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The 100 most-cited articles from JMB
Article No. jmbi.1999.3148 available online at http://www.idealibrary.com on
J. Mol. Biol. (1999) 293, 173±176
The 100 Most-Cited Articles from JMB Tessa Picknett1* and Kate Davis2 1
Academic Press, 24-28 Oval Road London, NW1 7DX, UK 2
Academic Press, 24-28 Oval Road, London, NW1 7DX, UK
Over the last 40 years, JMB has published many thousands of articles, all of which have been important in some way. Compiling a list of the `most important' however, is an invidious task. Friendships can falter on such an undertaking, but the Institute of Scienti®c Information has provided us with an objective methodology for `ranking' articles, according to the number of times any paper is cited in other publications. This evaluation can of course be criticised for its bias towards papers describing novel techniques or methods. Often, the true intellectual milestones may be found in the reference list of the most cited papers. With increasing age, each paper also has more time in which to have been cited, and so the group of highest scoring articles is also dominated by some of the oldest. On the other hand, with increasing time, papers have an increasing chance of being forgotten, and the citation rates of these are therefore also a measure of their persisting importance. On balance, it does represent a value in some way related to how often that paper has been used. With many caveats, we present the list of the 100 most cited papers in JMB over the past 40 years. Many of these papers have helped or in¯uenced both a great many people, and a great many subsequent advances in molecular biology. # 1999 Academic Press
*Corresponding author
1. Southern E. M.1975. Detection of speci®c sequences among DNA fragments separated by gel electrophoresi. J. Mol. Biol. 98, 503-517. 2. Rigby, P. W., Dieckmann, M., Rhodes, C. & Berg, P. (1977). Labeling deoxyribonucleic acid to high speci®c activity in vitro by nick translation with DNA polymerase I. J. Mol. Biol. 113, 237-251 3. Marmur, J. (1961). A procedure for the isolation of deoxyribonucleic acid from microorganisms. J. Mol. Biol. 3, 208-218. 4. Kyte, J. & Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132 5. Monod, J., Wyman, J. & Changeux, J.-P. (1965). On the Nature of Allosteric Transitions: A Plausible Model. J. Mol. Biol. 12, 88-118 6. Hanahan, D. (1983). Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166, 557580 7. Hirt, B. (1967). Selective extraction of polyoma DNA from infected mouse cell cultures. J. Mol. Biol. 26, 365-369 8. Sanger, F., Coulson, A. R., Barrell, B. G., Smith, A. J. & Roe, B. A. (1980). Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J. Mol. Biol. 143, 161-178 0022-2836/99/420173±4 $30.00/0
9. Bernstein, F. C., Koetzle, T. F., Williams, G. J., Meyer, E. E., Jr, Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T. & Tasumi, M. (1977). The Protein Data Bank: a computer-based archival ®le for macromolecular structures. J. Mol. Biol. 112, 535-542 10. Jacob, F. & Monod, J. (1961). Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 3, 318-356 11. Garnier, J., Osguthorpe, D. J. & Robson, B. (1978). Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97-120 12. Laemmli, U. K. & Favre, M. (1973). Maturation of the head of bacteriophage T4. I. DNA packaging events. J. Mol. Biol. 80, 575-599 13. Boyer, H. W. & Roulland-Dussoix, D. (1969). A complementation analysis of the restriction and modi®cation of DNA in Escherichia coli. J. Mol. Biol. 41, 459-472 14. Altschul, S. F., Gish, W., Miller, W., Myers, E. W. & Lipman, D. J. (1990). Basic local alignment search tool. J. Mol. Biol. 215, 403-410 15. Marmur, J. & Doty, P. (1962). Determination of the base composition of deoxyribonucleic acid from its thermal denaturation temperature. J. Mol. Biol. 5, 109-118 # 1999 Academic Press
174 16. Studier, F. W. (1965). Sedimentation Studies of the Size and Shape of DNA. J. Mol. Biol. 11, 373-390 17. Studier, F. W. (1973). Analysis of bacteriophage T7 early RNAs and proteins on slab gels. J. Mol. Biol. 2, 237-248. 18. Studier, F. W. & Moffatt, B. A. (1986). Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 79, 113-130 19. Gillespie, D. & Spiegelman, S. (1965). A quantitative assay for DNA-RNA hybrids with DNA immobilized on a membrane. J. Mol. Biol. 189, 829-842 20. Mandel, M. & Higa, A. (1970). Calcium-dependent bacteriophage DNA infection. J. Mol. Biol. 53, 159162 21. Matthews, B. W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497 22. Lee, B. & Richards, F. M. (1971). The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400 23. Schildkraut, C. L., Marmur, J. & Doty, P. (1962). Determination of the base composition of deoxyribonucleic acid from its buoyant density in CsC1. J. Mol. Biol. 4, 430-443 24. Clegg, J. B., Naughton, M. A. & Weatherball, D. J. (1966). Abnormal human haemoglobins. Separation and characterization of the alpha and beta chains by chromatography, and the determination of two new variants, hb Chesapeak and hb J (Bangkok). J. Mol. Biol. 19, 91-108 25. Needleman, S. B. & Wunsch, C. D. (1970). A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48, 443-453 26. Frischauf, A. M., Lehrach, H., Poustka, A. & Murray, N. (1983). Lambda replacement vectors carrying polylinker sequences. J. Mol. Biol. 170, 827-842 27. Huxley, H. E. (1963). Electron Microscope Studies on the Structure of Natural and Synthetic Protein Filaments from Striated Muscle. J. Mol. Biol. 7, 18-30 28. McDonell, M. W., Simon, M. N. & Studier, F. W. (1977). Analysis of restriction fragments of T7 DNA and determination of molecular weights by electrophoresis in neutral and alkaline gels. J. Mol. Biol. 110, 119-146 29. Casadaban, M. J. & Cohen, S. N. (1980). Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138, 179-207 30. Monod, J., Changeux, J.-P. & Jacob, F. (1963). Allosteric proteins and cellular control systems. J. Mol. Biol. 6, 306-329 31. Lerman, L. S. (1961). Structural considerations in the interaction of DNA and acridines. J. Mol. Biol. 3, 18-3 0 32. Penman, S. (1966). RNA metabolism in the HeLa cell nucleus. J. Mol. Biol. 17, 117-130 33. LePecq, J. B. & Paoletti, C. (1967). A ¯uorescent complex between ethidium bromide and nucleic acids. Physical-chemical characterization. J. Mol. Biol. 27, 87-106 34. Wetmur, J. G. & Davidson, N. (1968). Kinetics of renaturation of DNA. J. Mol. Biol. 31, 349-370 35. Sanger, F., Brownlee, G. G. & Barrell, B. G. (1965). A two-dimensional fractionation procedure for radioactive nucleotides. J. Mol. Biol. 13, 373-398 36. McGhee, J. D. & von Hippel, P. H. (1974). Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to
The 100 Most-Cited Articles from JMB
37.
38. 39.
40.
41.
42.
43. 44.
45. 46.
47.
48. 49.
50.
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a one-dimensional homogeneous lattice. J. Mol. Biol. 86, 469-489 Bangham, A. D., Standish, M. M. & Watkins, J. C. (1965). Diffusion of univalent ions across the lamellae of swollen phospholipids. J. Mol. Biol. 13, 238252 von Heijne, G. (1985). Signal sequences. The limits of variation. J. Mol. Biol. 184, 99-105 Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E. & Downing, K. H. (1990). Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 184, 899-929 Deisenhofer, J., Epp, O., Miki, K., Huber, R. & Michel, H. (1984). X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 180, 385-398 Pardee, A. B., Jacob, F. & Monod, J. (1959). The genetic control and cytoplasmic expression of ``Inductibility'' in the Synthesis of b-galactosidase by E. Coli. J. Mol. Biol. 1, 165-178 Casadaban, M. J. (1976). Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J. Mol. Biol. 104, 541-555 Crick, F. H. (1966). Codon ± anticodon pairing: the wobble hypothesis. J. Mol. Biol. 19, 548-555 Lowey, S., Slayter, H. S., Weeds, A. G. & Baker, H. (1969). Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation. J. Mol. Biol. 42, 1-29 King, J. & Laemmli, U. K. (1971). Polypeptides of the tail ®bres of bacteriophage T4. J. Mol. Biol. 62, 465-477 Eisenberg, D., Schwarz, E., Komaromy, M. & Wall, R. (1984). Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179, 125-142 Rupp, W. D. & Howard-Flanders, P. (1968). Discontinuities in the DNA synthesized in an excisiondefective strain of Escherichia coli following ultraviolet irradiation. J. Mol. Biol. 31, 291-304 Thomas, M. & Davis, R. W. (1975). Studies on the cleavage of bacteriophage lambda DNA with EcoRI Restriction endonuclease. J. Mol. Biol. 91, 315-328 Perlman, D. & Halvorson, H. O. (1983). A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J. Mol. Biol. 167, 391-409 Pohl, F. M. & Jovin, T. M. (1972). Salt-induced cooperative conformational change of a synthetic DNA: equilibrium and kinetic studies with poly (dG-dC). J. Mol. Biol. 67, 375-396 Bishop, D. H. L., Claybrook, J. R. & Spiegelman, S. (1967). Electrophoretic separation of viral nucleic acids on polyacrylamide gels. J. Mol. Biol. 26, 373387 Anderson, S., de Bruijn, M. H., Coulson, A. R., Eperon, I. C., Sanger, F. & Young, I. G. (1982). Complete sequence of bovine mitochondrial DNA. Conserved features of the mammalian mitochondrial genome. J. Mol. Biol. 156, 683-717 Tardieu, A., Luzzati, V. & Reman, F. C. (1973). Structure and polymorphism of the hydrocarbon chains of lipids: a study of lecithin-water phases. J. Mol. Biol. 75, 711-733
The 100 Most-Cited Articles from JMB 54. TissieÁres, A., Watson, J. D., Schlessinger, D. & Hollingworth, B. R. (1959). Ribonucleoprotein Particles from Escherichia coli. J. Mol. Biol. 1, 221-233 55. Huxley, H. E. & Brown, W. (1967). The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J. Mol. Biol. 30, 383-434 56. Stryer, L. (1965). The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A ¯uorescent probe of non-polar binding sites. J. Mol. Biol. 13, 482-495 57. Unwin, P. N. & Henderson, R. (1975). Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 94, 425440 58. Sanger, F., Coulson, A. R., Hong, G. F., Hill, D. F. & Petersen, G. B. (1982). Nucleotide sequence of bacteriophage lambda DNA. J. Mol. Biol. 162, 729773 59. Muller, W. & Crothers, D. M. (1968). Studies of the binding of actinomycin and related compounds to DNA. J. Mol. Biol. 35, 251-290 60. Chou, P. Y. & Fasman, G. D. (1977). Beta-turns in proteins. J. Mol. Biol. 115, 135-75 61. Huberman, J. A. & Riggs, A. D. (1968). On the mechanism of DNA replication in mammalian chromosomes.J. Mol. Biol. 32, 327-341 62. Waring, M. (1970). Variation of the supercoils in closed circular DNA by binding of antibiotics and drugs: evidence for molecular models involving intercalation. J. Mol. Biol. 54, 247-279 63. Dunn, J. J. & Studier, F. W. (1983). Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements. J. Mol. Biol. 166, 477-535 64. Privalov, P. L. & Khechinashvili, N. N. (1974). A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 86, 665-684 65. Sanger, F. & Coulson, A. R. (1975). A rapid method for determining sequences in DNA by primed synthesis with DNA polymerase. J. Mol. Biol. 94, 441448 66. Marushige, K. & Bonner, J. (1966). Template properties of liver chromatin. J. Mol. Biol. 15, 160-174 67. Gaskin, F., Cantor, C. R. & Shelanski, M. L. (1974). Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules. J. Mol. Biol. 89, 737-755. 68. Cairns, J. (1963). The bacterial chromosome and its manner of replication as seen by autoradiography. J. Mol. Biol. 6, 208-213 69. Birktoft, J. J. & Blow, D. M. (1972). Structure of crystalline -chymotrypsin. V. The atomic structure of tosyl-chymotrypsin at 2 A resolution. J. Mol. Biol. 68, 187-240 70. Zubay, G. (1962). The isolation and fractionation of soluble ribonucleic acid. J. Mol. Biol. 4, 347-356 71. Shinitzky, M. & Inbar, M. (1974). Difference in microviscosity induced by different cholesterol levels in the surface membrane lipid layer of normal lymphocytes and malignant lymphoma cells. J. Mol. Biol. 85, 603-615 72. Riggs, A. D., Suzuki, H. & Bourgeoss, S. (1970). Lac repressor-operator interaction. I. Equilibrium studies. J. Mol. Biol. 48, 67-83 73. Dickerson, R. E. & Drew, H. R. (1981). Structure of a B-DNA dodecamer. II. In¯uence of base sequence on helix structure. J. Mol. Biol. 149, 761-786
175 74. Loening, U. E. (1968). Molecular weights of ribosomal RNA in relation to evolution. J. Mol. Biol. 38, 355-365 75. Rousseau, G. G., Baxter, J. D. & Tomkins, G. M. (1972). Glucocorticoid receptors: relations between steroid binding and biological effects. J. Mol. Biol. 67, 99-115 76. Zubay, G. & Doty, P. (1959). The isolation and properties of deoxyribonucleoprotein particles containing single nucleic acid molecules. J. Mol. Biol. 1, 1-20 77. Eigner, J.& Doty, P. (1965). The native, denatured and renatured states of deoxyribonucleic acid. J. Mol. Biol. 12, 549-580 78. Paul, J. & Gilmour, R. S. (1968). Organ-speci®c restriction of transcription in mammalian chromatin. J. Mol. Biol. 34, 305-316 79. Maaloe, O. & Hanawalt, C. (1961). Thymine de®ciency and the normal DNA replication cycle. I. J. Mol. Biol. 3, 144-155 80. Cooper, S. & Helmstetter, C. E. (1968). Chromosome replication and the division cycle of Escherichia coli B/r. J. Mol. Biol. 31, 519-540 81. Takano, T. (1977). Structure of myoglobin re®ned at 2-0 A resolution. I. Crystallographic re®nement of metmyoglobin from sperm whale. J. Mol. Biol. 110, 537-568 82. Brosius, J., Dull, T. J., Sleeter, D. D. & Noller, H. F. (1981). Gene organization and primary structure of a ribosomal RNA operon from Escherichia coli. J. Mol. Biol. 148, 107-127 83. Weeds, A. G. & Pope, B. (1977). Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111, 129-157 84. Lathe, R. (1985). Synthetic oligonucleotide probes deduced from amino acid sequence data. Theoretical and practical considerations. J. Mol. Biol. 183, 1-12 85. Waring, M. J. (1965). Complex formation between ethidium bromide and nucleic acids. J. Mol. Biol. 13, 269-282 86. Sinsheimer, R. L. (1959). A single-stranded deoxyribonucleic acid from bacteriophage éX174. J. Mol. Biol. 1, 43-54 87. Noll, M. & Kornberg, R. D. (1977). Action of micrococcal nuclease on chromatin and the location of histone H1. J. Mol. Biol. 109, 393-404 88. Penman, S., Vesco, C. & Penman, M. (1968). Localization and kinetics of formation of nuclear heterodisperse RNA, cytoplasmic heterodisperse RNA and polyribosome-associated messenger RNA in HeLa cells. J. Mol. Biol. 34, 49-60 89. Wood, W. B. (1966). Host speci®city of DNA produced by Escherichia coli: bacterial mutations affecting the restriction and modi®cation of DNA. J. Mol. Biol. 16, 118-133 90. Smith, H. O. & Wilcox, K. W. (1970). A restriction enzyme from Hemophilus in¯uenzae. I. Puri®cation and general properties. J. Mol. Biol. 51, 379-391 91. Bauer, W. & Vinograd, J. (1968). The interaction of closed circular DNA with intercalative dyes. I. The superhelix density of SV40 DNA in the presence and absence of dye. J. Mol. Biol. 33, 141-171 92. Kurland, C. G. (1960). Molecular characterization of ribonucleic acid from Escherichia coli ribosomes. J. Mol. Biol. 2, 83-91 93. Eklund, H., Nordstrom, B., Zeppezauer, E., Soderlund, G., Ohlsson, I., Boiwe, T., Soderberg, B. O., Tapia, O., Branden, C. I. & Akeson, A., (1976).
176 Three-dimensional structure of horse liver alcohol dehydrogenase at 2-4 A resolution. J. Mol. Biol. 1, 27-59 94. Sueko, N., Cheng, T.-Y. (1962). Fractionation of nucleic acids with the methylated albumin column. J. Mol. Biol. 4, 161-172 95. Hanson, J. & Lowy, J. (1963). The structure of F-actin and of actin ®laments isolated from muscle. J. Mol. Biol. 6, 46-60 96. Franke, W. W., Schiller, D. L., Moll, R., Winter, S., Schmid, E., Engelbrecht, I., Denk, H., Krepler, R. & Platzer, B. (1981). Diversity of cytokeratins. Differentiation speci®c expression of cytokeratin polypeptides in epithelial cells and tissues. J. Mol. Biol. 4, 933-959
The 100 Most-Cited Articles from JMB 97. Steck, T. L. (1972). Cross-linking the major proteins of the isolated erythrocyte membrane. J. Mol. Biol. 2, 295-305 98. Ponder, J. W. & Richards, F. M. (1987). Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 4, 775-791 99. Perutz, M. F., Kendrew, J. C. & Watson, H. C. (1965). Structure and function of haemoglobin. J. Mol. Biol. 13, 669-678 100. MuÈller, A., KoÈhnlein, W. & Zimmer, G. (1963). Stereochemistry of polypeptide chain con®gerations. J. Mol. Biol. 7, 95-99
J. Mol. Biol. (1999) 293, 173±176
The 100 Most-Cited Articles from JMB Tessa Picknett1* and Kate Davis2 1
Academic Press, 24-28 Oval Road London, NW1 7DX, UK 2
Academic Press, 24-28 Oval Road, London, NW1 7DX, UK
Over the last 40 years, JMB has published many thousands of articles, all of which have been important in some way. Compiling a list of the `most important' however, is an invidious task. Friendships can falter on such an undertaking, but the Institute of Scienti®c Information has provided us with an objective methodology for `ranking' articles, according to the number of times any paper is cited in other publications. This evaluation can of course be criticised for its bias towards papers describing novel techniques or methods. Often, the true intellectual milestones may be found in the reference list of the most cited papers. With increasing age, each paper also has more time in which to have been cited, and so the group of highest scoring articles is also dominated by some of the oldest. On the other hand, with increasing time, papers have an increasing chance of being forgotten, and the citation rates of these are therefore also a measure of their persisting importance. On balance, it does represent a value in some way related to how often that paper has been used. With many caveats, we present the list of the 100 most cited papers in JMB over the past 40 years. Many of these papers have helped or in¯uenced both a great many people, and a great many subsequent advances in molecular biology. # 1999 Academic Press
*Corresponding author
1. Southern E. M.1975. Detection of speci®c sequences among DNA fragments separated by gel electrophoresi. J. Mol. Biol. 98, 503-517. 2. Rigby, P. W., Dieckmann, M., Rhodes, C. & Berg, P. (1977). Labeling deoxyribonucleic acid to high speci®c activity in vitro by nick translation with DNA polymerase I. J. Mol. Biol. 113, 237-251 3. Marmur, J. (1961). A procedure for the isolation of deoxyribonucleic acid from microorganisms. J. Mol. Biol. 3, 208-218. 4. Kyte, J. & Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132 5. Monod, J., Wyman, J. & Changeux, J.-P. (1965). On the Nature of Allosteric Transitions: A Plausible Model. J. Mol. Biol. 12, 88-118 6. Hanahan, D. (1983). Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166, 557580 7. Hirt, B. (1967). Selective extraction of polyoma DNA from infected mouse cell cultures. J. Mol. Biol. 26, 365-369 8. Sanger, F., Coulson, A. R., Barrell, B. G., Smith, A. J. & Roe, B. A. (1980). Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J. Mol. Biol. 143, 161-178 0022-2836/99/420173±4 $30.00/0
9. Bernstein, F. C., Koetzle, T. F., Williams, G. J., Meyer, E. E., Jr, Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T. & Tasumi, M. (1977). The Protein Data Bank: a computer-based archival ®le for macromolecular structures. J. Mol. Biol. 112, 535-542 10. Jacob, F. & Monod, J. (1961). Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 3, 318-356 11. Garnier, J., Osguthorpe, D. J. & Robson, B. (1978). Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97-120 12. Laemmli, U. K. & Favre, M. (1973). Maturation of the head of bacteriophage T4. I. DNA packaging events. J. Mol. Biol. 80, 575-599 13. Boyer, H. W. & Roulland-Dussoix, D. (1969). A complementation analysis of the restriction and modi®cation of DNA in Escherichia coli. J. Mol. Biol. 41, 459-472 14. Altschul, S. F., Gish, W., Miller, W., Myers, E. W. & Lipman, D. J. (1990). Basic local alignment search tool. J. Mol. Biol. 215, 403-410 15. Marmur, J. & Doty, P. (1962). Determination of the base composition of deoxyribonucleic acid from its thermal denaturation temperature. J. Mol. Biol. 5, 109-118 # 1999 Academic Press
174 16. Studier, F. W. (1965). Sedimentation Studies of the Size and Shape of DNA. J. Mol. Biol. 11, 373-390 17. Studier, F. W. (1973). Analysis of bacteriophage T7 early RNAs and proteins on slab gels. J. Mol. Biol. 2, 237-248. 18. Studier, F. W. & Moffatt, B. A. (1986). Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 79, 113-130 19. Gillespie, D. & Spiegelman, S. (1965). A quantitative assay for DNA-RNA hybrids with DNA immobilized on a membrane. J. Mol. Biol. 189, 829-842 20. Mandel, M. & Higa, A. (1970). Calcium-dependent bacteriophage DNA infection. J. Mol. Biol. 53, 159162 21. Matthews, B. W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497 22. Lee, B. & Richards, F. M. (1971). The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400 23. Schildkraut, C. L., Marmur, J. & Doty, P. (1962). Determination of the base composition of deoxyribonucleic acid from its buoyant density in CsC1. J. Mol. Biol. 4, 430-443 24. Clegg, J. B., Naughton, M. A. & Weatherball, D. J. (1966). Abnormal human haemoglobins. Separation and characterization of the alpha and beta chains by chromatography, and the determination of two new variants, hb Chesapeak and hb J (Bangkok). J. Mol. Biol. 19, 91-108 25. Needleman, S. B. & Wunsch, C. D. (1970). A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48, 443-453 26. Frischauf, A. M., Lehrach, H., Poustka, A. & Murray, N. (1983). Lambda replacement vectors carrying polylinker sequences. J. Mol. Biol. 170, 827-842 27. Huxley, H. E. (1963). Electron Microscope Studies on the Structure of Natural and Synthetic Protein Filaments from Striated Muscle. J. Mol. Biol. 7, 18-30 28. McDonell, M. W., Simon, M. N. & Studier, F. W. (1977). Analysis of restriction fragments of T7 DNA and determination of molecular weights by electrophoresis in neutral and alkaline gels. J. Mol. Biol. 110, 119-146 29. Casadaban, M. J. & Cohen, S. N. (1980). Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138, 179-207 30. Monod, J., Changeux, J.-P. & Jacob, F. (1963). Allosteric proteins and cellular control systems. J. Mol. Biol. 6, 306-329 31. Lerman, L. S. (1961). Structural considerations in the interaction of DNA and acridines. J. Mol. Biol. 3, 18-3 0 32. Penman, S. (1966). RNA metabolism in the HeLa cell nucleus. J. Mol. Biol. 17, 117-130 33. LePecq, J. B. & Paoletti, C. (1967). A ¯uorescent complex between ethidium bromide and nucleic acids. Physical-chemical characterization. J. Mol. Biol. 27, 87-106 34. Wetmur, J. G. & Davidson, N. (1968). Kinetics of renaturation of DNA. J. Mol. Biol. 31, 349-370 35. Sanger, F., Brownlee, G. G. & Barrell, B. G. (1965). A two-dimensional fractionation procedure for radioactive nucleotides. J. Mol. Biol. 13, 373-398 36. McGhee, J. D. & von Hippel, P. H. (1974). Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to
The 100 Most-Cited Articles from JMB
37.
38. 39.
40.
41.
42.
43. 44.
45. 46.
47.
48. 49.
50.
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52.
53.
a one-dimensional homogeneous lattice. J. Mol. Biol. 86, 469-489 Bangham, A. D., Standish, M. M. & Watkins, J. C. (1965). Diffusion of univalent ions across the lamellae of swollen phospholipids. J. Mol. Biol. 13, 238252 von Heijne, G. (1985). Signal sequences. The limits of variation. J. Mol. Biol. 184, 99-105 Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E. & Downing, K. H. (1990). Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 184, 899-929 Deisenhofer, J., Epp, O., Miki, K., Huber, R. & Michel, H. (1984). X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 180, 385-398 Pardee, A. B., Jacob, F. & Monod, J. (1959). The genetic control and cytoplasmic expression of ``Inductibility'' in the Synthesis of b-galactosidase by E. Coli. J. Mol. Biol. 1, 165-178 Casadaban, M. J. (1976). Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J. Mol. Biol. 104, 541-555 Crick, F. H. (1966). Codon ± anticodon pairing: the wobble hypothesis. J. Mol. Biol. 19, 548-555 Lowey, S., Slayter, H. S., Weeds, A. G. & Baker, H. (1969). Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation. J. Mol. Biol. 42, 1-29 King, J. & Laemmli, U. K. (1971). Polypeptides of the tail ®bres of bacteriophage T4. J. Mol. Biol. 62, 465-477 Eisenberg, D., Schwarz, E., Komaromy, M. & Wall, R. (1984). Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179, 125-142 Rupp, W. D. & Howard-Flanders, P. (1968). Discontinuities in the DNA synthesized in an excisiondefective strain of Escherichia coli following ultraviolet irradiation. J. Mol. Biol. 31, 291-304 Thomas, M. & Davis, R. W. (1975). Studies on the cleavage of bacteriophage lambda DNA with EcoRI Restriction endonuclease. J. Mol. Biol. 91, 315-328 Perlman, D. & Halvorson, H. O. (1983). A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J. Mol. Biol. 167, 391-409 Pohl, F. M. & Jovin, T. M. (1972). Salt-induced cooperative conformational change of a synthetic DNA: equilibrium and kinetic studies with poly (dG-dC). J. Mol. Biol. 67, 375-396 Bishop, D. H. L., Claybrook, J. R. & Spiegelman, S. (1967). Electrophoretic separation of viral nucleic acids on polyacrylamide gels. J. Mol. Biol. 26, 373387 Anderson, S., de Bruijn, M. H., Coulson, A. R., Eperon, I. C., Sanger, F. & Young, I. G. (1982). Complete sequence of bovine mitochondrial DNA. Conserved features of the mammalian mitochondrial genome. J. Mol. Biol. 156, 683-717 Tardieu, A., Luzzati, V. & Reman, F. C. (1973). Structure and polymorphism of the hydrocarbon chains of lipids: a study of lecithin-water phases. J. Mol. Biol. 75, 711-733
The 100 Most-Cited Articles from JMB 54. TissieÁres, A., Watson, J. D., Schlessinger, D. & Hollingworth, B. R. (1959). Ribonucleoprotein Particles from Escherichia coli. J. Mol. Biol. 1, 221-233 55. Huxley, H. E. & Brown, W. (1967). The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J. Mol. Biol. 30, 383-434 56. Stryer, L. (1965). The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A ¯uorescent probe of non-polar binding sites. J. Mol. Biol. 13, 482-495 57. Unwin, P. N. & Henderson, R. (1975). Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 94, 425440 58. Sanger, F., Coulson, A. R., Hong, G. F., Hill, D. F. & Petersen, G. B. (1982). Nucleotide sequence of bacteriophage lambda DNA. J. Mol. Biol. 162, 729773 59. Muller, W. & Crothers, D. M. (1968). Studies of the binding of actinomycin and related compounds to DNA. J. Mol. Biol. 35, 251-290 60. Chou, P. Y. & Fasman, G. D. (1977). Beta-turns in proteins. J. Mol. Biol. 115, 135-75 61. Huberman, J. A. & Riggs, A. D. (1968). On the mechanism of DNA replication in mammalian chromosomes.J. Mol. Biol. 32, 327-341 62. Waring, M. (1970). Variation of the supercoils in closed circular DNA by binding of antibiotics and drugs: evidence for molecular models involving intercalation. J. Mol. Biol. 54, 247-279 63. Dunn, J. J. & Studier, F. W. (1983). Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements. J. Mol. Biol. 166, 477-535 64. Privalov, P. L. & Khechinashvili, N. N. (1974). A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 86, 665-684 65. Sanger, F. & Coulson, A. R. (1975). A rapid method for determining sequences in DNA by primed synthesis with DNA polymerase. J. Mol. Biol. 94, 441448 66. Marushige, K. & Bonner, J. (1966). Template properties of liver chromatin. J. Mol. Biol. 15, 160-174 67. Gaskin, F., Cantor, C. R. & Shelanski, M. L. (1974). Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules. J. Mol. Biol. 89, 737-755. 68. Cairns, J. (1963). The bacterial chromosome and its manner of replication as seen by autoradiography. J. Mol. Biol. 6, 208-213 69. Birktoft, J. J. & Blow, D. M. (1972). Structure of crystalline -chymotrypsin. V. The atomic structure of tosyl-chymotrypsin at 2 A resolution. J. Mol. Biol. 68, 187-240 70. Zubay, G. (1962). The isolation and fractionation of soluble ribonucleic acid. J. Mol. Biol. 4, 347-356 71. Shinitzky, M. & Inbar, M. (1974). Difference in microviscosity induced by different cholesterol levels in the surface membrane lipid layer of normal lymphocytes and malignant lymphoma cells. J. Mol. Biol. 85, 603-615 72. Riggs, A. D., Suzuki, H. & Bourgeoss, S. (1970). Lac repressor-operator interaction. I. Equilibrium studies. J. Mol. Biol. 48, 67-83 73. Dickerson, R. E. & Drew, H. R. (1981). Structure of a B-DNA dodecamer. II. In¯uence of base sequence on helix structure. J. Mol. Biol. 149, 761-786
175 74. Loening, U. E. (1968). Molecular weights of ribosomal RNA in relation to evolution. J. Mol. Biol. 38, 355-365 75. Rousseau, G. G., Baxter, J. D. & Tomkins, G. M. (1972). Glucocorticoid receptors: relations between steroid binding and biological effects. J. Mol. Biol. 67, 99-115 76. Zubay, G. & Doty, P. (1959). The isolation and properties of deoxyribonucleoprotein particles containing single nucleic acid molecules. J. Mol. Biol. 1, 1-20 77. Eigner, J.& Doty, P. (1965). The native, denatured and renatured states of deoxyribonucleic acid. J. Mol. Biol. 12, 549-580 78. Paul, J. & Gilmour, R. S. (1968). Organ-speci®c restriction of transcription in mammalian chromatin. J. Mol. Biol. 34, 305-316 79. Maaloe, O. & Hanawalt, C. (1961). Thymine de®ciency and the normal DNA replication cycle. I. J. Mol. Biol. 3, 144-155 80. Cooper, S. & Helmstetter, C. E. (1968). Chromosome replication and the division cycle of Escherichia coli B/r. J. Mol. Biol. 31, 519-540 81. Takano, T. (1977). Structure of myoglobin re®ned at 2-0 A resolution. I. Crystallographic re®nement of metmyoglobin from sperm whale. J. Mol. Biol. 110, 537-568 82. Brosius, J., Dull, T. J., Sleeter, D. D. & Noller, H. F. (1981). Gene organization and primary structure of a ribosomal RNA operon from Escherichia coli. J. Mol. Biol. 148, 107-127 83. Weeds, A. G. & Pope, B. (1977). Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111, 129-157 84. Lathe, R. (1985). Synthetic oligonucleotide probes deduced from amino acid sequence data. Theoretical and practical considerations. J. Mol. Biol. 183, 1-12 85. Waring, M. J. (1965). Complex formation between ethidium bromide and nucleic acids. J. Mol. Biol. 13, 269-282 86. Sinsheimer, R. L. (1959). A single-stranded deoxyribonucleic acid from bacteriophage éX174. J. Mol. Biol. 1, 43-54 87. Noll, M. & Kornberg, R. D. (1977). Action of micrococcal nuclease on chromatin and the location of histone H1. J. Mol. Biol. 109, 393-404 88. Penman, S., Vesco, C. & Penman, M. (1968). Localization and kinetics of formation of nuclear heterodisperse RNA, cytoplasmic heterodisperse RNA and polyribosome-associated messenger RNA in HeLa cells. J. Mol. Biol. 34, 49-60 89. Wood, W. B. (1966). Host speci®city of DNA produced by Escherichia coli: bacterial mutations affecting the restriction and modi®cation of DNA. J. Mol. Biol. 16, 118-133 90. Smith, H. O. & Wilcox, K. W. (1970). A restriction enzyme from Hemophilus in¯uenzae. I. Puri®cation and general properties. J. Mol. Biol. 51, 379-391 91. Bauer, W. & Vinograd, J. (1968). The interaction of closed circular DNA with intercalative dyes. I. The superhelix density of SV40 DNA in the presence and absence of dye. J. Mol. Biol. 33, 141-171 92. Kurland, C. G. (1960). Molecular characterization of ribonucleic acid from Escherichia coli ribosomes. J. Mol. Biol. 2, 83-91 93. Eklund, H., Nordstrom, B., Zeppezauer, E., Soderlund, G., Ohlsson, I., Boiwe, T., Soderberg, B. O., Tapia, O., Branden, C. I. & Akeson, A., (1976).
176 Three-dimensional structure of horse liver alcohol dehydrogenase at 2-4 A resolution. J. Mol. Biol. 1, 27-59 94. Sueko, N., Cheng, T.-Y. (1962). Fractionation of nucleic acids with the methylated albumin column. J. Mol. Biol. 4, 161-172 95. Hanson, J. & Lowy, J. (1963). The structure of F-actin and of actin ®laments isolated from muscle. J. Mol. Biol. 6, 46-60 96. Franke, W. W., Schiller, D. L., Moll, R., Winter, S., Schmid, E., Engelbrecht, I., Denk, H., Krepler, R. & Platzer, B. (1981). Diversity of cytokeratins. Differentiation speci®c expression of cytokeratin polypeptides in epithelial cells and tissues. J. Mol. Biol. 4, 933-959
The 100 Most-Cited Articles from JMB 97. Steck, T. L. (1972). Cross-linking the major proteins of the isolated erythrocyte membrane. J. Mol. Biol. 2, 295-305 98. Ponder, J. W. & Richards, F. M. (1987). Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 4, 775-791 99. Perutz, M. F., Kendrew, J. C. & Watson, H. C. (1965). Structure and function of haemoglobin. J. Mol. Biol. 13, 669-678 100. MuÈller, A., KoÈhnlein, W. & Zimmer, G. (1963). Stereochemistry of polypeptide chain con®gerations. J. Mol. Biol. 7, 95-99