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Page 1
Amino-acid sequence of the cytochrome-b5-like heme-binding domain from Hansenula anomala flavocytochrome b2.
Haumont PY, Thomas MA, Labeyrie F, Lederer F. Haumont PY, et al. Among authors: lederer f. Eur J Biochem. 1987 Dec 15;169(3):539-46. doi: 10.1111/j.1432-1033.1987.tb13642.x. Eur J Biochem. 1987. PMID: 3319613 Free article.
Its first 100 residues constitute the heme-binding core, which is homologous to cytochrome b5 [B. Guiard, O. Groudinsky & F. Lederer (1974) Proc. Natl Acad. Sci. USA 71, 2539-2543]. We report here the amino acid sequence of the heme-binding domain isolated by tr …
Its first 100 residues constitute the heme-binding core, which is homologous to cytochrome b5 [B. Guiard, O. Groudinsky & F. L …
The noncompetitive blocker [3H]chlorpromazine labels three amino acids of the acetylcholine receptor gamma subunit: implications for the alpha-helical organization of regions MII and for the structure of the ion channel.
Revah F, Galzi JL, Giraudat J, Haumont PY, Lederer F, Changeux JP. Revah F, et al. Among authors: lederer f. Proc Natl Acad Sci U S A. 1990 Jun;87(12):4675-9. doi: 10.1073/pnas.87.12.4675. Proc Natl Acad Sci U S A. 1990. PMID: 1693775 Free PMC article.
Complete amino acid sequence of flavocytochrome b2 from baker's yeast.
Lederer F, Cortial S, Becam AM, Haumont PY, Perez L. Lederer F, et al. Eur J Biochem. 1985 Oct 15;152(2):419-28. doi: 10.1111/j.1432-1033.1985.tb09213.x. Eur J Biochem. 1985. PMID: 3902473 Free article.
The primary structure of the former has been reported before [Ghrir, B., Becam, A. M. & Lederer, F. (1984) Eur. J. Biochem. 139, 59-74]. The amino acid sequence of the 197-residue fragment beta has now been established. ...
The primary structure of the former has been reported before [Ghrir, B., Becam, A. M. & Lederer, F. (1984) Eur. J. Biochem …
Escherichia coli tyrosyl- and methionyl-tRNA synthetases display sequence similarity at the binding site for the 3'-end of tRNA.
Hountondji C, Lederer F, Dessen P, Blanquet S. Hountondji C, et al. Among authors: lederer f. Biochemistry. 1986 Jan 14;25(1):16-21. doi: 10.1021/bi00349a003. Biochemistry. 1986. PMID: 3513822
Interestingly, the labeled TyrRS structure showed significant similarities to the structure around the lysine residue of E. coli methionyl-tRNA synthetase which is the most reactive toward tRNAMetf(ox) (lysine-335) [Hountondji, C., Blanquet, S., & Lederer, F. (1 …
Interestingly, the labeled TyrRS structure showed significant similarities to the structure around the lysine residue of E. coli methionyl-t …
397 results