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1 to 11 of 11  Show
  1. 1
    "Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene."
    Hamilton W.D.O., Harrison D.A., Dyer T.A.
    Nucleic Acids Res. 16:8707-8707(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 other entries.

  2. 2
    "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 311 other entries.

  3. 3
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4394 other entries.

  4. 4
    "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4273 other entries.

  5. 5
    "Amino acid sequence homology among fructose-1,6-bisphosphatases."
    Marcus F., Gontero B., Harrsch P.B., Rittenhouse J.
    Biochem. Biophys. Res. Commun. 135:374-381(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 43-62; 220-229; 239-249; 254-269 AND 297-308.
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  6. 6
    "Fructose bisphosphatase of Escherichia coli: cloning of the structural gene (fbp) and preparation of a chromosomal deletion."
    Sedivy J.M., Daldal F., Fraenkel D.G.
    J. Bacteriol. 158:1048-1053(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
    Category: Function.
    Strain: K12.
    Source: UniProtKB/Swiss-Prot (reviewed).
  7. 7
    "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 299 other entries.

  8. 8
    "Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase."
    Hines J.K., Fromm H.J., Honzatko R.B.
    J. Biol. Chem. 281:18386-18393(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SULFATE IONS, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
    Category: Function, Interaction, Structure, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  9. 9
    "Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state."
    Hines J.K., Fromm H.J., Honzatko R.B.
    J. Biol. Chem. 282:11696-11704(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEXES WITH FRUCTOSE-6-PHOSPHATE; CITRATE AND PHOSPHOENOLPYRUVATE, ACTIVITY REGULATION, SUBUNIT.
    Category: Function, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  10. 10
    "Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch."
    Hines J.K., Kruesel C.E., Fromm H.J., Honzatko R.B.
    J. Biol. Chem. 282:24697-24706(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-1,6-BIPHOSPHATE; MAGNESIUM IONS; AMP AND GLUCOSE-6-PHOSPHATE, SUBUNIT, COFACTOR, ACTIVITY REGULATION.
    Category: Function, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  11. 11
    "Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition."
    Hines J.K., Chen X., Nix J.C., Fromm H.J., Honzatko R.B.
    J. Biol. Chem. 282:36121-36131(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-2,6-BIPHOSPHATE; MAGNESIUM IONS AND CITRATE, ACTIVITY REGULATION.
    Category: Function, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

1 to 11 of 11  Show
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