Zobrazeno 1 - 10
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pro vyhledávání: '"Paul A. Srere"'
Autor:
Paul A. Srere, Christian Vélot
Publikováno v:
Journal of Biological Chemistry. 275:12926-12933
The enzymes of the Krebs tricarboxylic acid cycle in mitochondria are proposed to form a supramolecular complex, in which there is channeling of intermediates between enzyme active sites. While interactions have been demonstrated in vitro between mos
Autor:
Paul A. Srere
Publikováno v:
Trends in Biochemical Sciences. 25:150-153
So, what is ‘new’ about ‘the new biochemistry’? Certainly not macromolecular interactions. Rather, it is the realization that the role of macromolecular interactions is fundamental to all of the currently ‘hot’ research areas in biochemis
Autor:
Sandrine Lebreton, Paul A. Srere, Konstantin Shatalin, Magali Rault-Leonardon, Christian Vélot
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 1999, 38, pp.881-889
Biochemistry, American Chemical Society, 1999, 38, pp.881-889
Mitochondrial malate dehydrogenase and citrate synthase are sequential enzymes in the Krebs tricarboxylic acid cycle. We have shown [Lindbladh, C., Rault, M., Hagglund, C., Small, W. C., Mosbach, K., Bülow, L., Evans, C., and Srere, P.A (1994) Bioch
Autor:
Igor Morgunov, Paul A. Srere
Publikováno v:
Journal of Biological Chemistry. 273:29540-29544
The interactions between pig heart citrate synthase and mitochondrial malate dehydrogenase or cytosolic malate dehydrogenase were studied using the frontal analysis method of gel filtration and by precipitation in polyethylene glycol. This method sho
Autor:
JUDIT OVÁDI, PAUL A. SRERE
Publikováno v:
Cell Biochemistry and Function. 14:249-258
Autor:
Paul A. Srere, Judit Ovádi
Publikováno v:
Cell Biochemistry and Function. 14:249-258
The fact that enzyme complexes, stable, quasi-stable, and dynamic, exist in cells can no longer be ignored. Experimental evidence done with a variety of techniques has demonstrated these interactions in vitro and in vivo. There is scarcely a single k
Publikováno v:
Biochemistry. 35:10661-10672
We examined the catalytic efficiency of 18 pig citrate synthase mutants. The residues mutated were selected according to two criteria: the conservation of that residue in all known citrate synthase sequences, and the importance of that residue in sub
Autor:
Clive A. Slaughter, Paul A. Srere, Mark A. L. Atkinson, Magali Rault-Leonardon, Carolyn R. Moomaw
Publikováno v:
Biochemistry. 34:257-263
We have purified the citrate synthase from Azotobacter vinelandii and have determined that the size of the subunit is 48,000 Da and the structure of the holoenzyme is a hexamer. This contrasts with earlier estimates that indicate a 58,000 Da subunit
Publikováno v:
Journal of Biological Chemistry. 269:29609-29612
We have characterized 1,2,3-benzenetricarboxylic acid-sensitive, mersalyl-insensitive citrate uptake by mitochondria from two strains of Saccharomyces cerevisiae by describing the time course, Km and Vmax values, pH dependence, and response to inhibi
Metabolic studies on Saccharomyces cerevisiae containing fused citrate synthase/malate dehydrogenase
Autor:
Paul A. Srere, Richard D. Brodeur, Christer Lindbladh, William C. Small, Lilius G, Leif Bülow, Klaus Mosbach
Publikováno v:
Biochemistry. 33:11684-11691
We have constructed two different fusion proteins consisting of the C-terminal end of CS1 fused in-frame to the N-terminal end of MDH1 and HSA, respectively. The fusion proteins were expressed in mutants of Saccharomyces cerevisiae in which CS1 and M