Zobrazeno 1 - 10
of 11
pro vyhledávání: '"W J Herring"'
Publikováno v:
International Journal of Clinical Practice. 70:577-586
SummaryAim The aim of this study was to evaluate the efficacy and safety of preservative-free (PF) tafluprost compared with PF timolol in Indian subjects with open-angle glaucoma (OAG) or ocular hypertension. Methods This was a randomised, multicentr
Autor:
W. J. Herring, T. Woo, C. A. Assaid, R. J. Lupinacci, H. J. Lemmens, M. Blobner, K. S. Khuenl-Brady
Publikováno v:
Survey of Anesthesiology. 61:124
Autor:
W J Herring, David T. Chuang, D J Danner, Kim S. Lau, Jacinta L. Chuang, Rody P. Cox, M McKean
Publikováno v:
Journal of Biological Chemistry. 267:24090-24096
We have determined the structural organization of the dihydrolipoyl transacylase (E2) gene of the human branched chain alpha-keto acid dehydrogenase complex. The single copy E2 gene spans approximately 68 kilobases of genomic DNA. The complete coding
Publikováno v:
Biochemical medicine and metabolic biology. 49(3)
Maple syrup urine disease results from inherited defects in human nuclear genes for branched chain α-ketoacid dehydrogenase, a mitochondrial multienzyme complex. Thiamin pyrophosphate is necessary for complex activity and a thiamin-responsive form o
Publikováno v:
The Journal of biological chemistry. 267(33)
We have determined the structural organization of the dihydrolipoyl transacylase (E2) gene of the human branched chain alpha-keto acid dehydrogenase complex. The single copy E2 gene spans approximately 68 kilobases of genomic DNA. The complete coding
Publikováno v:
American journal of human genetics. 48(2)
Maple syrup urine disease in humans results from inherited defects in branched chain alpha-ketoacid dehydrogenase, a mitochondrial multienzyme complex. A variety of genetic changes may produce this phenotype by affecting the function of any of the th
Publikováno v:
Journal of Biological Chemistry. 264:14597-14600
Branched chain alpha-ketoacid dehydrogenase is a heteroprotein complex of mitochondria and commits the branched chain alpha-ketoacids to their catabolic fate. Inherited nuclear mutations in humans decrease the activity of this complex and result in m
Publikováno v:
Journal of Biological Chemistry. 264:7742-7746
A cDNA (1.6 kilobases) for branched chain acyltransferase (E2b) isolated from a human liver library encoded only the amino-terminal half of the protein (Hummel, K. B., Litwer, S., Bradford, A. P., Aitken, A., Danner, D. J., and Yeaman, S. J. (1988) J
Publikováno v:
The Journal of biological chemistry. 264(25)
Branched chain alpha-ketoacid dehydrogenase is a heteroprotein complex of mitochondria and commits the branched chain alpha-ketoacids to their catabolic fate. Inherited nuclear mutations in humans decrease the activity of this complex and result in m
Publikováno v:
The Journal of biological chemistry. 264(13)
A cDNA (1.6 kilobases) for branched chain acyltransferase (E2b) isolated from a human liver library encoded only the amino-terminal half of the protein (Hummel, K. B., Litwer, S., Bradford, A. P., Aitken, A., Danner, D. J., and Yeaman, S. J. (1988) J