N‐terminal methylation of proteins: Structure, function and specificity

[1]  M. Tokunaga,et al.  Position of the amino terminus of myosin light chain 1 and light chain 2 determined by electron microscopy with monoclonal antibody. , 1987, Journal of molecular biology.

[2]  R. Macnab,et al.  Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium , 1986, Journal of bacteriology.

[3]  R. M. Smith,et al.  The action of chymotrypsin on nucleosome cores. Histone products and conformational effects of limited digestion. , 1986, The Journal of biological chemistry.

[4]  J. V. Van Beeumen,et al.  Multiple forms of histone H2B from the nematode Caenorhabditis elegans. , 1986, The Biochemical journal.

[5]  I. Trayer,et al.  Characterization of the actin-binding site on the alkali light chain of myosin. , 1985, Biochimica et biophysica acta.

[6]  G. Schoolnik,et al.  Cloning and sequencing of a Moraxella bovis pilin gene , 1985, Journal of bacteriology.

[7]  J. Stewart,et al.  Amino-terminal processing of mutant forms of yeast iso-1-cytochrome c. The specificities of methionine aminopeptidase and acetyltransferase. , 1985, The Journal of biological chemistry.

[8]  I. Trayer,et al.  The widespread distribution of alpha-N-trimethylalanine as the N-terminal amino acid of light chains from vertebrate striated muscle myosins. , 1985, European journal of biochemistry.

[9]  R. Yount,et al.  Identification of an active site peptide of skeletal myosin after photoaffinity labeling with N-(4-azido-2-nitrophenyl)-2-aminoethyl diphosphate. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[10]  P. Sautière,et al.  Primary structure of histone H2B from gonads of the starfish Asterias rubens. Identification of an N-dimethylproline residue at the amino-terminal. , 1985, European journal of biochemistry.

[11]  N. Mckern,et al.  Amino acid sequence of pilin from Bacteroides nodosus (strain 198), the causative organism of ovine footrot , 1983, FEBS letters.

[12]  Y. Kyōgoku,et al.  N-Trimethylalanine, a novel blocked N-terminal residue of Tetrahymena histone H2B. , 1982, Journal of biochemistry.

[13]  I. Trayer,et al.  The occurrence of α‐N‐trimethylalanine as the N‐terminal amino acid of some myosin light chains , 1982 .

[14]  G. Pettigrew,et al.  A cytochrome c methyltransferase from Crithidia oncopelti. , 1982, The Biochemical journal.

[15]  B. Wittmann-Liebold,et al.  Purification and primary structure determination of the N-terminal blocked protein, L11, from Escherichia coli ribosomes. , 1980, European journal of biochemistry.

[16]  G. M. Smith,et al.  Identification of N,N-dimethylproline as the N-terminal blocking group of Crithidia oncopelti cytochrome c557. , 1980, European journal of biochemistry.

[17]  H. Matsubara,et al.  Amino acid sequence of cytochrome c3 from Desulfovibrio vulgaris, Miyazaki. , 1980, Journal of biochemistry.

[18]  L. Hood,et al.  Sequence of histone 2B of Drosophila melanogaster. , 1979, Biochemistry.

[19]  F. Lederer,et al.  Methylated amino acids in ribosomal proteins from Escherichia coli treated with ethionine and from a mutant lacking methylation of protein L11. , 1979, Biochimie.

[20]  J. S. Parkinson,et al.  Interaction of the cheC and cheZ gene products is required for chemotactic behavior in Escherichia coli. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[21]  K. Chen,et al.  Neisseria pili proteins: amino-terminal amino acid sequences and identification of an unusual amino acid. , 1978, Biochemistry.

[22]  L. Frost,et al.  N-methylphenylalanine at the N-terminus of pilin isolated from Pseudomonas aeruginosa K. , 1978, Nature.

[23]  B. Wittmann-Liebold,et al.  The primary structure of L11, the most heavily methylated protein from Escherichia coli ribosomes , 1977, FEBS letters.

[24]  F. Lederer,et al.  N-Trimethylalanine, a novel blocking group, found in E. coli ribosomal protein L11. , 1977, Biochemical and biophysical research communications.

[25]  B. Wittmann-Liebold,et al.  The primary structure of the initiation factor IF‐3 from Escherichia coli , 1977, FEBS letters.

[26]  F. Chang,et al.  Characterization of methylated neutral amino acids from Escherichia coli ribosomes , 1977, Journal of bacteriology.

[27]  J. Brosius,et al.  Occurrence of methylated amino acids as N-termini of proteins from Escherichia coli ribosomes. , 1977, Journal of molecular biology.

[28]  G. Pettigrew,et al.  Novel N-terminal protein blocking group identified as dimethylproline , 1977, Nature.

[29]  F. Chang,et al.  Identification and characterization of a new methylated amino acid in ribosomal protein L33 of Escherichiacoli , 1976 .

[30]  J. Brosius,et al.  The primary structure of protein L16 located at the peptidyltransferase center of Escherichia coli ribosomes , 1976, FEBS letters.

[31]  B. Wittmann-Liebold,et al.  Primary structure of protein L33 from the large subunit of the Escherichia coli ribosome , 1976, FEBS letters.

[32]  H. Noller,et al.  Identification of a ribosomal protein essential for peptidyl transferase activity. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[33]  W. Jencks,et al.  The Reactivity of Nucleophilic Reagents toward the p-Nitrophenyl Phosphate Dianion1 , 1965 .

[34]  S. Tsunasawa,et al.  [14] Amino-terminal acetylation of proteins: An overview , 1984 .

[35]  F Wold,et al.  In vivo chemical modification of proteins (post-translational modification). , 1981, Annual review of biochemistry.

[36]  H. Klein,et al.  N‐terminal sequences of Escherichia coli and potato phosphorylase , 1980, FEBS letters.

[37]  W. N. Strickland,et al.  The complete amino-acid sequence of histone H2B from the mollusc Patella granatina. , 1979, European Journal of Biochemistry.

[38]  K. Sletten,et al.  Purification and N‐terminal sequence of a fimbrial protein fromMoraxella nonliquefaciens , 1977 .

[39]  M. O. Dayhoff,et al.  Atlas of protein sequence and structure , 1965 .