Colipase: structure and interaction with pancreatic lipase.
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[1] R. Kaptein,et al. 360-MHz nuclear magnetic resonance and laser photochemically induced dynamic nuclear polarization studies of bile salt interaction with porcine colipase A. , 2005, European journal of biochemistry.
[2] C. Chothia,et al. The atomic structure of protein-protein recognition sites. , 1999, Journal of molecular biology.
[3] D. Pignol,et al. Ion Pairing between Lipase and Colipase Plays a Critical Role in Catalysis* , 1998, The Journal of Biological Chemistry.
[4] R. Verger,et al. Structure and Activity of Rat Pancreatic Lipase-related Protein 2* , 1998, The Journal of Biological Chemistry.
[5] H. van Tilbeurgh,et al. Structural basis for the substrate selectivity of pancreatic lipases and some related proteins. , 1998, Biochimica et biophysica acta.
[6] J. Boisbouvier,et al. A structural homologue of colipase in black mamba venom revealed by NMR floating disulphide bridge analysis. , 1998, Journal of molecular biology.
[7] P. Barboni,et al. Pancreatic lipase-related protein 1 (PLRP1) is present in the pancreatic juice of several species. , 1998, Biochimica et biophysica acta.
[8] M. Lowe,et al. The hydrophobic surface of colipase influences lipase activity at an oil-water interface. , 1998, Journal of lipid research.
[9] R. Verger,et al. Reactivation of the totally inactive pancreatic lipase RP1 by structure‐predicted point mutations , 1998, Proteins.
[10] D. Moss,et al. Structure of the key toxin in gas gangrene , 1998, Nature Structural &Molecular Biology.
[11] E. Koonin,et al. A colipase fold in the carboxy-terminal domain of the Wnt antagonists – the Dickkopfs , 1998, Current Biology.
[12] D. Pignol,et al. Pancreatic lipase-related protein type 1: a double mutation restores a significant lipase activity. , 1998, Biochemical and biophysical research communications.
[13] C. Niehrs,et al. Dickkopf-1 is a member of a new family of secreted proteins and functions in head induction , 1998, Nature.
[14] Robert Fletterick,et al. The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity , 1997, Nature Structural Biology.
[15] S. Cole,et al. The carboxy‐terminal C2‐like domain of the α‐toxin from Clostridium perfringens mediates calcium‐dependent membrane recognition , 1997, Molecular microbiology.
[16] F. Dyda,et al. The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism. , 1997, Structure.
[17] S. Penel,et al. Neutron crystallographic evidence of lipase–colipase complex activation by a micelle , 1997, The EMBO journal.
[18] J. Kastelein,et al. Mutation of Tryptophan Residues in Lipoprotein Lipase , 1997, The Journal of Biological Chemistry.
[19] M. Lowe. Colipase Stabilizes the Lid Domain of Pancreatic Triglyceride Lipase* , 1997, The Journal of Biological Chemistry.
[20] J. Falke,et al. The C2 domain calcium‐binding motif: Structural and functional diversity , 1996, Protein science : a publication of the Protein Society.
[21] D. Bourgeois,et al. A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig. , 1996, Structure.
[22] D. Pignol,et al. Lipase Activation by Nonionic Detergents , 1996, The Journal of Biological Chemistry.
[23] Roger L. Williams,et al. Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ , 1996, Nature.
[24] S. Sprang,et al. Structure of the first C2 domain of synaptotagmin I: A novel Ca2+/phospholipid-binding fold , 1995, Cell.
[25] H. Tilbeurgh,et al. Crystallographic study of the structure of colipase and of the interaction with pancreatic lipase , 1995, Protein science : a publication of the Protein Society.
[26] R. Kaptein,et al. Solution structure of porcine pancreatic procolipase as determined from 1H homonuclear two-dimensional and three-dimensional NMR. , 1994, European journal of biochemistry.
[27] H. van Tilbeurgh,et al. The 2.46 A resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate. , 1994, Biochemistry.
[28] C Cambillau,et al. Horse pancreatic lipase. The crystal structure refined at 2.3 A resolution. , 1994, Journal of molecular biology.
[29] J. Lalouel,et al. The carboxyl-terminal domain of lipoprotein lipase binds to the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor (LRP) and mediates binding of normal very low density lipoproteins to LRP. , 1994, The Journal of biological chemistry.
[30] R. Verger,et al. Evidence for a pancreatic lipase subfamily with new kinetic properties. , 1994, Biochemistry.
[31] J. Lalouel,et al. Lipoprotein lipase. Molecular model based on the pancreatic lipase x-ray structure: consequences for heparin binding and catalysis. , 1994, The Journal of biological chemistry.
[32] L M Amzel,et al. The three-dimensional structure of an arachidonic acid 15-lipoxygenase. , 1993, Science.
[33] R. Titball,et al. Biochemical and immunological properties of the C-terminal domain of the alpha-toxin of Clostridium perfringens. , 1993, FEMS microbiology letters.
[34] L. Thim,et al. A structural domain (the lid) found in pancreatic lipases is absent in the guinea pig (phospho)lipase. , 1993, Biochemistry.
[35] H. Tilbeurgh,et al. Interfacial activation of the lipase–procolipase complex by mixed micelles revealed by X-ray crystallography , 1993, Nature.
[36] T. P. King,et al. Sequence similarity of a hornet (D. maculata) venom allergen phospholipase A1 with mammalian lipases , 1993, FEBS letters.
[37] G. Bengtsson-Olivecrona,et al. Chymotryptic cleavage of lipoprotein lipase. Identification of cleavage sites and functional studies of the truncated molecule. , 1993, European journal of biochemistry.
[38] H. Tilbeurgh,et al. Structure of the pancreatic lipase–procolipase complex , 1992, Nature.
[39] P. Buchwald,et al. Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. , 1992, The Journal of biological chemistry.
[40] F. Winkler,et al. Structure of human pancreatic lipase , 1990, Nature.
[41] R. Dixon,et al. Requirement of a 5-lipoxygenase-activating protein for leukotriene synthesis , 1990, Nature.
[42] P. Kraulis,et al. Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. , 1989, Biochemistry.
[43] R. Verger,et al. A new kinetic approach for studying phospholipase C (Clostridium perfringens alpha toxin) activity on phospholipid monolayers. , 1988, Biochemistry.
[44] S. Dahlén,et al. Leukotrienes and lipoxins: structures, biosynthesis, and biological effects. , 1987, Science.
[45] H. van Tilbeurgh,et al. Limited proteolysis of the cellobiohydrolase I from Trichoderma reesei , 1986 .
[46] T. P. King,et al. Wasp venom proteins: phospholipase A1 and B. , 1984, Archives of Biochemistry and Biophysics.
[47] C. Erlanson‐Albertsson,et al. Measurement of the binding of human colipase to human lipase and lipase substrates. , 1982, Biochimica et biophysica acta.
[48] L. Sarda,et al. Studies on the effect of bile salt and colipase on enzymatic lipolysis. Improved method for the determination of pancreatic lipase and colipase. , 1976, Biochimie.
[49] H. van Tilbeurgh,et al. Pancreatic lipases and their complexes with colipases and inhibitors: crystallization and crystal packing. , 1997, Methods in enzymology.