These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

135 related articles for article (PubMed ID: 11790778)

  • 1. Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the enzyme are important for the unusual high malonyl-CoA sensitivity.
    Nicot C; Relat J; Woldegiorgis G; Haro D; Marrero PF
    J Biol Chem; 2002 Mar; 277(12):10044-9. PubMed ID: 11790778
    [TBL] [Abstract][Full Text] [Related]  

  • 2. A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of rat liver carnitine palmitoyltransferase I increases its malonyl-CoA sensitivity close to that observed with the muscle isoform of the enzyme.
    Napal L; Dai J; Treber M; Haro D; Marrero PF; Woldegiorgis G
    J Biol Chem; 2003 Sep; 278(36):34084-9. PubMed ID: 12826662
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Deletion of the conserved first 18 N-terminal amino acid residues in rat liver carnitine palmitoyltransferase I abolishes malonyl-CoA sensitivity and binding.
    Shi J; Zhu H; Arvidson DN; Cregg JM; Woldegiorgis G
    Biochemistry; 1998 Aug; 37(31):11033-8. PubMed ID: 9692998
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Pig liver carnitine palmitoyltransferase I, with low Km for carnitine and high sensitivity to malonyl-CoA inhibition, is a natural chimera of rat liver and muscle enzymes.
    Nicot C; Hegardt FG; Woldegiorgis G; Haro D; Marrero PF
    Biochemistry; 2001 Feb; 40(7):2260-6. PubMed ID: 11329295
    [TBL] [Abstract][Full Text] [Related]  

  • 5. The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding.
    Shi J; Zhu H; Arvidson DN; Woldegiorgis G
    Biochemistry; 2000 Feb; 39(4):712-7. PubMed ID: 10651636
    [TBL] [Abstract][Full Text] [Related]  

  • 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; 277(49):47184-9. PubMed ID: 12351641
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat liver carnitine palmitoyltransferase I that are important for catalytic activity and malonyl-CoA sensitivity.
    Treber M; Dai J; Woldegiorgis G
    J Biol Chem; 2003 Mar; 278(13):11145-9. PubMed ID: 12540837
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Pig muscle carnitine palmitoyltransferase I (CPTI beta), with low Km for carnitine and low sensitivity to malonyl-CoA inhibition, has kinetic characteristics similar to those of the rat liver (CPTI alpha) enzyme.
    Relat J; Nicot C; Gacias M; Woldegiorgis G; Marrero PF; Haro D
    Biochemistry; 2004 Oct; 43(39):12686-91. PubMed ID: 15449958
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Substitution of glutamate-3, valine-19, leucine-23, and serine-24 with alanine in the N-terminal region of human heart muscle carnitine palmitoyltransferase I abolishes malonyl CoA inhibition and binding.
    Zhu H; Shi J; Treber M; Dai J; Arvidson DN; Woldegiorgis G
    Arch Biochem Biophys; 2003 May; 413(1):67-74. PubMed ID: 12706342
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the kinetics of carnitine palmitoyltransferase I isoforms.
    Jackson VN; Cameron JM; Fraser F; Zammit VA; Price NT
    J Biol Chem; 2000 Jun; 275(26):19560-6. PubMed ID: 10766754
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Roles of the N- and C-terminal domains of carnitine palmitoyltransferase I isoforms in malonyl-CoA sensitivity of the enzymes: insights from expression of chimaeric proteins and mutation of conserved histidine residues.
    Swanson ST; Foster DW; McGarry JD; Brown NF
    Biochem J; 1998 Nov; 335 ( Pt 3)(Pt 3):513-9. PubMed ID: 9794789
    [TBL] [Abstract][Full Text] [Related]  

  • 12. 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; 280(6):4524-31. PubMed ID: 15579906
    [TBL] [Abstract][Full Text] [Related]  

  • 13. A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver carnitine palmitoyltransferase I abolishes malonyl-CoA inhibition and high affinity binding.
    Shi J; Zhu H; Arvidson DN; Woldegiorgis G
    J Biol Chem; 1999 Apr; 274(14):9421-6. PubMed ID: 10092622
    [TBL] [Abstract][Full Text] [Related]  

  • 14. 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; 387(Pt 1):67-76. PubMed ID: 15498023
    [TBL] [Abstract][Full Text] [Related]  

  • 15. A characteristic Glu17 residue of pig carnitine palmitoyltransferase 1 is responsible for the low Km for carnitine and the low sensitivity to malonyl-CoA inhibition of the enzyme.
    Relat J; Pujol-Vidal M; Haro D; Marrero PF
    FEBS J; 2009 Jan; 276(1):210-8. PubMed ID: 19049515
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within the amino termini of rat liver- and muscle-type carnitine palmitoyltransferase I.
    Jackson VN; Zammit VA; Price NT
    J Biol Chem; 2000 Dec; 275(49):38410-6. PubMed ID: 10969089
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Reconstitution of purified, active and malonyl-CoA-sensitive rat liver carnitine palmitoyltransferase I: relationship between membrane environment and malonyl-CoA sensitivity.
    McGarry JD; Brown NF
    Biochem J; 2000 Jul; 349(Pt 1):179-87. PubMed ID: 10861226
    [TBL] [Abstract][Full Text] [Related]  

  • 18. 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; 278(11):9058-63. PubMed ID: 12499375
    [TBL] [Abstract][Full Text] [Related]  

  • 19. 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; 282(25):18212-18224. PubMed ID: 17452323
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Functional characterization of mitochondrial carnitine palmitoyltransferases I and II expressed in the yeast Pichia pastoris.
    de Vries Y; Arvidson DN; Waterham HR; Cregg JM; Woldegiorgis G
    Biochemistry; 1997 Apr; 36(17):5285-92. PubMed ID: 9136891
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 7.