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1 to 25 of 25  Show
  1. 1
    "The complete nucleotide sequence for rabbit muscle aldolase A messenger RNA."
    Tolan D.R., Amsden A.B., Putney S.D., Urdea M.S., Penhoet E.E.
    J. Biol. Chem. 259:1127-1131(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  2. 2
    "The amino acid sequence of rabbit muscle aldolase."
    Sajgo M., Hajos G.
    Acta Biochim. Biophys. Acad. Sci. Hung. 9:239-241(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-364.
    Category: Sequences.
    Tissue: Muscle.
    Source: UniProtKB/Swiss-Prot (reviewed).
  3. 3
    "Amino acid sequence of rabbit muscle aldolase and the structure of the active center."
    Lai C.-Y., Nakai N., Chang D.
    Science 183:1204-1206(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-364.
    Category: Sequences.
    Tissue: Muscle.
    Source: UniProtKB/Swiss-Prot (reviewed).
  4. 4
    "Studies on the structure of rabbit muscle aldolase. Ordering of the tryptic peptides; sequence of 164 amino acid residues in the NH2-terminal BrCN peptide."
    Nakai N., Chang D., Lai C.-Y.
    Arch. Biochem. Biophys. 166:347-357(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-165.
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  5. 5
    "Extended amino acid sequences around the active-site lysine residue of class-I fructose 1,6-bisphosphate aldolases from rabbit muscle, sturgeon muscle, trout muscle and ox liver."
    Benfield P.A., Forcina B.G., Gibbons I., Perham R.N.
    Biochem. J. 183:429-444(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 174-201, SEQUENCE REVISION.
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  6. 6
    "Studies on the structure of rabbit muscle aldolase. Determination of the primary structure of the COOH-terminal BrCN peptide; the complete sequence of the subunit polypeptide chain."
    Lai C.-Y.
    Arch. Biochem. Biophys. 166:358-368(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 252-364, SEQUENCE REVISION.
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  7. 7
    "A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing."
    Putney S.D., Herlihy W.C., Schimmel P.R.
    Nature 302:718-721(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-56 AND 350-364.
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 14 other entries.

  8. 8
    "Identification of the histidyl residue of rabbit muscle aldolase alkylated by N-bromoacetylethanolamine phosphate."
    Hartman F.C., Welch M.H.
    Biochem. Biophys. Res. Commun. 57:85-92(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE, DEAMIDATION AT ASN-361.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).
  9. 9
    "Affinity labeling of a previously undetected essential lysyl residue in class I fructose bisphosphate aldolase."
    Hartman F.C., Brown J.P.
    J. Biol. Chem. 251:3057-3062(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).
  10. 10
    "Identification of the C-1-phosphate-binding arginine residue of rabbit-muscle aldolase. Isolation of 1,2-cyclohexanedione-labeled peptide by chemisorption chromatography."
    Patthy L., Varadi A., Thesz J., Kovacs K.
    Eur. J. Biochem. 99:309-313(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE-BINDING SITE.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).
  11. 11
    "The effect of calcium ions on subcellular localization of aldolase-FBPase complex in skeletal muscle."
    Mamczur P., Rakus D., Gizak A., Dus D., Dzugaj A.
    FEBS Lett. 579:1607-1612(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBP2, SUBCELLULAR LOCATION.
    Category: Subcellular Location, Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  12. 12
    "Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase."
    Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D.
    Proteins 72:209-216(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBP2.
    Category: Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3 and mapped to 2 other entries.

  13. 13
    "Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase."
    Blom N., Sygusch J.
    Nat. Struct. Biol. 4:36-39(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    Category: Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  14. 14
    "Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 A."
    Choi K.H., Mazurkie A.S., Morris A.J., Utheza D., Tolan D.R., Allen K.N.
    Biochemistry 38:12655-12664(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-345 IN COMPLEX WITH SUBSTRATE, SUBUNIT, MUTAGENESIS OF GLU-35; ARG-43; LYS-147 AND ARG-304.
    Category: Pathology & Biotech, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  15. 15
    "A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases."
    Maurady A., Zdanov A., de Moissac D., Beaudry D., Sygusch J.
    J. Biol. Chem. 277:9474-9483(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS), MUTAGENESIS OF GLU-188; GLU-190 AND LYS-230.
    Category: Pathology & Biotech, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  16. 16
    "A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein."
    St-Jean M., Izard T., Sygusch J.
    J. Biol. Chem. 282:14309-14315(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH WAS, FUNCTION.
    Category: Function, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  17. 17
    "Structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variant."
    Sherawat M., Tolan D.R., Allen K.N.
    Acta Crystallogr. D 64:543-550(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 5-344 OF MUTANT VAL-129, SUBUNIT.
    Category: Pathology & Biotech, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  18. 18
    "Mechanism of aldolase control of sorting nexin 9 function in endocytosis."
    Rangarajan E.S., Park H., Fortin E., Sygusch J., Izard T.
    J. Biol. Chem. 285:11983-11990(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SNX9, INTERACTION WITH SNX9, SUBUNIT, CATALYTIC ACTIVITY.
    Category: Function, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 and mapped to 4 other entries.

  19. 19
    "Snapshots of catalysis: the structure of fructose-1,6-(bis)phosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate."
    Choi K.H., Shi J., Hopkins C.E., Tolan D.R., Allen K.N.
    Biochemistry 40:13868-13875(2001) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:1J4E.
  20. 20
    "High resolution reaction intermediates of rabbit muscle fructose-1,6-bisphosphate aldolase: substrate cleavage and induced fit."
    St-Jean M., Lafrance-Vanasse J., Liotard B., Sygusch J.
    J. Biol. Chem. 280:27262-27270(2005) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:1ZAL, PDB:1ZAH, PDB:1ZAI, PDB:1ZAJ.
  21. 21
    "Stereospecific proton transfer by a mobile catalyst in mammalian fructose-1,6-bisphosphate aldolase."
    St-Jean M., Sygusch J.
    J. Biol. Chem. 282:31028-31037(2007) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:2QUU, PDB:2QUV, PDB:2QUT.
  22. 22
    "Charge stabilization and entropy reduction of central lysine residues in fructose-bisphosphate aldolase."
    St-Jean M., Blonski C., Sygusch J.
    Biochemistry 48:4528-4537(2009) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Annotation: kinetic and structural analyses of fructose-bisphosphate aldolaseImported.
    Source: PDB:3DFN, GeneRIF:100009055, PDB:3DFS, PDB:3DFT, PDB:3DFQ, PDB:3DFP, PDB:3DFO.
  23. 23
    "Dramatic improvement of crystal quality for low-temperature-grown rabbit muscle aldolase."
    Park H., Rangarajan E.S., Sygusch J., Izard T.
    Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66:595-600(2010) [PubMed] [Europe PMC] [Abstract]
    Annotation: The lattice of muscle aldolase contacts corresponded to an increased number of interactions between high-entropy side chains that mitigate the lattice strain incurred upon cryocooling and accompanying mosaic spread increases.Imported.
    Source: GeneRIF:100009055.
  24. 24
    "Proliferating cell nuclear antigen in the cytoplasm interacts with components of glycolysis and cancer."
    Naryzhny S.N., Lee H.
    FEBS Lett. 584:4292-4298(2010) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:P00883.

    This publication is mapped to 23 other entries.

  25. 25
    "Achieving better-than-3-A resolution by single-particle cryo-EM at 200 keV."
    Herzik M.A. Jr., Wu M., Lander G.C.
    Nat. Methods 14:1075-1078(2017) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:5VY5.

    This publication is mapped to 2 other entries.

1 to 25 of 25  Show