Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Simon H. Chang"'
Publikováno v:
Analytical Biochemistry. 447:1-5
An assay was developed for phosphofructokinase-1 (PFK-1) using capillary electrophoresis (CE). In the glycolytic pathway, this enzyme catalyzes the rate-limiting step from fructose-6-phosphate and magnesium-bound adenosine triphosphate (Mg-ATP) to fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2b76f7330c3934090a01c424f42e2c7
https://doi.org/10.1016/j.ab.2013.10.028
https://doi.org/10.1016/j.ab.2013.10.028
Autor:
Simon H. Chang, Babak Javid, Ya Su, Aiwu Zhou, Katherine Bowers, Katherine G. Blake-Palmer, Sara L. Sorrell, Fiona E. Karet, Seema Qamar
Publikováno v:
American Journal of Physiology-Renal Physiology
The vacuolar-type ATPase (H+ATPase) is a ubiquitously expressed multisubunit pump whose regulation is poorly understood. Its membrane-integral a-subunit is involved in proton translocation and in humans has four forms, a1–a4. This study investigate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9b56dc0043e735d9a68ca89b9b4d7ee
http://europepmc.org/articles/PMC2576143
http://europepmc.org/articles/PMC2576143
Autor:
Kathryn S. Aultman, Simon H. Chang
Publikováno v:
European Journal of Biochemistry. 124:471-476
Partial P1 nuclease digestion of 5'-32P-labeled tRNAs, followed by polyacrylamide gel electrophoresis and autoradiography, results in a series of bands of unequal intensities. Comparison of the digestion profiles of two conformers of yeast tRNA3Leu s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a8e2611e1ac8716ed685b5ada31e2c5
https://doi.org/10.1111/j.1432-1033.1982.tb06617.x
https://doi.org/10.1111/j.1432-1033.1982.tb06617.x
Publikováno v:
Biochemistry. 34:2560-2565
Crystallographic studies indicate that the loop between alpha-helix 8 and beta-strand H (the 8H loop) which borders the effector site of Bacillus stearothermophilus phosphofructokinase (BsPFK) is involved in the allosteric mechanism of the enzyme [Sc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ca76c31d569de06e5a158c5b604fee6
https://doi.org/10.1021/bi00008a021
https://doi.org/10.1021/bi00008a021
Publikováno v:
FEBS Letters. 356:81-85
We previously reported that the D39N mutant of Drosophila alcohol dehydrogenase (ADH), in which Asp-39 is replaced with asparagine, has a 60-fold increase in affinity for NADP+ and a 1.5-fold increase in kcat compared to wild-type ADH [Chen et al. (1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68779a682ecdc3d59f30145afa214472
https://doi.org/10.1016/0014-5793(94)01234-2
https://doi.org/10.1016/0014-5793(94)01234-2
Publikováno v:
Journal of Biological Chemistry. 268:24599-24606
Full-length cDNA for rabbit muscle phosphofructokinase has been cloned and characterized (Li, J., Chen, Z., Lu, L., Byrnes, M., and Chang, S. H. (1990) Biochem. Biophys. Res. Commun. 170, 1056-1060). The 2.8-kilobase cDNA was inserted in the plasmid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::891fa8a16f9114fbf194c09f79d260a2
https://doi.org/10.1016/s0021-9258(19)74508-6
https://doi.org/10.1016/s0021-9258(19)74508-6
Autor:
Teresa Ruiz, Katarzyna Banaszak, Simon H. Chang, Galina Obmolova, Wojciech Rypniewski, Gerhard Kopperschläger, Ingrid Mechin, Michael L. Oldham, Michael Radermacher
Publikováno v:
Journal of molecular biology. 407(2)
Phosphofructokinase 1 (PFK) is a multisubunit allosteric enzyme that catalyzes the principal regulatory step in glycolysis—the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate by ATP. The activity of eukaryotic PFK is modulated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d433ce632e9703cebd002bddcc1357d
https://pubmed.ncbi.nlm.nih.gov/21241708
https://pubmed.ncbi.nlm.nih.gov/21241708
Publikováno v:
European Journal of Biochemistry. 202:263-267
Drosophila alcohol dehydrogenase (ADH), an NAD(+)-dependent dehydrogenase, shares little sequence similarity with horse liver ADH. However, these two enzymes do have substantial similarity in their secondary structure at the NAD(+)-binding domain [Be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c99c8a3e4a8224129df169837bff532
https://doi.org/10.1111/j.1432-1033.1991.tb16371.x
https://doi.org/10.1111/j.1432-1033.1991.tb16371.x
Autor:
Simon H. Chang, Robert G. Kemp
Publikováno v:
Biochemical and biophysical research communications. 290(2)
Fructose-2,6-bisphosphate (Fru-2,6-P(2)) is a potent allosteric activator of the ATP-dependent phosphofructokinase (PFK) in eukaryotes. Based on the sequence homology between rabbit muscle PFK and two bacterial PFKs and the crystal structures of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b929091458bbc423cbaf07e68221885
https://pubmed.ncbi.nlm.nih.gov/11785951
https://pubmed.ncbi.nlm.nih.gov/11785951
Publikováno v:
Biochemistry. 34(38)
The ability of Drosophila alcohol dehydrogenase (D-ADH) to catalyze the oxidation of aldehydes to carboxylic acids has been re-examined. Prior studies are shown to have been compromised by a nonenzymic reaction between the aldehydic substrates and am
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a65f5880c96f144880121325da96b249
https://pubmed.ncbi.nlm.nih.gov/7547972
https://pubmed.ncbi.nlm.nih.gov/7547972