References
Gilbert W & Müller-Hill B (1966) Isolation of thelac repressor. Proc. Natl. Acad. Sci. U.S.A.56, 1891–1898.
Gilbert W & Müller-Hill B (1967), Thelac operator is DNA. Proc. Natl. Acad. Sci. U.S.A.58, 2415–2421.
Gilbert W & Maxam A (1973) The nucleotide sequence of thelac operator. Proc. Natl. Acad. Sci. U.S.A.70, 3581–3584.
Gilbert W, Maizels N & Maxam A (1975) Sequences of controlling regions of theE. coli lactose operator. Genetics79, 227.
Dickson RC, Abelson J, Barnes WM & Reznikoff WS (1975) Genetic regulation: the lac control region. Science187, 27–35.
Gilbert W, Maxam A & Mirzabekov A (1976) Contacts between thelac repressor and DNA revealed by methylation. InControl of Ribosome Synthesis, pp 139–148, Alfred Benzon Symposium 9, Munksgaard.
Maxam AM & Gilbert W (1977) A new method for sequencing DNA. Proc. Natl. Acad. Sci. U.S.A.74, 560–564.
Tonegawa S, Maxam AM, Tizard R, Bernard O & Gilbert W (1978) Sequence of a mouse germ-line gene for a variable region of an immunoglobulin light chain. Proc. Natl. Acad. Sci. U.S.A.75, 1485–1489.
Maxam AM & Gilbert W (1980) Sequencing end-labeled DNA with base-specific chemical cleavages. Methods in Enzymology65, 499–560.
Sanger F & Coulson AR (1978) The use of thin acrylamide gels for DNA sequencing. FEBS Lett.87, 107–110.
Farabaugh PJ (1978) Sequence of thelacI gene. Nature274, 765–769.
Beyreuther K, Adler K, Fanning E, Murray C, Klemm A & Geisler N (1975) Amino-acid sequence oflac repressor fromEscherichia coli. Eur. J. Biochem.59, 491–509.
Coulondre C, Miller JH, Farabaugh PJ & Gilbert W (1978) Molecular basis of base substitution hotspots inEscherichia coli. Nature274, 775–780.
Lindahl T, Ljungquist S, Siegert W, Nyberg B & Sperens B (1977) DNAN-glycosidases. J. Biol. Chem.252, 3286–3294.
Sutcliffe JG (1978) Nucleotide sequence of the ampicillin resistance gene ofEscherichia coli plasmid pBR322. Proc. Natl. Acad. Sci. U.S.A.75, 3737–3741.
Ambler RP & Scott GK (1978) Partial amino acid sequence of penicillinase coded byEscherichia coli plasmid R6K. Proc. Natl. Acad. Sci. U.S.A.75, 3732–3736.
Sutcliffe JG (1978) Complete nucleotide sequence of theEscherichia coli plasmid pBR322. cold Spring Harbor Symposia on Quantitative Biology43, 77–90.
For a review, see: Yanofsky C (1981) Attenuation in the control of expression of bacterial operons. Nature289, 751–758.
Tilghman SM, Tiemeier DC, Seidman JG, Peterlin BM, Sullivan M, Maizel JV & Leder P (1978) Intervening sequence of DNA identified in the structural portion of a mouse β-globin gene. Proc. Natl. Acad. Sci. U.S.A.75, 725–729.
Konkel DA, Tilghman SM & Leder P (1978) The sequence of the chromosomal mouse β-globin major gene: homologies in capping, splicing and poly(A) sites. Cell15, 1125–1132.
Brack S & Tonegawa S (1977) Variable and constant parts of the immunoglobulin light chain gene of a mouse myeloma cell are 1250 nontranslated bases apart. Proc. Natl. Acad. Sci. U.S.A.74, 5652–5656.
Breathnach R, Mandel JL & Chambon P (1977) Ovalbumin gene is split in chicken DNA. Nature270, 314–319.
Berget SM, Moore C & Sharp PA (1977) Spliced segments at the 5′ terminus of adenovirus 2 late mRNA. Proc. Natl. Acad. Sci. U.S.A.74, 3171–3175.
Chow LT, Gelinas RE, Broker TR & Roberts RJ (1977) An amazing sequence arrangement at the 5′ ends of adenovirus 2 messenger RNA. Cell12, 1–8.
Gilbert W (1978) Why genes in pieces? Nature271, 501.
Bernard O, Hozumi N & Tonegawa S (1978) Sequences of mouse immunoglobulin light chain genes before and after somatic changes. Cell15, 1133–1144.
Sakano H, Rogers JH, Hüppi K, Brack C, Traunecker A, Maki R, Wall R & Tonegawa S (1979) Domains and the hinge region of an immunoglobulin heavy chain are encoded in separate DNA segments. Nature277, 627–633.
Honjo T, Obata M, Yamawaki-Kataoka Y, Kataoka T, Kawakami T, Takahashi N & Mano Y (1979) Cloning and complete nucleotide sequence of mouse immunoglobin γ1 chain gene. Cell18, 559–568.
Stein JP, Catterall JF, Kristo P, Means AR & O'Malley BW (1980) Ovomucoid intervening sequences specify functional domains and generate protein polymorphism. Cell21, 681–687.
Yamado Y, Avvedimento VE, Mudryj M, Ohkubo H, Vogeli G, Irani M, Pastan I & de Crombrugghe B (1980) The collagen gene: evidence for its evolutionary assembly by amplification of a DNA segment containing an exon of 54 bp. Cell22, 887–892.
Doolittle WF (1978) Genes in pieces: were they ever together? Nature272, 581.
Lomedico P, Rosenthal N, Efstratiadis A, Gilbert W, Kolodner R & Tizard R (1979) The structure and evolution of the two nonlllalic rat preproinsulin genes. Cell18, 545–558.
Early P, Rogers J, Davis M, Calame K, Bond M, Wall R & Hood L (1980) Two mRNAs can be produced from a single immunoglobin μ gene by alternative RNA processing pathways. Cell20, 313–319.
Perler F, Efstratiadis A, Lomedico P, Gilbert W, Kolodner R & Dodgson J (1980) The evolution of genes: the chicken preproinsulin gene. Cell20, 555–566.
Jung A, Sippel AE, Grez M & Schütz G (1980) Exons encode functional and structural units of chicken lysozyme. Proc. natl. Acad. Sci. U.S.A.77, 5759–5763.
Craik CS, Buchman SR & Beychok S (1980) Characterization of globin domains: heme binding to the central exon product. Proc. Natl. Acad. Sci. U.S.A.77, 1384–1388.
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Gilbert, W. DNA sequencing and gene structure. Biosci Rep 1, 353–375 (1981). https://doi.org/10.1007/BF01116186
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DOI: https://doi.org/10.1007/BF01116186