Dimensional Fourier Synthesis at 5.5 Å Resolution: Determination of the Phase Angles Proceedings of the Royal Society a: Mathematical, Physical and Engineering Sciences. 265: 15-38. DOI: 10.1098/Rspa.1961.0220 |
0.675 |
|
1961 |
Stockell A, Perutz M, Muirhead H, Glauser SC. A comparison of adult and foetal horse haemoglobins Journal of Molecular Biology. 3: 112-116. DOI: 10.1016/S0022-2836(61)80013-2 |
0.583 |
|
1960 |
PERUTZ MF, ROSSMANN MG, CULLIS AF, MUIRHEAD H, WILL G, NORTH AC. Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis. Nature. 185: 416-22. PMID 18990801 DOI: 10.1038/185416A0 |
0.688 |
|
1957 |
KENDREW JC, PERUTZ MF. X-ray studies of compounds of biological interest. Annual Review of Biochemistry. 26: 327-72. PMID 13488398 DOI: 10.1146/annurev.bi.26.070157.001551 |
0.723 |
|
1955 |
Perutz MF, Trotter IF, Howells ER, Green DW. An X-ray study of reduced human haemoglobin Acta Crystallographica. 8: 241-245. DOI: 10.1107/S0365110X55000790 |
0.306 |
|
1954 |
Green DW, Ingram VM, Perutz MF. The structure of haemoglobin - IV. Sign determination by the isomorphous replacement method Proceedings of the Royal Society a: Mathematical, Physical and Engineering Sciences. 225: 287-307. DOI: 10.1098/Rspa.1954.0203 |
0.312 |
|
1954 |
Bragg L, Howells ER, Perutz MF. The Structure of Haemoglobin. II Proceedings of the Royal Society a: Mathematical, Physical and Engineering Sciences. 222: 33-44. DOI: 10.1098/Rspa.1954.0050 |
0.324 |
|
1953 |
PERUTZ MF. An optical method for finding the molecular orientation in different forms of crystalline haemoglobin; changes in dichroism accompanying oxygenation and reduction Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character. Royal Society (Great Britain). 141: 69-71. PMID 13047271 DOI: 10.1098/Rspb.1953.0021 |
0.307 |
|
1952 |
Bragg WL, Perutz MF. The external form of the haemoglobin molecule. II Acta Crystallographica. 5: 323-328. DOI: 10.1107/S0365110X5200099X |
0.512 |
|
1952 |
Bragg WL, Howells ER, Perutz MF. Arrangement of polypeptide chains in horse methaemoglobin Acta Crystallographica. 5: 136-141. DOI: 10.1107/S0365110X52000277 |
0.546 |
|
1951 |
Perutz MF. New X-ray evidence on the configuration of polypeptide chains: Polypeptide chains in poly-γ-benzyl-l-glutamate, keratin and hæmoglobin Nature. 167: 1053-1054. PMID 14843172 DOI: 10.1038/1671053a0 |
0.302 |
|
1950 |
Bragg L, Kendrew JC, Perutz MF. Polypeptide chain configurations in crystalline proteins Proceedings of the Royal Society a: Mathematical, Physical and Engineering Sciences. 203: 321-357. DOI: 10.1098/Rspa.1950.0142 |
0.761 |
|
1949 |
PERUTZ MF. An X-ray study of horse methemoglobin Proceedings of the Royal Society of London. Series a: Mathematical And. 195: 474-499. PMID 18110616 DOI: 10.1098/rspa.1949.0005 |
0.317 |
|
1948 |
KENDREW JC, PERUTZ MF. A comparative X-ray study of foetal and adult sheep haemoglobins. Proceedings of the Royal Society of London. Series a, Mathematical and Physical Sciences. 194: 375-98. PMID 18884624 DOI: 10.1098/Rspa.1948.0087 |
0.743 |
|
1942 |
Perutz MF. Crystal structure of oxyhæmoglobin Nature. 150: 324-325. DOI: 10.1038/150324A0 |
0.321 |
|
1942 |
Perutz MF. X-ray analysis of hæmoglobin Nature. 149: 491-494. DOI: 10.1038/149491A0 |
0.303 |
|
1938 |
BERNAL JD, FANKUCHEN I, PERUTZ M. An X-Ray Study of Chymotrypsin and HÆmoglobin Nature. 141: 523-524. DOI: 10.1038/141523a0 |
0.625 |
|
Show low-probability matches. |