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Sanger, F. The early days of DNA sequences. Nat. Med. 3: 267–268 (2001).
Sanger, E, Dowding, M, eds., Selected Papers of Frederick Sanger. Singapore: World Scientific (1996).
Sanger, F, Nicklen, S, Coulson, AR. DNA sequencing with chain-terminating inhibitors. 1977. Biotechnology 24: 104–108 (1992).
Sanger, F. Sequences, sequences, and sequences. Ann. Rev. Biochem. 57: 1–28 (1988).
Daniels, DL, Sanger, F, Coulson, AR. Features of bacteriophage λ: analysis of the complete nucleotide sequence. Cold Spring Harb. Symp. Quant. Biol. 47: 1009–1024 (1983).
Sanger, F, Coulson, AR, Hong, GF, Hill, DF, Petersen, GB. Nucleotide sequence of bacteriophage λ DNA. J. Mol. Biol. 162: 729–773 (1982).
Anderson, S, de Bruijn, MH, Coulson, AR, Eperon, IC, Sanger, F, Young, IG. Complete sequence of bovine mitochondrial DNA: conserved features of the mammalian mitochondrial genome. J. Mol. Biol. 156: 683–717 (1982).
Anderson, S, Bankier, AT, Barrell, BG, de Bruijn, MHL, Coulson, AR, Drouin, J, Eperon, IC, Nierlich, DP, Roe, BA, Sanger, F, Schreier, PH, Smith, AJH, Staden, R, Young, IG. In Slonimski, PP, Borst, P, Attardi, G, eds., Mitochondrial Genes. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp. 5–43 (1982).
Sanger, F. Determination of nucleotide sequences in DNA. Science 214: 1205–1210 (1981).
Anderson, S, Bankier, AT, Barrell, BG, de Bruijn, MH, Coulson, AR, Drouin, J, Eperon, IC, Nierlich, DP, Roe, BA, Sanger, F, Schreier, PH, Smith, AJ, Staden, R, Young, IG. Sequence and organization of the human mitochondrial genome. Nature 290: 457–465 (1981).
Sanger, F. Determination of nucleotide sequences in DNA. Biosci. Rep. 1: 3–18 (1981).
Sanger, F. Nobel Lecture, 1980: Determination of nucleotide sequences in DNA. In Nobel Prizes, Chemistry 1970–1980. Singapore: World Scientific, pp. 431–447 (1993).
Sanger, F, Coulson, AR, Barrell, BG, Smith, AJ, Roe, BA. Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J. Mol. Biol. 143: 161–178 (1980).
Barrell, BG, Anderson, S, Bankier, AT, de Bruijn, MH, Chen, E, Coulson, AR, Drouin, J, Eperon, IC, Nierlich, DP, Roe, BA, Sanger, F, Schreier, PH, Smith, AJ, Staden, R, Young, IG. Different pattern of codon recognition by mammalian mitochondrial tRNAs. Proc. Natl Acad. Sci. USA 77: 3164–3166 (1980).
Air, GM, Coulson, AR, Fiddes, JC, Friedmann, T, Hutchison, CA, Sanger, F, Slocombe, PM, Smith, AJ. Nucleotide sequence of the F protein coding region of bacteriophage φX174 and the amino acid sequence of its product. J. Mol. Biol. 125: 247–254 (1978).
Sanger, F, Coulson, AR, Friedmann, T, Air, GM, Barrell, BG, Brown, NL, Fiddes, JC, Hutchison, CA, Slocombe, PM, Smith, M. The nucleotide sequence of bacteriophage φX174. J. Mol. Biol. 125: 225–246 (1978).
Sanger, F, Coulson, AR. The use of thin acrylamide gels for DNA sequencing. FEBS Lett. 87: 107–110 (1978).
Sanger, F, Nicklen, S, Coulson, AR. DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA 74: 5463–5467 (1977).
Sanger, F, Air, GM, Barrell, BG, Brown, NL, Coulson, AR, Fiddes, CA, Hutchison, CA, Slocombe, PM, Smith, M. Nucleotide sequence of bacteriophage φX174 DNA. Nature 265: 687–695 (1977).
Smith, M, Brown, NL, Air, GM, Barrell, BG, Coulson, AR, Hutchison, CA, Sanger, F. DNA sequence at the C termini of the overlapping genes A and B in bacteriophage φX174. Nature 265: 702–705 (1977).
Air, GM, Sanger, F, Coulson, AR. Nucleotide and amino acid sequences of gene G of φX174. J. Mol. Biol. 108: 519–533 (1976).
Air, GM, Blackburn, EH, Coulson, AR, Galibert, F, Sanger, F, Sedat, JW, Ziff, EB. Gene F of bacteriophage φX174: correlation of nucleotide sequences from the DNA and amino acid sequences from the gene product. J. Mol. Biol. 107: 445–458 (1976).
Sanger, F. The Croonian Lecture 1975: Nucleotide sequences in DNA. Proc. R. Soc. Lond. B 191: 317–333 (1975).
Air, GM, Blackburn, EH, Sanger, F, Coulson, AR. The nucleotide and amino acid sequence of the N (5′) terminal region of gene G of bacteriophage φX174. J. Mol. Biol. 96: 703–719 (1975).
Sanger, F, Coulson, AR. A rapid method for determining sequences in DNA by primed synthesis with DNA polymerase. J. Mol. Biol. 94: 441–448 (1975).
Sanger, F, Donelson, JE, Coulson, AR, Kössel, H, Fischer, D. Determination of a nucleotide sequence in bacteriophage f1 DNA by primed synthesis with DNA polymerase. J. Mol. Biol. 90: 315–333 (1974).
Sanger, F, Donelson, JE, Coulson, AR, Kössel, H, Fischer, D. Use of DNA polymerase I primed by a synthetic oligonucleotide to determine a nucleotide sequence in phage f1 DNA. Proc. Natl Acad. Sci. USA 70: 1209–1213 (1973).
Jeppesen, PGN, Barrell, BG, Sanger, F, Coulson, AR. Nucleotide sequences of two fragments from the coat-protein cistron of bacteriophage R17 ribonucleic acid. Biochem. J. 128: 993–1006 (1972).
Sanger, F. The eighth Hopkins Memorial Lecture: Nucleotide sequences in bacteriophage ribonucleic acid. Biochem. J. 124: 833–843 (1971).
Sanger, F, Brownlee, GG. Methods for determining sequences in RNA. Biochem. Soc. Symp. 30: 183–197 (1970).
Jeppesen, PJN, Nichols, JL, Sanger, F, Barrell, BJ. Nucleotide sequences from bacteriophage R17 RNA. Cold Spring Harb. Symp. Quant. Biol. 35: 13–19 (1970).
Brownlee, GG, Sanger, F. Chromatography of 32P-labelled oligonucleotides on thin layers of DEAE-cellulose. Eur. J. Biochem. 11: 395–399 (1969).
Adams, JM, Jeppesen, PG, Sanger, F, Barrell, BG. Nucleotide sequence from the coat protein cistron of R17 bacteriophage RNA. Nature 223: 1009–1014 (1969).
Labrie, F, Sanger, F. 32P-labelling of haemoglobin messenger and other reticulocyte ribonucleic acids with polynucleotide phosphokinase in vitro. Biochem. J. 114: 29P (1969).
Székely, M, Sanger, F. Use of polynucleotide kinase in fingerprinting non-radioactive nucleic acids. J. Mol. Biol. 43: 607–617 (1969).
Adams, JM, Jeppesen, PG, Sanger, F, Barrell, BG. Nucleotide sequences from fragments of R17 bacterophage RNA. Cold Spring Harb. Symp. Quant. Biol. 34: 611–620 (1969).
Barrell, BG, Sanger, F. The sequence of phenylalanine tRNA from E. coli. FEBS Lett. 3: 275–278 (1969).
Fellner, P, Sanger, F. Sequence analysis of specific areas of the 16S and 23S ribosomal RNAs. Nature 219: 236–238 (1968).
Brownlee, GG, Sanger, F, Barrell, BG. The sequence of 5S ribosomal ribonucleic acid. J. Mol. Biol. 34: 379–412 (1968).
Brownlee, GG, Sanger, F, Barrell, BG. Nucleotide sequence of 5S ribosomal RNA from Escherichia coli. Nature 215: 735–736 (1967).
Brownlee, GG, Sanger, F. Nucleotide sequences from the low molecular weight ribosomal RNA of Escherichia coli. J. Mol. Biol. 23: 337–353 (1967).
Sanger, F, Brownlee, GG. A two-dimensional fractionation method for radioactive nucleotides. In Grossman, L, Moldave, K, eds., Methods in Enzymology, vol. XII, Part A, New York: Academic Press, pp. 361–363 (1967).
Sanger, F, Brownlee, GG, Barrell, BG. A two-dimensional fractionation procedure for radioactive nucleotides. J. Mol. Biol. 13: 373–398 (1965).
Larner, J, Sanger, F. The amino acid sequence of the phosphorylation site of muscle uridine diphosphoglucose alpha-1,4-glucan α-4-glucosyl transferase. J. Mol. Biol. 11: 491–500 (1965).
Marcker, K, Sanger, F. N-formyl-methionyl-s-RNA. J. Mol. Biol. 8: 835–840 (1964).
Sanger, F, Bretscher, MS, Hocquard, EJ. A study of the products from a polynucleotide-directed cell-free protein synthesizing system. J. Mol. Biol. 8: 38–45 (1964).
Glazer, AN, Sanger, F. The iodination of chymotrypsinogen. Biochem. J. 90: 92–98 (1964).
Glazer, AN, Sanger, F. Effect of fatty acid on the iodination of bovine serum albumin. J. Mol. Biol. 7: 452–453 (1963).
Sanger, F, Thompson, EO. Halogenation of tyrosine during acid hydrolysis. Biochim. Biophys. Acta 71: 468–471 (1963).
Sanger, F, Hocquard, E. Formation of dephospho-ovalbumin as an intermediate in the biosynthesis of ovalbumin. Biochim. Biophys. Acta 62: 606–607 (1962).
Milstein, C, Sanger, F. An amino acid sequence in the active centre of phosphoglucomutase. Biochem. J. 79: 456–469 (1961).
Naughton, MA, Sanger, F. Purification and specificity of pancreatic elastase. Biochem. J. 78: 156–163 (1961).
Naughton, MA, Sanger, F, Hartley, BS, Shaw, DC. The amino acid sequence around the reactive serine residue of some proteolytic enzymes. Biochem. J. 77: 149–163 (1960).
Sanger, F, Shaw, DC. Amino-acid sequence about the reactive serine of a proteolytic enzyme from Bacillus subtilis. Nature 187: 872–873 (1960).
Sanger, F. Chemistry of insulin. Br. Med. Bull. 16: 183–188 (1960).
Milstein, C, Sanger, F. The amino acid sequence around the serine phosphate in phosphoglucomutase. Biochim. Biophys. Acta 42: 173–174 (1960).
Hartley, BS, Naughton, MA, Sanger, F. The amino acid sequence around the reactive serine of elastase. Biochim. Biophys. Acta 34: 243–244 (1959).
Sanger, F. Nobel Lecture, 1958: The chemistry of insulin. In Nobel Lectures, Chemistry 1942–1962. Amsterdam: Elsevier, pp. 134–146 (1964).
Sanger, F. Chemistry of insulin: determination of the structure of insulin opens the way to greater understanding of life processes. Science 129: 1340–1344 (1959).
Williams, J, Sanger, F. The grouping of serine phosphate residues in phosvitin and casein. Biochim. Biophys. Acta 33: 294–296 (1959).
Harris, JI, Naughton, MA, Sanger, F. Species differences in insulin. Arch. Biochem. Biophys. 65: 427–438 (1956).
Brown, H, Sanger, F, Kitai, R. The structure of pig and sheep insulins. Biochem. J. 60: 556–565 (1955).
Ryle, AP, Sanger, F, Smith, LF, Kitai, R. The disulphide bonds of insulin. Biochem. J. 60: 541–556 (1955).
Ryle, AP, Sanger, F. Disulphide interchange reactions. Biochem. J. 60: 535–540 (1955).
Sanger, F, Thompson, EO, Kitai, R. The amide groups of insulin. Biochem. J. 59: 509–518 (1955).
Sanger, F, Smith, LF, Kitai, R. The disulphide bridges of insulin. Biochem. J. 58: vi–vii (1954).
Ryle, AP, Sanger, F. Disulphide interchange reactions. Biochem. J. 58:v–vi (1954).
Sanger, F. A disulphide interchange reaction. Nature 171: 1025–1026 (1953).
Sanger, F, Thompson, EO. The amino-acid sequence in the glycyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates. Biochem. J. 53: 366–374 (1953).
Sanger, F, Thompson, EO. The amino-acid sequence in the glycyl chain of insulin. 1. The identification of lower peptides from partial hydrolysates. Biochem. J. 53: 353–366 (1953).
Sanger, F, Thompson, EO. The amino-acid sequence in the glycyl chain of insulin. Biochem. J. 52: iii (1952).
Sanger, F. The arrangement of amino acids in proteins. Adv. Protein Chem. 7: 1–67 (1952).
Sanger, F, Thompson, EO. The inversion of a dipeptide sequence during hydrolysis in dilute acid. Biochim. Biophys. Acta 9: 225–226 (1952).
Sanger, F, Tuppy, H. The amino-acid sequence in the phenylalanyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates. Biochem. J. 49: 481–490 (1951).
Sanger, F, Tuppy, H. The amino-acid sequence in the phenylalanyl chain of insulin. 1. The identification of lower peptides from partial hydrolysates. Biochem. J. 49: 463–481 (1951).
Bailey, K, Sanger, F. The chemistry of amino acids and proteins. Ann. Rev. Biochem. 20: 103–130 (1951).
Sanger, F. Some chemical investigations on the structure of insulin. Cold Spring Harb. Symp. Quant. Biol. 14: 153–160 (1950).
Sanger, F. The chemistry of insulin. Annu. Rep. Prog. Chem. 45: 283–292 (1949).
Sanger, F. Application of partition chromatography to the study of protein structure. Biochem. Soc. Symp. 3: 21 (1949).
Sanger, F. Species differences in insulins. Nature 164: 529 (1949).
Sanger, F. The terminal peptides of insulin. Biochem. J. 45: 563–574 (1949).
Sanger, F. Fractionation of oxidized insulin. Biochem. J. 44: 126–128 (1949).
Sanger, F. Some peptides from insulin. Nature 162: 49 (1948).
Porter, RR, Sanger, F. The free amino groups of haemoglobins. Biochem. J. 42: 287–294 (1948).
Tiselius, A, Sanger, F. Adsorption analysis of oxidized insulin. Nature 160: 433 (1947).
Sanger, F. Oxidation of insulin by performic acid. Nature 160: 295 (1947).
Sanger, F. The free amino group of gramicidin S. Biochem. J. 40: 261–262 (1946).
Sanger, F. The free amino groups of insulin. Biochem. J. 39: 507–515 (1945).
Neuberger, A, Sanger, F. The availability of ε-acetyl-d-lysine and ε-methyl-dl-lysine for growth. Biochem. J. 38: 125–129 (1944).
Neuberger, A, Sanger, F. The metabolism of lysine. Biochem. J. 38: 119–125 (1944).
Neuberger, A, Sanger, F. The availability of the acetyl derivatives of lysine for growth. Biochem. J. 37: 515–518 (1943).
Harris, HA, Neuberger, A, Sanger, F. Lysine deficiency in young rats. Biochem. J. 37: 508–513 (1943).
Sanger, F. The metabolism of the amino-acid lysine in the animal body. PhD thesis, Cambridge University (1943).
Neuberger, A, Sanger, F. The nitrogen of the potato. Biochem. J. 36: 662 (1942).