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Novel insights into the chemical mechanism of ATP synthase. Evidence that in the transition state the gamma-phosphate of ATP is near the conserved alanine within the P-loop of the beta-subunit.
Ko YH, Bianchet M, Amzel LM, Pedersen PL. Ko YH, et al. J Biol Chem. 1997 Jul 25;272(30):18875-81. doi: 10.1074/jbc.272.30.18875. J Biol Chem. 1997. PMID: 9228065
Mitochondrial ATP synthasome: three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP.
Chen C, Ko Y, Delannoy M, Ludtke SJ, Chiu W, Pedersen PL. Chen C, et al. Among authors: ko y. J Biol Chem. 2004 Jul 23;279(30):31761-8. doi: 10.1074/jbc.M401353200. Epub 2004 May 27. J Biol Chem. 2004. PMID: 15166242
Under mild conditions, these entities sub-fractionate as an ATP synthase/PIC/ANC complex or "ATP synthasome" (Ko, Y.H., Delannoy, M, Hullihen, J., Chiu, W., and Pedersen, P.L. (2003) J. ...
Under mild conditions, these entities sub-fractionate as an ATP synthase/PIC/ANC complex or "ATP synthasome" (Ko, Y.H., Delannoy, M, …
Multiprotein complex containing succinate dehydrogenase confers mitochondrial ATP-sensitive K+ channel activity.
Ardehali H, Chen Z, Ko Y, Mejía-Alvarez R, Marbán E. Ardehali H, et al. Among authors: ko y. Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11880-5. doi: 10.1073/pnas.0401703101. Epub 2004 Jul 29. Proc Natl Acad Sci U S A. 2004. PMID: 15284438 Free PMC article.
Cystic fibrosis transmembrane conductance regulator: the NBF1+R (nucleotide-binding fold 1 and regulatory domain) segment acting alone catalyses a Co2+/Mn2+/Mg2+-ATPase activity markedly inhibited by both Cd2+ and the transition-state analogue orthovanadate.
Annereau JP, Ko YH, Pedersen PL. Annereau JP, et al. Among authors: ko yh. Biochem J. 2003 Apr 15;371(Pt 2):451-62. doi: 10.1042/BJ20021318. Biochem J. 2003. PMID: 12523935 Free PMC article.
Signal transduction to mitochondrial ATP synthase: evidence that PDGF-dependent phosphorylation of the delta-subunit occurs in several cell lines, involves tyrosine, and is modulated by lysophosphatidic acid.
Ko YH, Pan W, Inoue C, Pedersen PL. Ko YH, et al. Mitochondrion. 2002 Feb;1(4):339-48. doi: 10.1016/s1567-7249(01)00036-8. Mitochondrion. 2002. PMID: 16120288
Mitochondrial F(0)F(1) ATP synthase. Subunit regions on the F1 motor shielded by F(0), Functional significance, and evidence for an involvement of the unique F(0) subunit F(6).
Ko YH, Hullihen J, Hong S, Pedersen PL. Ko YH, et al. J Biol Chem. 2000 Oct 20;275(42):32931-9. doi: 10.1074/jbc.M004453200. J Biol Chem. 2000. PMID: 10887193
Mechanism of action of human P-glycoprotein ATPase activity. Photochemical cleavage during a catalytic transition state using orthovanadate reveals cross-talk between the two ATP sites.
Hrycyna CA, Ramachandra M, Ambudkar SV, Ko YH, Pedersen PL, Pastan I, Gottesman MM. Hrycyna CA, et al. Among authors: ko yh. J Biol Chem. 1998 Jul 3;273(27):16631-4. doi: 10.1074/jbc.273.27.16631. J Biol Chem. 1998. PMID: 9642211
Chemical mechanism of ATP synthase. Magnesium plays a pivotal role in formation of the transition state where ATP is synthesized from ADP and inorganic phosphate.
Ko YH, Hong S, Pedersen PL. Ko YH, et al. J Biol Chem. 1999 Oct 8;274(41):28853-6. doi: 10.1074/jbc.274.41.28853. J Biol Chem. 1999. PMID: 10506126
In an earlier report (Ko, Y. H., Bianchet, M. A., Amzel, L.M., and Pedersen, P. L. (1997) J. Biol. Chem. 272, 18875-18881), we provided evidence for transition state formation in the presence of Mg(2+), ADP, and orthovanadate (V(i)), a photoreactive phosphate analog with a …
In an earlier report (Ko, Y. H., Bianchet, M. A., Amzel, L.M., and Pedersen, P. L. (1997) J. Biol. Chem. 272, 18875-18881), we provid …
Cystic fibrosis: a brief look at some highlights of a decade of research focused on elucidating and correcting the molecular basis of the disease.
Ko YH, Pedersen PL. Ko YH, et al. J Bioenerg Biomembr. 2001 Dec;33(6):513-21. doi: 10.1023/a:1012831322753. J Bioenerg Biomembr. 2001. PMID: 11804193 Review.
Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation.
Massiah MA, Ko YH, Pedersen PL, Mildvan AS. Massiah MA, et al. Among authors: ko yh. Biochemistry. 1999 Jun 8;38(23):7453-61. doi: 10.1021/bi9903603. Biochemistry. 1999. PMID: 10360942
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