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Appendix: Complete bibliography of Fred Sanger

Published online by Cambridge University Press:  05 November 2014

George G. Brownlee
Foreword by
Edwin Southern
George G. Brownlee
Affiliation:
University of Oxford
Edwin Southern
Affiliation:
University of Oxford
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Fred Sanger - Double Nobel Laureate
A Biography
 , pp. 171 - 178
Publisher: Cambridge University Press
Print publication year: 2014

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References

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Sanger, F. The early days of DNA sequences. Nat. Med. 3: 267–268 (2001).CrossRefGoogle Scholar
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Sanger, F, Nicklen, S, Coulson, AR. DNA sequencing with chain-terminating inhibitors. 1977. Biotechnology 24: 104–108 (1992).Google ScholarPubMed
Sanger, F. Sequences, sequences, and sequences. Ann. Rev. Biochem. 57: 1–28 (1988).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle ScholarPubMed
Sanger, F, Coulson, AR, Hong, GF, Hill, DF, Petersen, GB. Nucleotide sequence of bacteriophage λ DNA. J. Mol. Biol. 162: 729–773 (1982).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle ScholarPubMed
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).Google Scholar
Sanger, F. Determination of nucleotide sequences in DNA. Science 214: 1205–1210 (1981).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle ScholarPubMed
Sanger, F. Determination of nucleotide sequences in DNA. Biosci. Rep. 1: 3–18 (1981).CrossRefGoogle ScholarPubMed
Sanger, F. Nobel Lecture, 1980: Determination of nucleotide sequences in DNA. In Nobel Prizes, Chemistry 1970–1980. Singapore: World Scientific, pp. 431–447 (1993).Google Scholar
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).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle Scholar
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).CrossRefGoogle ScholarPubMed
Sanger, F, Coulson, AR. The use of thin acrylamide gels for DNA sequencing. FEBS Lett. 87: 107–110 (1978).Google ScholarPubMed
Sanger, F, Nicklen, S, Coulson, AR. DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA 74: 5463–5467 (1977).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle Scholar
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).CrossRefGoogle Scholar
Air, GM, Sanger, F, Coulson, AR. Nucleotide and amino acid sequences of gene G of φX174. J. Mol. Biol. 108: 519–533 (1976).CrossRefGoogle Scholar
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).CrossRefGoogle ScholarPubMed
Sanger, F. The Croonian Lecture 1975: Nucleotide sequences in DNA. Proc. R. Soc. Lond. B 191: 317–333 (1975).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle Scholar
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).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle Scholar
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).CrossRefGoogle ScholarPubMed
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Sanger, F, Brownlee, GG. Methods for determining sequences in RNA. Biochem. Soc. Symp. 30: 183–197 (1970).Google ScholarPubMed
Jeppesen, PJN, Nichols, JL, Sanger, F, Barrell, BJ. Nucleotide sequences from bacteriophage R17 RNA. Cold Spring Harb. Symp. Quant. Biol. 35: 13–19 (1970).CrossRefGoogle Scholar
Brownlee, GG, Sanger, F. Chromatography of 32P-labelled oligonucleotides on thin layers of DEAE-cellulose. Eur. J. Biochem. 11: 395–399 (1969).CrossRefGoogle ScholarPubMed
Adams, JM, Jeppesen, PG, Sanger, F, Barrell, BG. Nucleotide sequence from the coat protein cistron of R17 bacteriophage RNA. Nature 223: 1009–1014 (1969).CrossRefGoogle ScholarPubMed
Labrie, F, Sanger, F. 32P-labelling of haemoglobin messenger and other reticulocyte ribonucleic acids with polynucleotide phosphokinase in vitro. Biochem. J. 114: 29P (1969).CrossRefGoogle Scholar
Székely, M, Sanger, F. Use of polynucleotide kinase in fingerprinting non-radioactive nucleic acids. J. Mol. Biol. 43: 607–617 (1969).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle ScholarPubMed
Barrell, BG, Sanger, F. The sequence of phenylalanine tRNA from E. coli. FEBS Lett. 3: 275–278 (1969).CrossRefGoogle ScholarPubMed
Fellner, P, Sanger, F. Sequence analysis of specific areas of the 16S and 23S ribosomal RNAs. Nature 219: 236–238 (1968).CrossRefGoogle ScholarPubMed
Brownlee, GG, Sanger, F, Barrell, BG. The sequence of 5S ribosomal ribonucleic acid. J. Mol. Biol. 34: 379–412 (1968).CrossRefGoogle Scholar
Brownlee, GG, Sanger, F, Barrell, BG. Nucleotide sequence of 5S ribosomal RNA from Escherichia coli. Nature 215: 735–736 (1967).CrossRefGoogle ScholarPubMed
Brownlee, GG, Sanger, F. Nucleotide sequences from the low molecular weight ribosomal RNA of Escherichia coli. J. Mol. Biol. 23: 337–353 (1967).CrossRefGoogle ScholarPubMed
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).Google Scholar
Sanger, F, Brownlee, GG, Barrell, BG. A two-dimensional fractionation procedure for radioactive nucleotides. J. Mol. Biol. 13: 373–398 (1965).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle ScholarPubMed
Marcker, K, Sanger, F. N-formyl-methionyl-s-RNA. J. Mol. Biol. 8: 835–840 (1964).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle ScholarPubMed
Glazer, AN, Sanger, F. The iodination of chymotrypsinogen. Biochem. J. 90: 92–98 (1964).CrossRefGoogle ScholarPubMed
Glazer, AN, Sanger, F. Effect of fatty acid on the iodination of bovine serum albumin. J. Mol. Biol. 7: 452–453 (1963).CrossRefGoogle ScholarPubMed
Sanger, F, Thompson, EO. Halogenation of tyrosine during acid hydrolysis. Biochim. Biophys. Acta 71: 468–471 (1963).CrossRefGoogle ScholarPubMed
Sanger, F, Hocquard, E. Formation of dephospho-ovalbumin as an intermediate in the biosynthesis of ovalbumin. Biochim. Biophys. Acta 62: 606–607 (1962).CrossRefGoogle ScholarPubMed
Milstein, C, Sanger, F. An amino acid sequence in the active centre of phosphoglucomutase. Biochem. J. 79: 456–469 (1961).CrossRefGoogle ScholarPubMed
Naughton, MA, Sanger, F. Purification and specificity of pancreatic elastase. Biochem. J. 78: 156–163 (1961).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle ScholarPubMed
Sanger, F, Shaw, DC. Amino-acid sequence about the reactive serine of a proteolytic enzyme from Bacillus subtilis. Nature 187: 872–873 (1960).CrossRefGoogle ScholarPubMed
Sanger, F. Chemistry of insulin. Br. Med. Bull. 16: 183–188 (1960).CrossRefGoogle ScholarPubMed
Milstein, C, Sanger, F. The amino acid sequence around the serine phosphate in phosphoglucomutase. Biochim. Biophys. Acta 42: 173–174 (1960).CrossRefGoogle ScholarPubMed
Hartley, BS, Naughton, MA, Sanger, F. The amino acid sequence around the reactive serine of elastase. Biochim. Biophys. Acta 34: 243–244 (1959).CrossRefGoogle ScholarPubMed
Sanger, F. Nobel Lecture, 1958: The chemistry of insulin. In Nobel Lectures, Chemistry 1942–1962. Amsterdam: Elsevier, pp. 134–146 (1964).Google Scholar
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).CrossRefGoogle ScholarPubMed
Williams, J, Sanger, F. The grouping of serine phosphate residues in phosvitin and casein. Biochim. Biophys. Acta 33: 294–296 (1959).CrossRefGoogle ScholarPubMed
Harris, JI, Naughton, MA, Sanger, F. Species differences in insulin. Arch. Biochem. Biophys. 65: 427–438 (1956).CrossRefGoogle ScholarPubMed
Brown, H, Sanger, F, Kitai, R. The structure of pig and sheep insulins. Biochem. J. 60: 556–565 (1955).CrossRefGoogle ScholarPubMed
Ryle, AP, Sanger, F, Smith, LF, Kitai, R. The disulphide bonds of insulin. Biochem. J. 60: 541–556 (1955).CrossRefGoogle ScholarPubMed
Ryle, AP, Sanger, F. Disulphide interchange reactions. Biochem. J. 60: 535–540 (1955).CrossRefGoogle ScholarPubMed
Sanger, F, Thompson, EO, Kitai, R. The amide groups of insulin. Biochem. J. 59: 509–518 (1955).CrossRefGoogle ScholarPubMed
Sanger, F, Smith, LF, Kitai, R. The disulphide bridges of insulin. Biochem. J. 58: vi–vii (1954).Google ScholarPubMed
Ryle, AP, Sanger, F. Disulphide interchange reactions. Biochem. J. 58:v–vi (1954).Google ScholarPubMed
Sanger, F. A disulphide interchange reaction. Nature 171: 1025–1026 (1953).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle Scholar
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).CrossRefGoogle Scholar
Sanger, F, Thompson, EO. The amino-acid sequence in the glycyl chain of insulin. Biochem. J. 52: iii (1952).Google ScholarPubMed
Sanger, F. The arrangement of amino acids in proteins. Adv. Protein Chem. 7: 1–67 (1952).CrossRefGoogle ScholarPubMed
Sanger, F, Thompson, EO. The inversion of a dipeptide sequence during hydrolysis in dilute acid. Biochim. Biophys. Acta 9: 225–226 (1952).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle ScholarPubMed
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).CrossRefGoogle Scholar
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Sanger, F. Some chemical investigations on the structure of insulin. Cold Spring Harb. Symp. Quant. Biol. 14: 153–160 (1950).CrossRefGoogle ScholarPubMed
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Sanger, F. The terminal peptides of insulin. Biochem. J. 45: 563–574 (1949).CrossRefGoogle ScholarPubMed
Sanger, F. Fractionation of oxidized insulin. Biochem. J. 44: 126–128 (1949).CrossRefGoogle ScholarPubMed
Sanger, F. Some peptides from insulin. Nature 162: 49 (1948).CrossRefGoogle ScholarPubMed
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Tiselius, A, Sanger, F. Adsorption analysis of oxidized insulin. Nature 160: 433 (1947).CrossRefGoogle ScholarPubMed
Sanger, F. Oxidation of insulin by performic acid. Nature 160: 295 (1947).CrossRefGoogle ScholarPubMed
Sanger, F. The free amino group of gramicidin S. Biochem. J. 40: 261–262 (1946).CrossRefGoogle ScholarPubMed
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Neuberger, A, Sanger, F. The availability of ε-acetyl-d-lysine and ε-methyl-dl-lysine for growth. Biochem. J. 38: 125–129 (1944).CrossRefGoogle ScholarPubMed
Neuberger, A, Sanger, F. The metabolism of lysine. Biochem. J. 38: 119–125 (1944).CrossRefGoogle Scholar
Neuberger, A, Sanger, F. The availability of the acetyl derivatives of lysine for growth. Biochem. J. 37: 515–518 (1943).CrossRefGoogle ScholarPubMed
Harris, HA, Neuberger, A, Sanger, F. Lysine deficiency in young rats. Biochem. J. 37: 508–513 (1943).CrossRefGoogle ScholarPubMed
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Neuberger, A, Sanger, F. The nitrogen of the potato. Biochem. J. 36: 662 (1942).CrossRefGoogle ScholarPubMed
Smith, AJ. The use of exonuclease III for preparing single stranded DNA for use as a template in the chain terminator sequencing method. Nucl. Acids Res. 6: 831–848 (1979).CrossRefGoogle ScholarPubMed
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