Zobrazeno 1 - 10
of 178
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ca8c1443ee6d5773cd7e463b9ad23ee1
https://doi.org/10.1074/jbc.275.17.12926
https://doi.org/10.1074/jbc.275.17.12926
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95f065cd573207dcc42bf2e1fc113ffd
https://doi.org/10.1016/s0968-0004(00)01550-4
https://doi.org/10.1016/s0968-0004(00)01550-4
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef5b4a6c7f287e75d95c549c6e534674
https://doi.org/10.1021/bi982195h
https://doi.org/10.1021/bi982195h
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5adf1777b12cf3a2517977ae574197fa
https://doi.org/10.1002/cbf.699
https://doi.org/10.1002/cbf.699
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbad46fb6ff29ddbfeb94ff99480cd13
https://doi.org/10.1021/bi960336e
https://doi.org/10.1021/bi960336e
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e9fc63c555b8b8e4c8d6232157bfa51
https://doi.org/10.1021/bi00001a031
https://doi.org/10.1021/bi00001a031
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d17d12f955d15bc817dd9d324d414684
https://doi.org/10.1016/s0021-9258(18)43924-5
https://doi.org/10.1016/s0021-9258(18)43924-5
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::082b4c067f968a3d0c8814092bb7d393
https://doi.org/10.1021/bi00205a003
https://doi.org/10.1021/bi00205a003
Autor:
Christer Lindbladh, Klaus Mosbach, C Hagglund, M Rault, W. C. Small, Paul A. Srere, Leif Bülow, Claudia T. Evans
Publikováno v:
Biochemistry. 33:11692-11698
We have expressed the DNA of the fusion of CS1 to MDH1 in Escherichia coli gltA-. The fusion protein (CS1/MDH1) is the C-terminus of CS1 linked in-frame to the N-terminus of MDH1 with a short linker of glycyl-seryl-glycyl. The fusion protein produced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::507cc216c4304cf955b4b39da4a0f5ad
https://doi.org/10.1021/bi00205a004
https://doi.org/10.1021/bi00205a004
Autor:
Paul A. Srere
Publikováno v:
The Roots of Modern Biochemistry: Fritz Lippmann's Squiggle and its Consequences
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::17472962b0516feecaa3c35c14d06365
https://doi.org/10.1515/9783110852455.135
https://doi.org/10.1515/9783110852455.135
