[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6383359 [NCBI, ExPASy, EBI, Israel, Japan]
Wood D.,
Darlison M.G.,
Wilde R.J.,
Guest J.R.;
"Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli.";
Biochem. J. 222:519-534(1984).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan]
Oshima T.,
Aiba H.,
Baba T.,
Fujita K.,
Hayashi K.,
Honjo A.,
Ikemoto K.,
Inada T.,
Itoh T.,
Kajihara M.,
Kanai K.,
Kashimoto K.,
Kimura S.,
Kitagawa M.,
Makino K.,
Masuda S.,
Miki T.,
Mizobuchi K.,
Mori H.,
Motomura K.,
Nakamura Y.,
Nashimoto H.,
Nishio Y.,
Saito N.,
Sampei G.,
Seki Y.,
Tagami H.,
Takemoto K.,
Wada C.,
Yamamoto Y.,
Yano M.,
Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R.,
Plunkett G. III,
Bloch C.A.,
Perna N.T.,
Burland V.,
Riley M.,
Collado-Vides J.,
Glasner J.D.,
Rode C.K.,
Mayhew G.F.,
Gregor J.,
Davis N.W.,
Kirkpatrick H.A.,
Goeden M.A.,
Rose D.J.,
Mau B.,
Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K.,
Morooka N.,
Yamamoto Y.,
Fujita K.,
Isono K.,
Choi S.,
Ohtsubo E.,
Baba T.,
Wanner B.L.,
Mori H.,
Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
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[5]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 578-588.
STRAIN=K12;
PubMed=6388571 [NCBI, ExPASy, EBI, Israel, Japan]
Darlison M.G.,
Guest J.R.;
"Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli.";
Biochem. J. 223:507-517(1984).
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[6]
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PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J.,
Robison K.,
Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
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[7]
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PROTEIN SEQUENCE OF 1-4.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1006/jmbi.1998.1726; PubMed=9600841 [NCBI, ExPASy, EBI, Israel, Japan]
Wilkins M.R.,
Gasteiger E.,
Tonella L.,
Ou K.,
Tyler M.,
Sanchez J.-C.,
Gooley A.A.,
Walsh B.J.,
Bairoch A.,
Appel R.D.,
Williams K.L.,
Hochstrasser D.F.;
"Protein identification with N and C-terminal sequence tags in proteome projects.";
J. Mol. Biol. 278:599-608(1998).
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[8]
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SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BL21-DE3;
DOI=10.1074/jbc.M506479200; PubMed=16079137 [NCBI, ExPASy, EBI, Israel, Japan]
Stenberg F.,
Chovanec P.,
Maslen S.L.,
Robinson C.V.,
Ilag L.,
von Heijne G.,
Daley D.O.;
"Protein complexes of the Escherichia coli cell envelope.";
J. Biol. Chem. 280:34409-34419(2005).
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[9]
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ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M800187-MCP200; PubMed=18723842 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J.,
Sprung R.,
Pei J.,
Tan X.,
Kim S.,
Zhu H.,
Liu C.F.,
Grishin N.V.,
Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli.";
Mol. Cell. Proteomics 0:0-0(2008).
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[10]
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X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD AND OXALOACETATE, ENZYME REGULATION, SUBCELLULAR LOCATION, AND SUBUNIT.
DOI=10.1126/science.1079605; PubMed=12560550 [NCBI, ExPASy, EBI, Israel, Japan]
Yankovskaya V.,
Horsefield R.,
Toernroth S.,
Luna-Chavez C.,
Miyoshi H.,
Leger C.,
Byrne B.,
Cecchini G.,
Iwata S.;
"Architecture of succinate dehydrogenase and reactive oxygen species generation.";
Science 299:700-704(2003).
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[11]
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X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH FAD AND OXALOACETATE, AND SUBUNIT.
DOI=10.1074/jbc.M508173200; PubMed=16407191 [NCBI, ExPASy, EBI, Israel, Japan]
Horsefield R.,
Yankovskaya V.,
Sexton G.,
Whittingham W.,
Shiomi K.,
Omura S.,
Byrne B.,
Cecchini G.,
Iwata S.;
"Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction.";
J. Biol. Chem. 281:7309-7316(2006).
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