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Items: 1 to 20 of 315

1.

Definition by functional and structural analysis of two malonyl-CoA sites in carnitine palmitoyltransferase 1A.

López-Viñas E, Bentebibel A, Gurunathan C, Morillas M, de Arriaga D, Serra D, Asins G, Hegardt FG, Gómez-Puertas P.

J Biol Chem. 2007 Jun 22;282(25):18212-24. Epub 2007 Apr 23.

2.

Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for malonyl-CoA inhibition. Mutation of methionine 593 abolishes malonyl-CoA inhibition.

Morillas M, Gómez-Puertas P, Bentebibel A, Sellés E, Casals N, Valencia A, Hegardt FG, Asins G, Serra D.

J Biol Chem. 2003 Mar 14;278(11):9058-63. Epub 2002 Dec 23.

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Cysteine-scanning mutagenesis of muscle carnitine palmitoyltransferase I reveals a single cysteine residue (Cys-305) is important for catalysis.

Liu H, Zheng G, Treber M, Dai J, Woldegiorgis G.

J Biol Chem. 2005 Feb 11;280(6):4524-31. Epub 2004 Dec 3.

6.

The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA sensitivity but in initial protein folding.

Pan Y, Cohen I, Guillerault F, Fève B, Girard J, Prip-Buus C.

J Biol Chem. 2002 Dec 6;277(49):47184-9. Epub 2002 Sep 25.

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Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: mutational analysis of a malonyl-CoA affinity domain.

Morillas M, Gómez-Puertas P, Rubí B, Clotet J, Ariño J, Valencia A, Hegardt FG, Serra D, Asins G.

J Biol Chem. 2002 Mar 29;277(13):11473-80. Epub 2002 Jan 14.

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Demonstration of N- and C-terminal domain intramolecular interactions in rat liver carnitine palmitoyltransferase 1 that determine its degree of malonyl-CoA sensitivity.

Faye A, Borthwick K, Esnous C, Price NT, Gobin S, Jackson VN, Zammit VA, Girard J, Prip-Buus C.

Biochem J. 2005 Apr 1;387(Pt 1):67-76.

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