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Journal of Molecular Biology|July 20, 1990
High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes cG V Louie, G D BrayerJournal of Molecular Biology|November 20, 1989
A polypeptide chain-refolding event occurs in the Gly82 variant of yeast iso-1-cytochrome cG V Louie, G D BrayerJournal of Molecular Biology|July 20, 1990
High-resolution three-dimensional structure of horse heart cytochrome cG W Bushnell, G V Louie, G D BrayerJournal of Molecular Biology|January 20, 1988
Yeast iso-1-cytochrome c. A 2.8 A resolution three-dimensional structure determinationG V Louie, W L Hutcheon, G D BrayerMolecular Cell|July 11, 1998
Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptorG V Louie, W Yang, M E Bowman, et al.Biochemistry|October 4, 1988
Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this positionG V Louie, G J Pielak, M Smith, et al.Biochemistry|January 10, 1995
Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome cT P Lo, J G Guillemette, G V Louie, et al.Human Molecular Genetics|May 1, 1994
Identification of five novel mutations in the porphobilinogen deaminase geneC S Mgone, W G Lanyon, M R Moore, et al.Human Genetics|December 1, 1993
Detection of a high mutation frequency in exon 12 of the porphobilinogen deaminase gene in patients with acute intermittent porphyriaC S Mgone, W G Lanyon, M R Moore, et al.The Journal of Biological Chemistry|November 5, 1985
Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIaD E Cool, C J Edgell, G V Louie, et al.Pageof 2