{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T02:15:23Z","timestamp":1772763323943,"version":"3.50.1"},"reference-count":141,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[1996,1,1]],"date-time":"1996-01-01T00:00:00Z","timestamp":820454400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[1996,1]]},"DOI":"10.1016\/s0300-9084(96)80001-0","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T11:32:04Z","timestamp":1027596724000},"page":"543-554","source":"Crossref","is-referenced-by-count":47,"title":["Molecular recognition governing the initiation of translation in Escherichia coli. A review"],"prefix":"10.1016","volume":"78","author":[{"given":"E","family":"Schmitt","sequence":"first","affiliation":[]},{"given":"JM","family":"Guillon","sequence":"additional","affiliation":[]},{"given":"T","family":"Meinnel","sequence":"additional","affiliation":[]},{"given":"Y","family":"Mechulam","sequence":"additional","affiliation":[]},{"given":"F","family":"Dardel","sequence":"additional","affiliation":[]},{"given":"S","family":"Blanquet","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0300-9084(96)80001-0_BIB1","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1016\/0300-9084(93)90005-D","article-title":"Methionine as translation start signal: a review of the enzymes of the pathway in Escherichia coli","volume":"75","author":"Meinnel","year":"1993","journal-title":"Biochimie"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB2","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/0022-2836(86)90165-8","article-title":"Information content of binding sites on nucleotide sequences","volume":"188","author":"Schneider","year":"1986","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB3","doi-asserted-by":"crossref","first-page":"1342","DOI":"10.1073\/pnas.71.4.1342","article-title":"The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites","volume":"71","author":"Shine","year":"1974","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB4","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1093\/nar\/22.7.1287","article-title":"Quantitative analysis of ribosome binding sites in E coli","volume":"22","author":"Barrick","year":"1994","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB5","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/0022-2836(91)90875-7","article-title":"Influence of mRNA determinants on translation initiation in Escherichia coli","volume":"218","author":"Hartz","year":"1991","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB6","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1128\/jb.175.4.993-1000.1993","article-title":"The Escherichia coli fmt gene, encoding methionyl-transfer RNAfMet formyltransferase, escapes metabolic control","volume":"175","author":"Meinnel","year":"1993","journal-title":"J Bacteriol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB7","doi-asserted-by":"crossref","first-page":"4953","DOI":"10.1093\/nar\/22.23.4953","article-title":"Determination of the optimal aligned spacing between the Shine-Dalgarno sequence and the translation initiation codon of Escherichia coli mRNAs","volume":"22","author":"Chen","year":"1994","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB8","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/0022-2836(91)90876-8","article-title":"Detection of Escherichia coli ribosome binding at translation initiation sites in the absence of tRNA","volume":"218","author":"Hartz","year":"1991","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB9","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0079-6603(08)60707-2","article-title":"Control of prokaryotic translational initiation by mRNA secondary structure","volume":"38","author":"de Smit","year":"1990","journal-title":"Progr Nucleic Acid Res Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB10","doi-asserted-by":"crossref","first-page":"6427","DOI":"10.1073\/pnas.85.17.6427","article-title":"Selection of the mRNA translation initiation region by Escherichia coli ribosomes","volume":"85","author":"Calogero","year":"1988","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB11","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/0168-9525(94)90057-4","article-title":"Prokaryotic translation: the interactive pathway leading to initiation","volume":"10","author":"McCarthy","year":"1994","journal-title":"Trends Genet"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB12","doi-asserted-by":"crossref","first-page":"1719","DOI":"10.1093\/nar\/18.7.1719","article-title":"The initiation of translation in E coli: apparent base pairing between the 16S rRNA and downstream sequences of the mRNA","volume":"18","author":"Sprengart","year":"1990","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB13","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1002\/j.1460-2075.1996.tb00399.x","article-title":"The downstream box: an efficient and independent translation initiation signal in Escherichia coli","volume":"15","author":"Sprengart","year":"1996","journal-title":"EMBO J"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB14","doi-asserted-by":"crossref","first-page":"3402","DOI":"10.1021\/bi00465a037","article-title":"The anti Shine-Dalgarno region in Escherichia coli 16S ribosomal RNA is not essential for the correct selection of translational starts","volume":"29","author":"Melan\u00e7on","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB15","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/0022-2836(88)90601-8","article-title":"What constitutes the signal for the initiation of protein synthesis on Escherichia coli mRNAs?","volume":"204","author":"Dreyfus","year":"1988","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB16","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1146\/annurev.bi.57.070188.001215","article-title":"Post-transcriptional regulatory mechanisms in E coli","volume":"57","author":"Gold","year":"1988","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB17","article-title":"Role of the initiation factors in E coli initiation of translation","author":"Gualerzi","year":"1986"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB18","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1016\/S0022-2836(66)80150-X","article-title":"The role of N-formyl-methionyl-sRNA in protein biosynthesis","volume":"17","author":"Clark","year":"1966","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB19","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1016\/S0022-2836(64)80164-9","article-title":"N-formyl-methionyl-S-RNA","volume":"8","author":"Marcker","year":"1964","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB20","doi-asserted-by":"crossref","first-page":"4507","DOI":"10.1128\/jb.175.14.4507-4514.1993","article-title":"Importance of formylability and anticodon stem sequence to give tRNAMet an initiator identity in Escherichia coli","volume":"175","author":"Guillon","year":"1993","journal-title":"J Bacteriol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB21","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1073\/pnas.88.1.291","article-title":"Selection of suppressor methionyl-tRNA synthetases: Mapping the tRNA anticodon binding site","volume":"88","author":"Meinnel","year":"1991","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB22","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1006\/jmbi.1993.1540","article-title":"Two acidic residues of Escherichia coli methionyl-transfer RNA synthetase act as negative discriminants towards the binding of non-cognate transfer RNA anticodons","volume":"233","author":"Schmitt","year":"1993","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB23","doi-asserted-by":"crossref","first-page":"1586","DOI":"10.1073\/pnas.87.4.1586","article-title":"Initiation of protein synthesis from a termination codon","volume":"87","author":"Varshney","year":"1990","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB24","doi-asserted-by":"crossref","first-page":"18018","DOI":"10.1016\/S0021-9258(18)55231-5","article-title":"Mutants of initiator tRNA that function both as initiators and elongators","volume":"266","author":"Varshney","year":"1991","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB25","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1073\/pnas.84.2.334","article-title":"Escherichia coli formylmethionine tRNA: Mutations in GGGCCC sequence conserved in anticodon stem of initiator tRNAs affect initiation of protein synthetis and conformation of anticodon loop","volume":"84","author":"Seong","year":"1987","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB26","doi-asserted-by":"crossref","first-page":"8859","DOI":"10.1073\/pnas.84.24.8859","article-title":"Mutants of Escherichia coli formylmethionine tRNA: A single base change enables initiator tRNA to act as an elongator in vitro","volume":"84","author":"Seong","year":"1987","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB27","doi-asserted-by":"crossref","first-page":"2305","DOI":"10.1073\/pnas.90.6.2305","article-title":"From elongator tRNA to initiator tRNA","volume":"90","author":"Varshney","year":"1993","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB28","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1038\/286346a0","article-title":"Three-dimensional structure of E coli initiator tRNAfMet","volume":"286","author":"Woo","year":"1980","journal-title":"Nature"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB29","doi-asserted-by":"crossref","first-page":"3289","DOI":"10.1073\/pnas.76.7.3289","article-title":"Initiator tRNAs have a unique anticodon loop conformation","volume":"76","author":"Wrede","year":"1979","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB30","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/S0022-2836(05)80331-6","article-title":"Crystallographic study at 2.5 \u00c5 resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP","volume":"216","author":"Brunie","year":"1990","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB31","doi-asserted-by":"crossref","first-page":"6755","DOI":"10.1073\/pnas.80.22.6755","article-title":"Anticodon loop size and sequence requirements for recognition of formylmethionine tRNA by methionyl-tRNA synthetase","volume":"80","author":"Schulman","year":"1983","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB32","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1126\/science.3055296","article-title":"Anticodon switching changes the identity of methionine and valine transfer RNAs","volume":"242","author":"Schulman","year":"1988","journal-title":"Science"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB33","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/0022-2836(91)90003-O","article-title":"Binding of the anticodon domain of tRNAfMet to Escherichia coli methionyl-tRNA synthetase","volume":"220","author":"Meinnel","year":"1991","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB34","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1006\/jmbi.1993.1005","article-title":"Critical role of the acceptor stem of tRNAsMet in their aminoacylation by Escherichia coli methionyl-tRNA synthetase","volume":"229","author":"Meinnel","year":"1993","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB35","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/0022-2836(89)90507-X","article-title":"Identification of an amino acid region supporting specific methionyl-tRNA synthetase:tRNA recognition","volume":"208","author":"Mellot","year":"1989","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB36","doi-asserted-by":"crossref","first-page":"15681","DOI":"10.1021\/bi00048a012","article-title":"Crucial role of an idiosyncratic insertion in the Rossman fold of class I aminoacyl-tRNA synthetases: the case of methionyl-tRNA synthetase","volume":"34","author":"Fourmy","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB37","doi-asserted-by":"crossref","first-page":"13026","DOI":"10.1021\/bi00211a011","article-title":"C-terminal peptide appendix in a class-I transfer RNA synthetase needed for acceptor-helix contacts, microhelix aminoacylation","volume":"32","author":"Kim","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB38","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1006\/jmbi.1993.1352","article-title":"Mapping of the zinc binding domain of Escherichia coli methionyl-tRNA synthetase","volume":"231","author":"Fourmy","year":"1993","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB39","doi-asserted-by":"crossref","first-page":"1078","DOI":"10.1006\/jmbi.1993.1353","article-title":"Methionyl-tRNA synthetase zinc binding site. 3-D structure and homology with rubredoxin and gag retroviral proteins","volume":"231","author":"Fourmy","year":"1993","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB40","doi-asserted-by":"crossref","first-page":"7113","DOI":"10.1021\/bi00396a037","article-title":"Covalent coupling of 4-thiouridine in the initiator methionine tRNA to specific lysine residues in Escherichia coli methionyl-tRNA synthetase","volume":"26","author":"Leon","year":"1987","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB41","doi-asserted-by":"crossref","first-page":"2220","DOI":"10.1021\/bi00461a003","article-title":"Identification of the tRNA anticodon recognition site of Escherichia coli methionyl-tRNA synthetase","volume":"29","author":"Ghosh","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB42","doi-asserted-by":"crossref","first-page":"11767","DOI":"10.1021\/bi00115a005","article-title":"Arginine 395 is required for efficient in vivo and in vitro aminoacylation of tRNAs by Escherichia coli methionyl-tRNA synthetase","volume":"30","author":"Ghosh","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB43","doi-asserted-by":"crossref","first-page":"4263","DOI":"10.1021\/bi00470a001","article-title":"Initiation of protein synthesis with non-methionine amino acids","volume":"29","author":"Chattapadhyay","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB44","doi-asserted-by":"crossref","first-page":"3872","DOI":"10.1073\/pnas.88.9.3872","article-title":"Anticodon-dependent aminoacylation of a noncognate tRNA with isoleucine, valine, and phenylalanine in vivo","volume":"88","author":"Pallanck","year":"1991","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB45","doi-asserted-by":"crossref","first-page":"7819","DOI":"10.1128\/jb.174.23.7819-7826.1992","article-title":"Role of methionine and formylation of initiator tRNA in initiation of protein synthesis in Escherichia coli","volume":"174","author":"Varshney","year":"1992","journal-title":"J Bacteriol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB46","doi-asserted-by":"crossref","first-page":"18012","DOI":"10.1016\/S0021-9258(18)55230-3","article-title":"Structural and sequence elements important for recognition of Escherichia coli formylmethionine tRNA by methionyl-tRNA transformylase are clustered in the acceptor stem","volume":"266","author":"Lee","year":"1991","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB47","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/0022-2836(92)91000-F","article-title":"Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNAMetf formyltransferase","volume":"224","author":"Guillon","year":"1992","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB48","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1111\/j.1432-1033.1980.tb04524.x","article-title":"Methionyl-transfer-RNA transformylase from Escherichia coli. Purification and characterisation","volume":"105","author":"Kahn","year":"1980","journal-title":"Eur J Biochem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB49","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/0076-6879(84)06013-4","article-title":"Properties and specificity of methionyl-tRNAMetf formyltransferase from Escherichia coli","volume":"106","author":"Blanquet","year":"1984","journal-title":"Methods Enzymol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB50","doi-asserted-by":"crossref","first-page":"7668","DOI":"10.1021\/bi00023a013","article-title":"Heteronuclear NMR studies of the interactions of the 15N-labeled methionine specific transfer RNAs with methionyl-tRNA transformylase","volume":"34","author":"Wallis","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB51","doi-asserted-by":"crossref","first-page":"9262","DOI":"10.1073\/pnas.89.19.9262","article-title":"Striking effects of coupling mutations in the acceptor stem on recognition of tRNAs by Escherichia coli Met-tRNA synthetase and Met-tRNA transformylase","volume":"89","author":"Lee","year":"1992","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB52","doi-asserted-by":"crossref","first-page":"7149","DOI":"10.1073\/pnas.90.15.7149","article-title":"The discriminator base influences tRNA structure at the end of the acceptor stem and possibly its interaction with proteins","volume":"90","author":"Lee","year":"1993","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB53","doi-asserted-by":"crossref","first-page":"11467","DOI":"10.1073\/pnas.91.24.11467","article-title":"NMR analysis of tRNA acceptor stem microhelices: discriminator base change affects tRNA conformation at the 3' end","volume":"91","author":"Viani-Puglisi","year":"1994","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB54","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/0014-5793(73)80672-6","article-title":"Formylation of mischarged E coli tRNAMetf","volume":"30","author":"Gieg\u00e9","year":"1973","journal-title":"FEBS Lett"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB55","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1002\/prot.14","article-title":"Crystallization and preliminary X-Ray analysis of Escherichia coli methionyl tRNAfMet formyltransferase","volume":"25","author":"Schmitt","year":"1996","journal-title":"Proteins"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB56","doi-asserted-by":"crossref","first-page":"4749","DOI":"10.1002\/j.1460-2075.1996.tb00852.x","article-title":"Structure of crystalline Escherichia coli methionyl-tRNAfMet formyltransferase: comparison with glycinamide ribonucleotide formyltransferase","volume":"17","author":"Schmitt","year":"1996","journal-title":"EMBO J"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB57","doi-asserted-by":"crossref","first-page":"4242","DOI":"10.1016\/S0021-9258(17)34710-5","article-title":"N10-formyltetrahydrofolate is the formyl donor for glycinamide ribonucleotide transformylase in Escherichia coli","volume":"253","author":"Dev","year":"1978","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB58","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1002\/j.1460-2075.1993.tb05726.x","article-title":"OB (oligonucleotide\/oligosaccharide)-fold: common structural and functional solution for non-homologous sequences","volume":"12","author":"Murzin","year":"1993","journal-title":"EMBO J"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB59","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1126\/science.154.3748.524","article-title":"Formylmethionyl-tRNA dependence of aminoacid incorporation in extracts of trimethoprim-treated Escherichia coli","volume":"154","author":"Eisendstadt","year":"1966","journal-title":"Science"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB60","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1128\/JB.114.1.309-322.1973","article-title":"Growth and initiation of protein synthesis in Escherichia coli in the presence of trimethoprim","volume":"114","author":"Harvey","year":"1973","journal-title":"J Bacteriol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB61","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1016\/0003-9861(79)90366-7","article-title":"DNA-directed in vivo synthesis of \u03b2-galactosidase: Requirement for formylation of methionyl-tRNAMetf","volume":"195","author":"Kung","year":"1979","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB62","doi-asserted-by":"crossref","first-page":"4294","DOI":"10.1128\/jb.174.13.4294-4301.1992","article-title":"Disruption of the gene for Met-tRNAMetf formyltransferase severely impairs the growth of Escherichia coli","volume":"174","author":"Guillon","year":"1992","journal-title":"J Bacteriol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB63","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/0022-2836(91)90017-Z","article-title":"A severely truncated form of translation initiation factor 2 supports growth of Escherichia coli","volume":"220","author":"Laalami","year":"1991","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB64","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1016\/0006-291X(79)91989-2","article-title":"Specific interaction of initiator factor IF2 of E coli with formylmethionyl-tRNAMetf","volume":"91","author":"Petersen","year":"1979","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB65","doi-asserted-by":"crossref","first-page":"3338","DOI":"10.1016\/S0021-9258(17)33442-7","article-title":"Interaction of initiation factor 2 with initiator tRNA","volume":"251","author":"Sundari","year":"1976","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB66","doi-asserted-by":"crossref","first-page":"1899","DOI":"10.1101\/gad.3.12a.1899","article-title":"Selection of the initiator tRNA by Escherichia coli initiation factors","volume":"3","author":"Hartz","year":"1989","journal-title":"Genes Dev"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB67","doi-asserted-by":"crossref","first-page":"12203","DOI":"10.1074\/jbc.270.20.12203","article-title":"Mutants of Escherichia coli initiator tRNA defective in initiation. Effects of overproduction of methionyl-tRNA transformylase and the initiation factors IF2 ans IF3","volume":"270","author":"Mangroo","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB68","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.271.37.22321","article-title":"Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli","author":"Guillon","year":"1996","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB69","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1016\/S0021-9258(19)68177-9","article-title":"The binding of fluorescein-labeled protein synthesis initiation factor 2 to E coli 30S ribosomal subunits determined by fluorescence polarization","volume":"257","author":"Weiel","year":"1982","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB70","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1146\/annurev.bi.51.070182.004253","article-title":"Initiation factors in protein biosynthesis","volume":"51","author":"Maitra","year":"1982","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB71","doi-asserted-by":"crossref","first-page":"10119","DOI":"10.1016\/S0021-9258(18)33992-9","article-title":"Kinetic studies on the interaction of chain initiation factor 3 with E coli 70S ribosomes and subunits","volume":"257","author":"Goss","year":"1982","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB72","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0014-5793(86)80637-8","article-title":"Procaryotic initiation factor 2 acts at the level of the 30S subunit. A fluorescence stopped-flow study","volume":"202","author":"Gualerzi","year":"1986","journal-title":"FEBS Lett"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB73","doi-asserted-by":"crossref","first-page":"5881","DOI":"10.1021\/bi00477a001","article-title":"Initiation of mRNA translation in prokaryotes","volume":"29","author":"Gualerzi","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB74","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/0014-5793(86)81488-0","article-title":"Mechanism of translational initiation in procaryotes. Evidence for a direct effect of IF2 on the activity of the 30S ribosomal subunit","volume":"207","author":"Canonaco","year":"1986","journal-title":"FEBS Lett"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB75","doi-asserted-by":"crossref","first-page":"20363","DOI":"10.1016\/S0021-9258(19)47072-5","article-title":"The solution structure of the Escherichia coli initiator tRNA and its interaction with initiation factor 2 and the ribosomal 30S subunit","volume":"264","author":"Wakao","year":"1989","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB76","doi-asserted-by":"crossref","first-page":"7787","DOI":"10.1073\/pnas.81.24.7787","article-title":"Sequence of the initiation factor IF2 gene: unusual protein features and homologies with elongation factors","volume":"81","author":"Sacerdot","year":"1984","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB77","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/0022-2836(92)91026-L","article-title":"Both forms of translational initiation factor IF2 (\u03b1 and \u03b2) are required for maximal growth of Escherichia coli","volume":"225","author":"Sacerdot","year":"1992","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB78","doi-asserted-by":"crossref","first-page":"1636","DOI":"10.1016\/S0021-9258(18)55305-9","article-title":"Molecular dissection of translation initiation factor IF2","volume":"266","author":"Gualerzi","year":"1991","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB79","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1111\/j.1365-2958.1994.tb00309.x","article-title":"In vivo study of engineered G-domain mutants of Escherichia coli translation initiation factor IF2","volume":"11","author":"Laalami","year":"1994","journal-title":"Mol Microbiol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB80","doi-asserted-by":"crossref","first-page":"2978","DOI":"10.1021\/bi9519415","article-title":"Topography of the Escherichia coli initiation factor 2\/fMet-tRNAfMet complex as studied by cross linking","volume":"35","author":"Yusupova","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB81","article-title":"Crystallization and preliminary X-ray diffraction data of the IF2 C-terminal fragment from B stearothermophilus complexed with fMet-tRNAfMet","author":"F\u00f6rster","year":"1995","journal-title":"16th International tRNA Workshop, May 27\u2013June 1, Madison, USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB82","doi-asserted-by":"crossref","first-page":"7102","DOI":"10.1016\/S0021-9258(19)42080-2","article-title":"Structural requirements for recognition of Escherichia coli initiator and non-initiatortransferribonucleic acids by bacterial T factor","volume":"249","author":"Schulman","year":"1974","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB83","doi-asserted-by":"crossref","first-page":"6433","DOI":"10.1021\/bi00344a019","article-title":"Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5'-triphosphate-aminoacyl-tRNA complexes","volume":"24","author":"Louie","year":"1985","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB84","doi-asserted-by":"crossref","first-page":"4268","DOI":"10.1021\/bi00470a002","article-title":"Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu GTP: evidence for a new functional role for elongation factor Tu in protein biosynthesis","volume":"29","author":"Janiak","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB85","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/S0300-9084(86)80163-8","article-title":"Interaction between initiator Met-tRNAfMet and elongation factor EF-Tu from E coli","volume":"68","author":"Hansen","year":"1986","journal-title":"Biochimie"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB86","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1016\/0300-9084(87)90214-8","article-title":"Interaction between nonformylated initiator Met-tRNAfMet and the ribosomal A-site from Escherichia coli","volume":"69","author":"Hansen","year":"1987","journal-title":"Biochimie"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB87","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1016\/S0021-9258(19)41930-3","article-title":"The structural basis for the resistance of Escherichia coli formylmethionyl transfer ribonucleic acid to cleavage by Escherichia coli peptidyl transfer ribonucleic acid hydrolase","volume":"250","author":"Schulman","year":"1975","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB88","doi-asserted-by":"crossref","first-page":"4025","DOI":"10.1093\/nar\/21.17.4025","article-title":"Role of the 1\u201372 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolase","volume":"21","author":"Dutka","year":"1993","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB89","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1128\/JB.137.1.694-696.1979","article-title":"Accumulation of peptidyl tRNA is lethal to Escherichia coli","volume":"137","author":"Menninger","year":"1979","journal-title":"J Bacteriol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB90","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1016\/S0022-2836(68)80013-0","article-title":"Studies on polynucleotides. LXXXVI. Enzymic hydrolysis of N-acylaminoacyl-transfer RNA","volume":"35","author":"K\u00f6ssel","year":"1968","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB91","doi-asserted-by":"crossref","first-page":"2073","DOI":"10.1016\/S0021-9258(18)46054-1","article-title":"Purification and initial characterization of peptidyl-tRNA hydrolase from rabbit reticulocytes","volume":"267","author":"Gross","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB92","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1038\/newbio240245a0","article-title":"Mutant E coli strain with temperature sensitive peptidyl-transfer RNA hydrolase","volume":"240","author":"Atherly","year":"1972","journal-title":"Nature New Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB93","doi-asserted-by":"crossref","first-page":"3549","DOI":"10.1002\/j.1460-2075.1991.tb04919.x","article-title":"Peptidyl-tRNA hydrolase is involved in \u03bb inhibition of host protein synthesis","volume":"10","author":"Garcia-Villegas","year":"1991","journal-title":"EMBO J"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB94","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.1038\/2191016a0","article-title":"Function of three protein factors and ribosomal subunits in the initiation of protein synthesis","volume":"219","author":"Revel","year":"1968","journal-title":"Nature"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB95","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1016\/0022-2836(75)90215-6","article-title":"Light-scattering studies showing the effect of initiation factors on the reversible dissociation of E coli ribosomes","volume":"94","author":"Godefroy-Colburn","year":"1975","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB96","doi-asserted-by":"crossref","first-page":"2035","DOI":"10.1093\/nar\/11.7.2035","article-title":"Nuclease mapping of the secondary structure of the 49-nucleotide 3' terminal cloacin fragment of Escherichia coli 16S RNA and its interaction with initiation factor 3","volume":"11","author":"Wickstrom","year":"1983","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB97","doi-asserted-by":"crossref","first-page":"4803","DOI":"10.1093\/nar\/14.12.4803","article-title":"Cross-linking of initiation factor IF3 to Escherichia coli 30S ribosomal subunit by trans-diamminedichloro-platinum (II): characterization of two cross-linking sites in 16S rRNA; a possible way of functioning for IF3","volume":"14","author":"Ehresmann","year":"1986","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB98","doi-asserted-by":"crossref","first-page":"1312","DOI":"10.1016\/0006-291X(71)90162-8","article-title":"Initiation factor dependent release of aminoacyl-tRNAs from complexes of 30S ribosomal subunits, synthetic polynucleotide and aminoacyl-tRNA","volume":"45","author":"Gualerzi","year":"1971","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB99","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1111\/j.1432-1033.1976.tb10726.x","article-title":"Specificity and properties of the destabilization induced by initiation factor IF3 of ternary complexes of the 30S ribosomal subunit, aminoacyl-tRNA and polynucleotides","volume":"67","author":"Risuleo","year":"1976","journal-title":"Eur J Biochem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB100","doi-asserted-by":"crossref","first-page":"1790","DOI":"10.1101\/gad.4.10.1790","article-title":"Domains of initiator tRNA and initiation codon crucial for initiator tRNA selection by Escherichia coli IF3","volume":"4","author":"Hartz","year":"1990","journal-title":"Genes Dev"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB101","doi-asserted-by":"crossref","first-page":"5681","DOI":"10.1021\/bi00645a005","article-title":"Cross-linking of Escherichia coli initiation factor IF-3 to the RNA moiety of the 30S ribosomal subunits","volume":"16","author":"Pon","year":"1977","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB102","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1021\/bi00649a012","article-title":"The role of 16S rRNA in ribosomal binding of IF3","volume":"15","author":"Pon","year":"1976","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB103","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1016\/0006-291X(73)91007-3","article-title":"Nature of the ribosomal binding site for initiation factor 3","volume":"52","author":"Gualerzi","year":"1973","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB104","doi-asserted-by":"crossref","first-page":"7505","DOI":"10.1021\/bi00445a002","article-title":"Escherichia coli initiation factor 3 protein binding to 30S ribosomal subunits alters the accessibility of nucleotides within the conserved central region of 16S rRNA","volume":"28","author":"Muralikrishna","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB105","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/S0022-2836(95)80042-5","article-title":"Specific protection of 16S RNA by translational initiation factors","volume":"248","author":"Moazed","year":"1995","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB106","doi-asserted-by":"crossref","first-page":"10526","DOI":"10.1016\/S0021-9258(19)70495-5","article-title":"Photochemical cross-linking of initiation factor-3 to Escherichia coli 30S ribosomal subunits","volume":"255","author":"MacKeen","year":"1980","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB107","doi-asserted-by":"crossref","first-page":"4693","DOI":"10.1074\/jbc.271.9.4693","article-title":"Mutations at two invariant nucleotides in the 3'-minor domain of Escherichia coli 16S rRNA affecting translational initiation and initiation factor 3 function","volume":"271","author":"Firpo","year":"1996","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB108","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/0300-9084(94)90111-2","article-title":"The N-terminal half of initiation factor IF3 is folded as a stable independent domain","volume":"76","author":"Fortier","year":"1994","journal-title":"Biochimie"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB109","doi-asserted-by":"crossref","first-page":"1670","DOI":"10.1021\/bi00549a023","article-title":"Structure-function relationships in Escherichia coli initiation factors: role of tyrosine residues in ribosomal binding and functional activity of IF3","volume":"19","author":"Bruhns","year":"1980","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB110","doi-asserted-by":"crossref","first-page":"11984","DOI":"10.1021\/bi00163a005","article-title":"Structure-function analysis of Escherichia coli translation initiation factor IF3: tyrosine 107 and lysine 110 are required for ribosome binding","volume":"31","author":"De Bellis","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB111","doi-asserted-by":"crossref","first-page":"4905","DOI":"10.1016\/S0021-9258(19)69342-7","article-title":"Structure-function relationships in Escherichia coli initiation factors. Identification of a lysine residue in the ribosomal binding site of initiation factor IF3 by site-specific chemical modification with pyridoxal phosphate","volume":"256","author":"Ohsawa","year":"1981","journal-title":"J Biol Chem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB112","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1006\/jmbi.1995.0615","article-title":"Solution structure of the ribosome-binding domain of E coli translation initiation factor IF3. Homology with the UIA protein of the eukaryotic spliceosome","volume":"254","author":"Garcia","year":"1995","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB113","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1111\/j.1432-1033.1995.tb20276.x","article-title":"1H and 15N resonance assignment and structure of the N-terminal domain of Escherichia coli initiation factor 3","volume":"228","author":"Garcia","year":"1995","journal-title":"Eur J Biochem"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB114","doi-asserted-by":"crossref","first-page":"6183","DOI":"10.1021\/bi00018a022","article-title":"Prokaryotic initiation factor IF3 is an elongated protein consisting of two crystallizable domains","volume":"34","author":"Kycia","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB115","doi-asserted-by":"crossref","first-page":"4056","DOI":"10.1002\/j.1460-2075.1995.tb00077.x","article-title":"X-ray crystallography shows that translational initiation factor IF3 consists of two compact \u03b1\/\u03b2 domains linked by an a helix","volume":"14","author":"Biou","year":"1995","journal-title":"EMBO J"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB116","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/S0022-2836(67)80091-3","article-title":"Amidohydrolase activity of Escherichia coli extracts with formylated amino acids and dipeptides as substrates","volume":"28","author":"Fry","year":"1967","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB117","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1016\/0022-2836(68)90307-0","article-title":"On the release of the formyl group from nascent protein","volume":"33","author":"Adams","year":"1968","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB118","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1016\/S0022-2836(63)80096-0","article-title":"The NH2-terminal residue of the proteins from cell-free extract of E coli","volume":"7","author":"Waller","year":"1963","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB119","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1128\/jb.169.2.751-757.1987","article-title":"Processing of the initiation methionine from proteins: Properties of the Escherichia coli methionine aminopeptidase and its gene structure","volume":"169","author":"Ben-Bassat","year":"1987","journal-title":"J Bacteriol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB120","doi-asserted-by":"crossref","first-page":"8247","DOI":"10.1073\/pnas.86.21.8247","article-title":"Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid","volume":"86","author":"Hirel","year":"1989","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB121","doi-asserted-by":"crossref","first-page":"3907","DOI":"10.1021\/bi00066a009","article-title":"Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme","volume":"32","author":"Roderick","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB122","doi-asserted-by":"crossref","first-page":"4071","DOI":"10.1128\/jb.171.7.4071-4072.1989","article-title":"Methionine aminopeptidase gene of Escherichia coli is essential for cell growth","volume":"171","author":"Chang","year":"1989","journal-title":"J Bacteriol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB123","doi-asserted-by":"crossref","first-page":"914","DOI":"10.1002\/j.1460-2075.1994.tb06335.x","article-title":"Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation","volume":"13","author":"Mazel","year":"1994","journal-title":"EMBO J"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB124","doi-asserted-by":"crossref","first-page":"7737","DOI":"10.1128\/jb.175.23.7737-7740.1993","article-title":"Evidence that peptide deformylase and methionyl-tRNAMetf formyltransferase are encoded within the same operon in Escherichia coli","volume":"175","author":"Meinnel","year":"1993","journal-title":"J Bacteriol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB125","doi-asserted-by":"crossref","first-page":"7387","DOI":"10.1128\/jb.176.23.7387-7390.1994","article-title":"Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA-Metf formyltransferase","volume":"176","author":"Meinnel","year":"1994","journal-title":"J Bacteriol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB126","doi-asserted-by":"crossref","first-page":"1883","DOI":"10.1128\/jb.177.7.1883-1887.1995","article-title":"Enzymatic properties of Escherichia coli peptide deformylase","volume":"177","author":"Meinnel","year":"1995","journal-title":"J Bacteriol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB127","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1006\/jmbi.1995.0609","article-title":"Mapping of the active site zinc ligands of peptide deformylase","volume":"254","author":"Meinnel","year":"1995","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB128","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1006\/jmbi.1996.0521","article-title":"The solution structure of peptide deformylase reveals a new class of zinc metalloproteases","volume":"262","author":"Meinnel","year":"1996","journal-title":"J Mol Biol"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB129","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/0014-5793(96)00357-2","article-title":"The C-terminal domain of peptide deformylase is disordered and dispensable for activity","volume":"385","author":"Meinnel","year":"1996","journal-title":"FEBS Lett"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB130","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1021\/bi00829a059","article-title":"Deformylation and protein synthesis","volume":"8","author":"Livingston","year":"1969","journal-title":"Biochemistry"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB131","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/0005-2787(69)90261-5","article-title":"Kinetics of maturation of the amino termini of the cell proteins of Escherichia coli","volume":"174","author":"Pine","year":"1969","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB132","first-page":"323","article-title":"A family of RNA binding proteins: the aminoacyl-tRNA synthetases","author":"Mechulam","year":"1995"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB133","first-page":"251","article-title":"Aminoacyl-tRNA synthetases: general features","author":"Meinnel","year":"1995"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB134","doi-asserted-by":"crossref","first-page":"2945","DOI":"10.1002\/j.1460-2075.1995.tb07294.x","article-title":"Macromolecular recognition through electrostatic repulsion","volume":"14","author":"Bedouelle","year":"1995","journal-title":"EMBO J"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB135","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1038\/344787a0","article-title":"Relaxation of a transfer RNA specificity by removal of modified nucleotides","volume":"344","author":"Perret","year":"1990","journal-title":"Nature (Lond)"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB136","doi-asserted-by":"crossref","first-page":"1696","DOI":"10.1126\/science.2047878","article-title":"Identity elements for specific aminoacylation of yeast tRNAAsp by cognate aspartyl-tRNA synthetase","volume":"252","author":"Putz","year":"1991","journal-title":"Science"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB137","doi-asserted-by":"crossref","first-page":"5795","DOI":"10.1002\/j.1460-2075.1994.tb06923.x","article-title":"Complete DNA sequence of yeast chromosome II","volume":"13","author":"Feldmann","year":"1994","journal-title":"EMBO J"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB138","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1126\/science.3051379","article-title":"tRNAiMet functions in directing the scanning ribosome to the start site of translation","volume":"242","author":"Cigan","year":"1988","journal-title":"Science"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB139","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/0092-8674(94)90262-3","article-title":"Rit1, a tRNA backbone-modifying enzyme that mediates initiator and elongator tRNA discrimination","volume":"79","author":"Astr\u00f6m","year":"1994","journal-title":"Cell"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB140","doi-asserted-by":"crossref","first-page":"5679","DOI":"10.1093\/nar\/21.24.5679","article-title":"Discrimination between initiation and elongation of protein biosynthesis in yeast: identity assured by a nucleotide modification in the initiator tRNA","volume":"21","author":"F\u00f6rster","year":"1993","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/S0300-9084(96)80001-0_BIB141","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1002\/j.1460-2075.1996.tb00397.x","article-title":"Antideterminants present in minihelixSec hinder its recognition by prokaryotic elongation factor Tu","volume":"15","author":"Rudinger","year":"1996","journal-title":"EMBO J"}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908496800010?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908496800010?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,4,7]],"date-time":"2023-04-07T07:00:56Z","timestamp":1680850856000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908496800010"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,1]]},"references-count":141,"journal-issue":{"issue":"7","published-print":{"date-parts":[[1996,1]]}},"alternative-id":["S0300908496800010"],"URL":"https:\/\/doi.org\/10.1016\/s0300-9084(96)80001-0","relation":{},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[1996,1]]}}}