Author pages are created from data sourced from our academic publisher partnerships and public sources.
- Publications
- Influence
Insights from retinitis pigmentosa into the roles of isocitrate dehydrogenases in the Krebs cycle
- D. T. Hartong, Mayura Dange, T. McGee, E. Berson, T. Dryja, R. F. Colman
- Biology, Medicine
- Nature Genetics
- 21 September 2008
Here we describe two families with retinitis pigmentosa, a hereditary neurodegeneration of rod and cone photoreceptors in the retina. Affected family members were homozygous for loss-of-function… Expand
Crystal Structure of Porcine Mitochondrial NADP+-dependent Isocitrate Dehydrogenase Complexed with Mn2+ and Isocitrate
- C. Ceccarelli, N. Grodsky, Nandana Ariyaratne, R. F. Colman, B. J. Bahnson
- Chemistry, Medicine
- The Journal of Biological Chemistry
- 8 November 2002
The crystal structure of porcine heart mitochondrial NADP+-dependent isocitrate dehydrogenase (IDH) complexed with Mn2+ and isocitrate was solved to a resolution of 1.85 Å. The enzyme was expressed… Expand
Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes.
- L. Ralat, Y. Manevich, A. Fisher, R. F. Colman
- Chemistry, Medicine
- Biochemistry
- 17 January 2006
Glutathione S-transferase pi (GST pi) has been shown to reactivate oxidized 1-cysteine peroxiredoxin (1-Cys Prx, Prx VI, Prdx6, and AOP2). We now demonstrate that a heterodimer complex is formed… Expand
Affinity labeling of purine nucleotide sites in proteins.
- R. F. Colman
- Chemistry, Medicine
- Annual review of biochemistry
- 1983
Adenylosuccinate lyase deficiency.
- E. Spiegel, R. F. Colman, D. Patterson
- Biology, Medicine
- Molecular genetics and metabolism
- 1 September 2006
Adenylosuccinate lyase deficiency is a disease of purine metabolism which affects patients both biochemically and behaviorally. The symptoms are variable and include psychomotor retardation, autistic… Expand
Chemical characterization of distinct subunits of pig heart DPN-specific isocitrate dehydrogenase.
- N. Ramachandran, R. F. Colman
- Medicine, Chemistry
- The Journal of biological chemistry
- 25 September 1980
Pig heart DPN-dependent isocitrate dehydrogenase is heterogeneous on isoelectric focusing in 6 M urea. Under these conditions, three types of subunits (termed alpha, beta, and gamma), which have… Expand
Clopidogrel inhibits the binding of ADP analogues to the receptor mediating inhibition of platelet adenylate cyclase.
- D. C. Mills, R. Puri, +5 authors R. Colman
- Chemistry, Medicine
- Arteriosclerosis and thrombosis : a journal of…
- 1 April 1992
Clopidogrel, like the homologous thienopyridine derivative ticlopidine, selectively inhibits platelet aggregation induced by ADP. We have previously described two nucleotide-binding sites on… Expand
Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism.
- M. Tsai, J. Koo, P. Yip, R. F. Colman, M. Segall, P. Howell
- Chemistry, Medicine
- Journal of molecular biology
- 13 July 2007
Adenylosuccinate lyase (ADL) catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR) to 5-aminoimidazole-4-carboxamide ribotide (AICAR) and fumarate, and of… Expand
Critical Role of Lys212 and Tyr140 in Porcine NADP-dependent Isocitrate Dehydrogenase*
- Tae-Kang Kim, P. Lee, R. F. Colman
- Chemistry, Medicine
- Journal of Biological Chemistry
- 5 December 2003
Lys212 and Tyr140 are close to the enzyme-bound isocitrate in the recently determined crystal structure of porcine NADP-specific isocitrate dehydrogenase (Ceccarelli, C., Grodsky, N. B., Ariyaratne,… Expand
Expression, purification, and characterization of stable, recombinant human adenylosuccinate lyase.
- P. Lee, R. F. Colman
- Biology, Medicine
- Protein expression and purification
- 1 February 2007
The full length human adenylosuccinate lyase gene was generated by a PCR method using a plasmid encoding a truncated human enzyme as template, and was cloned into a pET-14b vector. Human… Expand