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Biol-Chem., 241, 5391, 10.1016\u002FS0021-9258(18)96443-4\nYarus, 1967, J. Mol. Biol., 28, 479, 10.1016\u002FS0022-2836(67)80098-6\nOkamoto, 1967, Biochim. Biophys. Acta, 145, 613, 10.1016\u002F0005-2787(67)90120-7\nSeifert, 1968, J. Mol. Biol., 33, 507, 10.1016\u002F0022-2836(68)90208-8\nLagekkvist, 1969, J. Biol. Chem., 244, 2476, 10.1016\u002FS0021-9258(19)78246-5\nYarus, 1969, J. Mol. Biol., 42, 171, 10.1016\u002F0022-2836(69)90037-0\nHayashi, 1970, J. Biol. Chem., 245, 1401, 10.1016\u002FS0021-9258(18)63250-8\nSoll, 1967, J. Mol. Biol., 29, 97, 10.1016\u002F0022-2836(67)90183-0\nKatze, 1970, J. Biol. Chem., 245, 923, 10.1016\u002FS0021-9258(18)63270-3\nZubay, 1962, J. Mol. Biol., 4, 347, 10.1016\u002FS0022-2836(62)80015-1\nRoy, 1970, J. Biol. Chem., 245, 1394, 10.1016\u002FS0021-9258(18)63249-1\nBurgi, 1963, Biophys. J., 3, 309, 10.1016\u002FS0006-3495(63)86823-X\nJohnston, 1946, Trans. Faraday Soc., 42, 789, 10.1039\u002Ftf9464200789\nKegeles, 1967, Proc. Nat. Acad. Sci. U. S. A., 58, 45, 10.1073\u002Fpnas.58.1.45\nBethune, 1961, J. Phys. Chem., 65, 1755, 10.1021\u002Fj100827a018\nWeiss, 1967, Biochemistry, 6, 2507, 10.1021\u002Fbi00860a030\nBethune, 1961",{"EN":842},"The Interaction of Seryl and of Leucyl Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids",{"VOID":844},"10.1016\u002Fs0021-9258(18)63251-x","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS002192581863251X",[847,864,876,888],{"id":848,"sortIndex":193,"researcher":18,"roles":849,"affiliations":850,"properties":861},"993cbbec-cf90-40d3-add6-39699b47a4b8",[140],[851],{"id":18,"sortIndex":19,"affiliation":852,"properties":18},{"id":853,"createTime":854,"updateTime":855,"relativeEntities":856,"slug":857,"properties":858,"entityType":55,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"a3f02c6a-b898-48dc-84a5-8e494b152dda","2024-01-18T23:59:54.221+00:00","2024-12-23T05:28:03.339+00:00",[],"From-the-Department-of-Molecular-Biophysics-and-Biochemistry-Yale-University-New-Haven-Connecticut-06520",{"title":859},{"VI":860},"From the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520",{"title":862},{"VI":863},"Dieter Söll",{"id":865,"sortIndex":138,"researcher":18,"roles":866,"affiliations":867,"properties":873},"ed21b68d-c638-41a0-83c0-94142d47718e",[140],[868],{"id":18,"sortIndex":19,"affiliation":869,"properties":18},{"id":853,"createTime":854,"updateTime":855,"relativeEntities":870,"slug":857,"properties":871,"entityType":55,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":872},{"VI":860},{"title":874},{"VI":875},"William Konigsberg",{"id":877,"sortIndex":19,"researcher":18,"roles":878,"affiliations":879,"properties":885},"0f7ed8d4-0fd6-46bd-837a-42e324ae3bd6",[140],[880],{"id":18,"sortIndex":19,"affiliation":881,"properties":18},{"id":853,"createTime":854,"updateTime":855,"relativeEntities":882,"slug":857,"properties":883,"entityType":55,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":884},{"VI":860},{"title":886},{"VI":887},"J.R. Knowles",{"id":889,"sortIndex":110,"researcher":18,"roles":890,"affiliations":891,"properties":897},"c46220e6-2402-4341-bd76-e9336500651e",[140],[892],{"id":18,"sortIndex":19,"affiliation":893,"properties":18},{"id":853,"createTime":854,"updateTime":855,"relativeEntities":894,"slug":857,"properties":895,"entityType":55,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":896},{"VI":860},{"title":898},{"VI":899},"Jon R. Katze",{"url":845,"publisher":901,"properties":928},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":902,"slug":10,"properties":903,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":906,"manageAffiliations":907,"indexDatabases":908,"url":18,"thumbnailPath":18,"statistic":923,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":904,"title":905},{"VOID":13},{"EN":15},[],[],[909,916],{"id":88,"indexDatabase":910,"url":101,"indexYears":102,"academicFieldIds":915,"indexDatabaseRanking":107},{"id":90,"createTime":91,"updateTime":92,"relativeEntities":911,"label":912,"description":913,"key":98,"publicationTags":914,"standard":18},[],{"EN":95,"VI":95},{"EN":95,"VI":97},[100],[104,105,106],{"id":70,"indexDatabase":917,"url":18,"indexYears":18,"academicFieldIds":922,"indexDatabaseRanking":18},{"id":72,"createTime":73,"updateTime":74,"relativeEntities":918,"label":919,"description":920,"key":81,"publicationTags":921,"standard":18},[],{"EN":77,"VI":77},{"VI":79,"EN":80},[83,84],[86],{"impactFactor":19,"impactFactorByYear":924,"i10Index":19,"i10IndexLast5Year":19,"totalPublication":110,"totalPublicationByYear":925,"totalCitation":19,"totalCitationByYear":926,"totalCitationPerPublication":19,"totalCitationPerPublicationByYear":927,"hindexLast5Year":19,"hindex":19},{},{"1981":110},{},{},{"volume":929,"pages":931},{"VOID":930},"245",{"VOID":932},"1407-1415","1970-03-01",1970,{"id":936,"createTime":937,"updateTime":937,"relativeEntities":938,"slug":939,"properties":940,"entityType":131,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":953,"fullTextUrl":18,"authors":954,"publicationType":216,"publisherRelationship":1058,"citationCount":18,"citationInfo":18,"publishDate":1091,"publishYear":1092,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":252},"6a5a3b81-36d8-420e-bdea-1310d9b5e018","2023-11-12T23:59:54.609+00:00",[],"Involvement-of-c-Src-Tyrosine-Kinase-Upstream-of-Class-I-Phosphatidylinositol-PI-3-Kinases-in-Salmonella-Enteritidis-Rck-Protein-mediated-Invasion",{"pii":941,"references":943,"keywords":945,"abstract":947,"title":949,"doi":951},{"VOID":942},"S0021925820630605",{"VOID":944},"1 P. Velge A. Wiedemann M. Rosselin N. Abed Z. Boumart A. Chaussé O. Grépinet F. Namdari S. Roche A. Rossignol I. Virlogeux-Payant Multiplicity of Salmonella entry mechanisms, a new paradigm for Salmonella pathogenesis Microbiology Open 2012 in press Velge, P., Wiedemann, A., Rosselin, M., Abed, N., Boumart, Z., Chaussé, A., Grépinet, O., Namdari, F., Roche, S., Rossignol, A., Virlogeux-Payant, I., (2012) Multiplicity of Salmonella entry mechanisms, a new paradigm for Salmonella pathogenesis. Microbiology Open, in press,\n2 M. Rosselin N. Abed F. Namdari I. Virlogeux-Payant P. Velge A. Wiedemann The different strategies used by Salmonella to invade host cells B.A. Annous J.B. Gurtler Salmonella: Distribution, Adaptation, Control Measures and Molecular Technologies 2012 InTech Europe Rijeka, Croatia 339 364 in press Rosselin, M., Abed, N., Namdari, F., Virlogeux-Payant, I., Velge, P., Wiedemann, A., (2012) The different strategies used by Salmonella to invade host cells. in Salmonella: Distribution, Adaptation, Control Measures and Molecular Technologies (Annous, B. A., Gurtler, J. B., eds) pp. 339–364, InTech Europe, Rijeka, Croatia, in press,\n3 P. Cossart P. Sansonetti Bacterial invasion: the paradigms of enteroinvasive pathogens Science 304 2004 242 248 Cossart, P., Sansonetti, P., (2004) Bacterial invasion: the paradigms of enteroinvasive pathogens. Science 304, 242–248,\n4 M. Rosselin I. Virlogeux-Payant C. Roy E. Bottreau P.Y. Sizaret L. Mijouin P. Germon E. Caron P. Velge A. Wiedemann Rck of Salmonella enterica, subspecies enterica serovar enteritidis, mediates Zipper-like internalization Cell Res. 20 2010 647 664 Rosselin, M., Virlogeux-Payant, I., Roy, C., Bottreau, E., Sizaret, P. Y., Mijouin, L., Germon, P., Caron, E., Velge, P., Wiedemann, A., (2010) Rck of Salmonella enterica, subspecies enterica serovar enteritidis, mediates Zipper-like internalization. Cell Res. 20, 647–664,\n5 E.J. Heffernan L. Wu J. Louie S. Okamoto J. Fierer D.G. Guiney Specificity of the complement resistance and cell association phenotypes encoded by the outer membrane protein genes rck from Salmonella typhimurium and ail from Yersinia enterocolitica Infect. Immun. 62 1994 5183 5186 Heffernan, E. J., Wu, L., Louie, J., Okamoto, S., Fierer, J., Guiney, D. G., (1994) Specificity of the complement resistance and cell association phenotypes encoded by the outer membrane protein genes rck from Salmonella typhimurium and ail from Yersinia enterocolitica, . Infect. Immun. 62, 5183–5186,\n6 L. Mijouin M. Rosselin E. Bottreau J. Pizarro-Cerda P. Cossart P. Velge A. Wiedemann Salmonella enteritidis Rck-mediated invasion requires activation of Rac1, which is dependent on the class I PI 3-kinases-Akt signaling pathway FASEB J. 26 2012 1569 1581 Mijouin, L., Rosselin, M., Bottreau, E., Pizarro-Cerda, J., Cossart, P., Velge, P., Wiedemann, A., (2012) Salmonella enteritidis Rck-mediated invasion requires activation of Rac1, which is dependent on the class I PI 3-kinases-Akt signaling pathway. FASEB J. 26, 1569–1581,\n7 S.A. Courtneidge S. Fumagalli M. Koegl G. Superti-Furga G.M. Twamley-Stein The Src family of protein tyrosine kinases: regulation and functions Dev. Suppl. 1993 1993 57 64 Courtneidge, S. A., Fumagalli, S., Koegl, M., Superti-Furga, G., Twamley-Stein, G. M., (1993) The Src family of protein tyrosine kinases: regulation and functions. Dev. Suppl. 1993, 57–64,\n8 J. Mounier M.R. Popoff J. Enninga M.C. Frame P.J. Sansonetti G.T. Van Nhieu The IpaC carboxyl-terminal effector domain mediates Src-dependent actin polymerization during Shigella invasion of epithelial cells PLoS Pathog. 5 2009 e1000271 Mounier, J., Popoff, M. R., Enninga, J., Frame, M. C., Sansonetti, P. J., Van Nhieu, G. T., (2009) The IpaC carboxyl-terminal effector domain mediates Src-dependent actin polymerization during Shigella invasion of epithelial cells. PLoS Pathog. 5, e1000271,\n9 N. Van Langendonck P. Velge E. Bottreau Host cell protein tyrosine kinases are activated during the entry of Listeria monocytogenes: possible role of pp60c-src family protein kinases FEMS Microbiol. Lett. 162 1998 169 176 Van Langendonck, N., Velge, P., Bottreau, E., (1998) Host cell protein tyrosine kinases are activated during the entry of Listeria monocytogenes: possible role of pp60c-src family protein kinases. FEMS Microbiol. Lett. 162, 169–176,\n10 J. Eitel T. Heise U. Thiesen P. Dersch Cell invasion and IL-8 production pathways initiated by YadA of Yersinia pseudotuberculosis require common signaling molecules (FAK, c-Src, Ras) and distinct cell factors Cell Microbiol. 7 2005 63 77 Eitel, J., Heise, T., Thiesen, U., Dersch, P., (2005) Cell invasion and IL-8 production pathways initiated by YadA of Yersinia pseudotuberculosis require common signaling molecules (FAK, c-Src, Ras) and distinct cell factors. Cell Microbiol. 7, 63–77,\n11 S. Sousa D. Cabanes L. Bougnères M. Lecuit P. Sansonetti G. Tran-Van-Nhieu P. Cossart Src, cortactin, and Arp2\u002F3 complex are required for E-cadherin-mediated internalization of Listeria into cells Cell Microbiol. 9 2007 2629 2643 Sousa, S., Cabanes, D., Bougnères, L., Lecuit, M., Sansonetti, P., Tran-Van-Nhieu, G., Cossart, P., (2007) Src, cortactin, and Arp2\u002F3 complex are required for E-cadherin-mediated internalization of Listeria into cells. Cell Microbiol. 9, 2629–2643,\n12 R.A. Klinghoffer C. Sachsenmaier J.A. Cooper P. Soriano Src family kinases are required for integrin but not PDGFR signal transduction EMBO J. 18 1999 2459 2471 Klinghoffer, R. A., Sachsenmaier, C., Cooper, J. A., Soriano, P., (1999) Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J. 18, 2459–2471,\n13 M.C. Chen T.E. Solomon E. Perez Salazar R. Kui E. Rozengurt A.H. Soll Secretin regulates paracellular permeability in canine gastric monolayers by a Src kinase-dependent pathway Am. J. Physiol. Gastrointest. Liver Physiol. 283 2002 G893 G899 Chen, M. C., Solomon, T. E., Perez Salazar, E., Kui, R., Rozengurt, E., Soll, A. H., (2002) Secretin regulates paracellular permeability in canine gastric monolayers by a Src kinase-dependent pathway. Am. J. Physiol. Gastrointest. Liver Physiol. 283, G893–G899,\n14 J.H. Hanke J.P. Gardner R.L. Dow P.S. Changelian W.H. Brissette E.J. Weringer B.A. Pollok P.A. Connelly Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. Study of Lck- and FynT-dependent T cell activation J. Biol. Chem. 271 1996 695 701 Hanke, J. H., Gardner, J. P., Dow, R. L., Changelian, P. S., Brissette, W. H., Weringer, E. J., Pollok, B. A., Connelly, P. A., (1996) Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. Study of Lck- and FynT-dependent T cell activation. J. Biol. Chem. 271, 695–701,\n15 S.M. Thomas J.S. Brugge Cellular functions regulated by Src family kinases Annu. Rev. Cell Dev. Biol. 13 1997 513 609 Thomas, S. M., Brugge, J. S., (1997) Cellular functions regulated by Src family kinases. Annu. Rev. Cell Dev. Biol. 13, 513–609,\n16 L. Buday Membrane-targeting of signaling molecules by SH2\u002FSH3 domain-containing adaptor proteins Biochim. Biophys. Acta 1422 1999 187 204 Buday, L., (1999) Membrane-targeting of signaling molecules by SH2\u002FSH3 domain-containing adaptor proteins. Biochim. Biophys. Acta 1422, 187–204,\n17 T. Pawson Dynamic control of signaling by modular adaptor proteins Curr. Opin. Cell Biol. 19 2007 112 116 Pawson, T., (2007) Dynamic control of signaling by modular adaptor proteins. Curr. Opin. Cell Biol. 19, 112–116,\n18 M. Ui T. Okada K. Hazeki O. Hazeki Wortmannin as a unique probe for an intracellular signaling protein, phosphoinositide 3-kinase Trends Biochem. Sci. 20 1995 303 307 Ui, M., Okada, T., Hazeki, K., Hazeki, O., (1995) Wortmannin as a unique probe for an intracellular signaling protein, phosphoinositide 3-kinase. Trends Biochem. Sci. 20, 303–307,\n19 P. Kefalas T.R. Brown P.M. Brickell Signaling by the p60c-src family of protein-tyrosine kinases Int. J. Biochem. Cell Biol. 27 1995 551 563 Kefalas, P., Brown, T. R., Brickell, P. M., (1995) Signaling by the p60c-src family of protein-tyrosine kinases. Int. J. Biochem. Cell Biol. 27, 551–563,\n20 A.G. Tatosyan O.A. Mizenina Kinases of the Src family: structure and functions Biochemistry 65 2000 49 58 Tatosyan, A. G., Mizenina, O. A., (2000) Kinases of the Src family: structure and functions. Biochemistry 65, 49–58,\n21 M.A. Alrutz R.R. Isberg Involvement of focal adhesion kinase in invasin-mediated uptake Proc. Natl. Acad. Sci. U.S.A. 95 1998 13658 13663 Alrutz, M. A., Isberg, R. R., (1998) Involvement of focal adhesion kinase in invasin-mediated uptake. Proc. Natl. Acad. Sci. U.S.A. 95, 13658–13663,\n22 H. Slanina A. König S. Hebling C.R. Hauck M. Frosch A. Schubert-Unkmeir Entry of Neisseria meningitidis into mammalian cells requires the Src family protein tyrosine kinases Infect. Immun. 78 2010 1905 1914 Slanina, H., König, A., Hebling, S., Hauck, C. R., Frosch, M., Schubert-Unkmeir, A., (2010) Entry of Neisseria meningitidis into mammalian cells requires the Src family protein tyrosine kinases. Infect. Immun. 78, 1905–1914,\n24 J. Shi J. Casanova Invasion of host cells by Salmonella typhimurium requires focal adhesion kinase and p130Cas Mol. Biol. Cell 17 2006 4698 4708 Shi, J., Casanova, J., (2006) Invasion of host cells by Salmonella typhimurium requires focal adhesion kinase and p130Cas. Mol. Biol. Cell 17, 4698–4708,\n25 G. Duménil J.C. Olivo S. Pellegrini M. Fellous P.J. Sansonetti G.T. Nhieu Interferon α inhibits a Src-mediated pathway necessary for Shigella-induced cytoskeletal rearrangements in epithelial cells J. Cell Biol. 143 1998 1003 1012 Duménil, G., Olivo, J. C., Pellegrini, S., Fellous, M., Sansonetti, P. J., Nhieu, G. T., (1998) Interferon α inhibits a Src-mediated pathway necessary for Shigella-induced cytoskeletal rearrangements in epithelial cells. J. Cell Biol. 143, 1003–1012,\n23 Deleted in proof Deleted in proof,",{"EN":946},"Microbiology,Signaling,siRNA,Src,Tyrosine Protein Kinase (Tyrosine Kinase)",{"EN":948},"The Salmonella outer membrane protein Rck mediates a Zipper entry mechanism controlled by tyrosine phosphorylation and class I phosphatidylinositol 3-kinase (PI 3-kinase). However, the underlying mechanism leading to this signaling cascade remains unclear. The present study showed that using Rck-coated beads or Rck-overexpressing Escherichia coli, Rck-mediated actin polymerization and invasion were blocked by PP2, a Src family tyrosine kinase inhibitor. In addition, phosphorylation of Src family kinases significantly increased after stimulation with Rck. The specific contribution of c-Src, one member of the Src family kinases, was demonstrated using c-Src-deficient fibroblasts or c-Src siRNA transfected epithelial cells. We also observed that Rck-mediated internalization led to the formation of a complex between c-Src and at least one tyrosine-phosphorylated protein. Furthermore, our results revealed that the c-Src signal molecule was upstream of PI 3-kinase during the Rck-mediated signaling pathway as Rck-mediated PI 3-kinase activation was blocked by PP2, and PI 3-kinase inhibitor had no effect on the Src phosphorylation. These results demonstrate the involvement of c-Src upstream of the PI 3-kinase in the Zipper entry process mediated by Rck.",{"EN":950},"Involvement of c-Src Tyrosine Kinase Upstream of Class I Phosphatidylinositol (PI) 3-Kinases in Salmonella Enteritidis Rck Protein-mediated 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1979, Annu. Rev. Biochem., 48, 601, 10.1146\u002Fannurev.bi.48.070179.003125\nBroach, 1982, 653\nHartwell, 1968, J. Bacteriol., 96, 1664, 10.1128\u002Fjb.96.5.1664-1671.1968\nHartwell, 1968, Proc. Natl. Acad. Sci. U. S. A., 59, 422, 10.1073\u002Fpnas.59.2.422\nMcLaughlin, 1969, J. Bacteriol., 100, 579, 10.1128\u002Fjb.100.2.579-584.1969\nMessenguy, 1976, Eur. J. Biochem., 67, 335, 10.1111\u002Fj.1432-1033.1976.tb10696.x\nMcLaughlin, 1969, Genetics, 61, 557, 10.1093\u002Fgenetics\u002F61.3.557\nCherest, 1975, J. Bacteriol., 123, 428, 10.1128\u002Fjb.123.2.428-435.1975\nUnger, 1977, J. Bacteriol., 130, 11, 10.1128\u002Fjb.130.1.11-19.1977\nFasiolo, 1981, J. Biol. Chem., 256, 2324, 10.1016\u002FS0021-9258(19)69782-6\nCherest, 1971, J. Bacteriol., 106, 758, 10.1128\u002Fjb.106.3.758-772.1971\nUnger, 1976, Proc. Natl. Acad. Sci. U. S. A., 73, 1664, 10.1073\u002Fpnas.73.5.1664\nMortimer, 1982, 641\nBroach, 1979, Gene, 8, 121, 10.1016\u002F0378-1119(79)90012-X\nBolivar, 1977, Gene, 2, 95, 10.1016\u002F0378-1119(77)90000-2\nStruhl, 1979, Proc. Natl. Acad. Sci. U. S. A., 76, 1035, 10.1073\u002Fpnas.76.3.1035\nFink, 1970, Methods Enzymol., 17A, 59, 10.1016\u002F0076-6879(71)17167-4\nSherman, 1974\nDavis, 1980\nHinnen, 1978, Proc. Natl. Acad. Sci. U. S. A., 75, 1929, 10.1073\u002Fpnas.75.4.1929\nFarabaugh, 1980, Nature (Lond.), 286, 352, 10.1038\u002F286352a0\nIlgen, 1979, Vol. 1, 117\nRoeder, 1980, Cell, 21, 239, 10.1016\u002F0092-8674(80)90131-2\nCarlson, 1982, Cell, 28, 145, 10.1016\u002F0092-8674(82)90384-1\nSilverman, 1982, Mol. Cell. Biol., 2, 1212\nVennegar, 1974, Methods Enzymol., 29, 584, 10.1016\u002F0076-6879(74)29052-9\nLowry, 1951, J. Biol. Chem., 193, 265, 10.1016\u002FS0021-9258(19)52451-6\nAhmed, 1973, Mol. Gen. Genet., 123, 299, 10.1007\u002FBF00433648\nOrr-Weaver, 1981, Proc. Natl. Acad. Sci. U. S. A., 78, 6354, 10.1073\u002Fpnas.78.10.6354\nBhanot, 1974, Methods Enzymol., 29, 547, 10.1016\u002F0076-6879(74)29050-5\nDeleted in proof\nWolfner, 1975, J. Mol. Biol., 96, 273, 10.1016\u002F0022-2836(75)90348-4\nNeiderberger, 1981, Mol. Cell. Biol., 1, 584\nDobson, 1981, Gene, 16, 133, 10.1016\u002F0378-1119(81)90069-X\nDelforge, 1975, Eur. J. Biochem., 57, 231, 10.1111\u002Fj.1432-1033.1975.tb02295.x\nStruhl, 1981, J. Mol. Biol., 152, 535, 10.1016\u002F0022-2836(81)90267-9\nMessenguy, 1980\nZalkin, 1982, J. Biol. Chem., 257, 1491, 10.1016\u002FS0021-9258(19)68220-7\nEhresmann, 1971, Biochim. Biophys. Acta, 254, 226, 10.1016\u002F0005-2787(71)90831-8\nSurdin-Kerjan, 1973, J. Bacteriol., 113, 1156, 10.1128\u002Fjb.113.3.1156-1160.1973\nMcLaughlin, 1973, J. Biol. Chem., 248, 1466, 10.1016\u002FS0021-9258(19)44322-6\nRosbash, 1981, Cell, 24, 679, 10.1016\u002F0092-8674(81)90094-5\nSt. John, 1981, J. Mol. 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Biophys. Res. Commun., 75, 401, 10.1016\u002F0006-291X(77)91056-7\nStillwell, 1978, Res. Commun. Chem. Pathol. Pharmacol., 20, 509\nMio, 1976, Chem. Pharm. Bull. (Tokyo), 24, 1958, 10.1248\u002Fcpb.24.1958\nMiller, 1968, Mol. Pharmacol., 4, 147\nTateishi, 1978, J. Biol. Chem., 253, 8854, 10.1016\u002FS0021-9258(17)34256-4\nTateishi, 1980, Vol. 2, 121\nTateishi, 1981, Methods Enzymol., 77, 253, 10.1016\u002FS0076-6879(81)77033-2\nSuzuki, 1981, Drub Metab. Dispos., 9, 573\nSuzuki, 1983, Biochem. Pharmacol., 31, 2137, 10.1016\u002F0006-2952(82)90437-3\nSaunders, 1934, Biochem. J., 28, 1977, 10.1042\u002Fbj0281977\nParke, 1951, Biochem. J., 48, 624, 10.1042\u002Fbj0480624\nParrod, 1944, C. R. Hebd. Seances Acad. Sci., 218, 599\nSoda, 1967, Agric. Biol. Chem., 31, 1054, 10.1080\u002F00021369.1967.10858916\nLowry, 1951, J. Biol. Chem., 193, 265, 10.1016\u002FS0021-9258(19)52451-6\nTanaka, 1977, Biochemistry, 16, 100, 10.1021\u002Fbi00620a016\nMushahwar, 1973, J. Biol. 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