Functional aspects of ribosomal architecture: Symmetry, chirality and regulation (329 views visite)
J Phys Org Chem (ISSN: 0894-3230), 2004; 17(11): 901-912.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 1.211, 5-year impact factor Impact factor a 5 anni: 1.41
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-8344271978&partnerID=40&md5=eabd2a9549b57ed38dc49e6e3b7b41c6
Keywords Parole chiave: D-Amino Acids, Elongation Arrest, Peptide-Bond Formation, Positional-Catalysis, Protein Ctc, Protein L22, Ribosomes, Tunnel Dynamics, Biosynthesis, Crystal Structure, Crystallography, Molecular Weight, Polymerization, Polypeptides, Ribosomal Architecture,
Affiliations Affiliazioni:
*** IBB - CNR ***
Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel
Max-Planck-Res. U. Ribosomal Struct., 22603 Hamburg, Germany
Inst. of Biostructure and Bioimaging, CNR, 80138 Napoli, Italy
References Riferimenti:
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Ban, N., Nissen, P., Hansen, J., Moore, P.B., Steitz, T.A., (2000) Science, 289, pp. 905-920
Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janeil, D., Bashan, A., Yonath, A., (2000) Cell, 102, pp. 615-623
Wimberly, B.T., Brodersen, D.E., Clemons Jr., W.M., Morgan-Warren, R.J., Carter, A.P., Vonrhein, C., Hartsch, T., Ramakrishnan, V., (2000) Nature, 407, pp. 327-339
Yusupov, M.M., Yusupova, G.Z., Baucom, A., Lieberman, K., Earnest, T.N., Gate, J.H., Noller, H.F., (2001) Science, 292, pp. 883-896
Harms, J., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Yonath, A., (2001) Cell, 107, pp. 679-688
Bashan, A., Agmon, I., Zarivach, R., Schluenzen, F., Harms, J., Berisio, R., Bartels, H., Yonath, A., (2003) Mol. Cell, 11, pp. 91-102
Bashan, A., Zarivach, R., Schluenzen, F., Agmon, I., Harms, J., Auerbach, T., Baram, D., Yonath, A., (2003) Biopolymers, 70, pp. 19-41
Agmon, I., Auerbach, T., Baram, D., Bartels, H., Bashan, A., Berisio, R., Fucini, P., Zarivach, R., (2003) Eur. J. Biochem., 270, pp. 2543-2556
Harms, J.M., Schluenzen, F., Fucini, P., Bartels, H., Yonath, A., (2004) BMC Biol., 2 (4), pp. 1-10
Berisio, R., Schluenzen, F., Harms, J., Bashan, A., Auerbach, T., Baram, D., Yonath, A., (2003) Nat. Struct. Biol., 10, pp. 366-370
Berisio, R., Harms, J., Schluenzen, F., Zarivach, R., Hansen, H.A., Fucini, P., Yonath, A., (2003) J. Bacterial., 185, pp. 4276-4279
Stark, H., Orlova, E.V., Rinke-Appel, J., Junke, N., Mueller, F., Rodnina, M., Wintermeyer, W., Van Heel, M., (1997) Cell, 88, pp. 19-28
Gabashvili, I.S., Agrawal, R.K., Grassucci, R., Squires, C.L., Dahlberg, A.E., Frank, J., (1999) Embo. J., 18, pp. 6501-6507
Pioletti, M., Schluenzen, F., Harms, J., Zarivach, R., Gluehmann, M., Avila, H., Bashan, A., Franceschi, F., (2001) Embo. J., 20, pp. 1829-1839
Yonath, A., (2002) Annu. Rev. Biophys. Biomol. Struct., 31, pp. 257-273
Kim, D.F., Green, R., (1999) Mol. Cell, 4, pp. 859-864
Wilson, K.S., Noller, H.F., (1998) Cell, 92, pp. 337-349
Moazed, D., Noller, H.F., (1989) Nature, 342, pp. 142-148
Green, R., Noller, H.F., (1997) Annu. Rev. Biochem., 66, pp. 679-716
Malkin, L.I., Rich, A., (1967) J. Mol. Biol., 26, pp. 329-346
Sabatini, D.D., Blobel, G., (1970) J. Cell. Biol., 45, pp. 146-157
Milligan, R.A., Unwin, P.N., (1986) Nature, 319, pp. 693-695
Yonath, A., Leonard, K.R., Wittmann, H.G., (1987) Science, 236, pp. 813-816
Frank, J., Zhu, J., Penczek, P., Li, Y., Srivastava, S., Verschoor, A., Radermacher, M., Agrawal, R.K., (1995) Nature, 376, pp. 441-444
Stark, H., Mueller, F., Orlova, E.V., Schatz, M., Dube, P., Erdemir, T., Zemlin, F., Van Heel, M., (1995) Structure, 3, pp. 815-821
Eisenstein, M., Hardesty, B., Odom, O.W., Kudlicki, W., Kramer, G., Arad, T., Franceschi, F., Yonath, A., (1994) Supramolecular Structure and Function, pp. 213-246. , Pifat G (ed). Balaban Press: Rehovot
Kurzchalia, T.V., Wiedmann, M., Breter, H., Zimmermann, W., Bauschke, E., Rapoport, T.A., (1988) Eur. J. Biochem., 172, pp. 663-668
Nakatogawa, H., Ito, K., (2002) Cell, 108, pp. 629-636
Nierhaus, K.H., Schulze, H., Cooperman, B.S., (1980) Biochem. Int., 1, pp. 185-192
Katunin, V., Muth, G., Strobel, S., Wintermeyer, W., Mol, R.M., (2002) Cell., 10, pp. 339-346
Rodnina, M.V., Wintermeyer, W., (2001) Trends. Biochem. Sci., 26, pp. 124-130
Schmeing, T.M., Seila, A.C., Hansen, J.L., Freeborn, B., Soukup, J.K., Scaringe, S.A., Strobel, S.A., Steitz, T.A., (2002) Nat. Struct. Biol., 9, pp. 225-230
Hansen, J.L., Schmeing, T.M., Moore, P.B., Steitz, T.A., (2002) Proc. Natl. Acad. Sci. USA, 99, pp. 11670-11675
Yonath, A., (2003) Chem. Bio. Chem., 4, pp. 1008-1017
Miskin, R., Zamir, A., Biochem, E.D., (1968) Biophys. Res. Commun., 33, pp. 551-557
Vogel, Z., Vogel, T., Zamir, A., Elson, D., (1971) J. Mol. Biol., 60, pp. 339-346
Zamir, A., Miskin, R., Vogel, Z., Elson, D., (1974) Methods Enzymol., 30, pp. 406-426
Bayfield, M.A., Dahlberg, A.E., Schulmeister, U., Dorner, S., Barta, A., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 10096-10101
Agrawal, R.K., Penczek, P., Grassucci, R.A., Burkhardt, N., Nierhaus, K.H., Frank, J., (1999) J. Biol. Chem., 274, pp. 8723-8729
Calendar, R., Berg, P., (1967) J. Mol. Biol., 26, pp. 39-54
Briza, P., Ellinger, A., Winkler, G., Breitenbach, M., (1990) J. Biol. Chem., 265, pp. 15118-15123
Cosloy, S.D., McFall, E., (1973) J. Bacteriol., 114, pp. 685-694
Soutourina, J., Blanquet, S., Plateau, P., (2000) J. Biol. Chem., 275, pp. 11626-11630
Yamane, T., Miller, D.L., Hopfield, J.J., (1981) Biochemistry, 20, pp. 7059-7064
Heckler, T.G., Roesser, J.R., Xu, C., Chang, P.I., Hecht, S.M., (1988) Biochemistry, 27, pp. 7254-7262
Bain, J.D., Diala, E.S., Glabe, C.G., Wacker, D.A., Lyttle, M.H., Dix, T.A., Chamberlin, A.R., (1991) Biochemistry, 30, pp. 5411-5421
Dedkova, L.M., Fahmi, N.E., Golovine, S.Y., Hecht, S.M., (2003) J. Am. Chem. Soc., 125, pp. 6616-6617
Gabashvili, I.S., Gregory, S.T., Valle, M., Grassucci, R., Worbs, M., Wahl, M.C., Dahlberg, A.E., Frank, J., (2001) Mol. Cell., 8, pp. 181-188
Tenson, T., Ehrenberg, M., (2002) Cell, 108, pp. 591-594
Gong, F., Yanofsky, C., (2002) Science, 297, pp. 1864-1867
Liao, S., Lin, J., Do, H., Johnson, A.E., (1997) Cell, 90, pp. 31-41
Stroud, R.M., Walter, P., (1999) Curr. Opin. Struct. Biol., 9, pp. 754-759
Morris, D.R., Geballe, A.P., (2000) Mol. Cell. Biol., 20, pp. 8635-8642
Chepkwony, H.K., Roets, E., Hoogmartens, J., (2001) J. Chromatogr. A, 914, pp. 53-58
Auerbach, T., Bashan, A., Harms, J., Schluenzen, F., Zarivach, R., Bartels, H., Agmon, I., Yonath, A., (2002) Curr. Drug Targets-infect. Disord., 2, pp. 169-186
Unge, J., Berg, A., Al-Kharadaghi, S., Nikulin, A., Nikonov, S., Davydova, N., Nevskaya, N., Liljas, A., (1998) Structure, 6, pp. 1577-1586
Davydova, N., Streltsov, V., Wilce, M., Liljas, A., Garber, M., (2002) J. Mol. Biol., 322, pp. 635-644
White, O., Eisen, J.A., Heidelberg, J.F., Hickey, E.K., Peterson, J.D., Dodson, R.J., Haft, D.H., Fraser, C.L., (1999) Science, 286, pp. 1571-1577
Levin-Zaidman, S., Englander, A., Shimoni, E., Sharma, A., Minton, W., Minsky, A., (2003) Science, 299, pp. 254-256
Lu, M., Steitz, T.A., (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 2023-2028
Fedorov, R., Meshcheryakov, V., Gongadze, G., Fomenkova, N., Nevskaya, N., Seimer, M., Laurberg, M., Nikonov, S., (2001) Acta Crystallogr. D. Biol. Crystallogr., 57, pp. 968-976
Rheinberger, H.J., Sternbach, H., Nierhaus, K.H., (1981) Proc. Natl. Acad. Sci. USA, 78, pp. 5310-5314
Lill, R., Wintermeyer, W., (1987) J. Mol. Biol., 196, pp. 137-148
Dabrowski, M., Spahn, C.M., Schafer, M.A., Patzke, S., Nierhaus, K.H., (1998) J. Biol. Chem., 273, pp. 32793-32800
Noller, H.F., Yusupov, M.M., Yusupova, G.Z., Baucom, A., Cate, J.H., (2002) FEBS Lett., 514, pp. 11-16
Wimberly, B. T., Brodersen, D. E., Clemons Jr., W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., Ramakrishnan, V., (2000) Nature, 407, pp. 327-339
Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Gate, J. H., Noller, H. F., (2001) Science, 292, pp. 883-896
Harms, J. M., Schluenzen, F., Fucini, P., Bartels, H., Yonath, A., (2004) BMC Biol., 2 (4), pp. 1-10
Gabashvili, I. S., Agrawal, R. K., Grassucci, R., Squires, C. L., Dahlberg, A. E., Frank, J., (1999) Embo. J., 18, pp. 6501-6507
Kim, D. F., Green, R., (1999) Mol. Cell, 4, pp. 859-864
Wilson, K. S., Noller, H. F., (1998) Cell, 92, pp. 337-349
Malkin, L. I., Rich, A., (1967) J. Mol. Biol., 26, pp. 329-346
Sabatini, D. D., Blobel, G., (1970) J. Cell. Biol., 45, pp. 146-157
Milligan, R. A., Unwin, P. N., (1986) Nature, 319, pp. 693-695
Kurzchalia, T. V., Wiedmann, M., Breter, H., Zimmermann, W., Bauschke, E., Rapoport, T. A., (1988) Eur. J. Biochem., 172, pp. 663-668
Nierhaus, K. H., Schulze, H., Cooperman, B. S., (1980) Biochem. Int., 1, pp. 185-192
Rodnina, M. V., Wintermeyer, W., (2001) Trends. Biochem. Sci., 26, pp. 124-130
Schmeing, T. M., Seila, A. C., Hansen, J. L., Freeborn, B., Soukup, J. K., Scaringe, S. A., Strobel, S. A., Steitz, T. A., (2002) Nat. Struct. Biol., 9, pp. 225-230
Hansen, J. L., Schmeing, T. M., Moore, P. B., Steitz, T. A., (2002) Proc. Natl. Acad. Sci. USA, 99, pp. 11670-11675
Bayfield, M. A., Dahlberg, A. E., Schulmeister, U., Dorner, S., Barta, A., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 10096-10101
Agrawal, R. K., Penczek, P., Grassucci, R. A., Burkhardt, N., Nierhaus, K. H., Frank, J., (1999) J. Biol. Chem., 274, pp. 8723-8729
Cosloy, S. D., McFall, E., (1973) J. Bacteriol., 114, pp. 685-694
Heckler, T. G., Roesser, J. R., Xu, C., Chang, P. I., Hecht, S. M., (1988) Biochemistry, 27, pp. 7254-7262
Bain, J. D., Diala, E. S., Glabe, C. G., Wacker, D. A., Lyttle, M. H., Dix, T. A., Chamberlin, A. R., (1991) Biochemistry, 30, pp. 5411-5421
Dedkova, L. M., Fahmi, N. E., Golovine, S. Y., Hecht, S. M., (2003) J. Am. Chem. Soc., 125, pp. 6616-6617
Gabashvili, I. S., Gregory, S. T., Valle, M., Grassucci, R., Worbs, M., Wahl, M. C., Dahlberg, A. E., Frank, J., (2001) Mol. Cell., 8, pp. 181-188
Stroud, R. M., Walter, P., (1999) Curr. Opin. Struct. Biol., 9, pp. 754-759
Morris, D. R., Geballe, A. P., (2000) Mol. Cell. Biol., 20, pp. 8635-8642
Chepkwony, H. K., Roets, E., Hoogmartens, J., (2001) J. Chromatogr. A, 914, pp. 53-58
Lu, M., Steitz, T. A., (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 2023-2028
Rheinberger, H. J., Sternbach, H., Nierhaus, K. H., (1981) Proc. Natl. Acad. Sci. USA, 78, pp. 5310-5314
Noller, H. F., Yusupov, M. M., Yusupova, G. Z., Baucom, A., Cate, J. H., (2002) FEBS Lett., 514, pp. 11-16
J Phys Org Chem (ISSN: 0894-3230), 2004; 17(11): 901-912.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 1.211, 5-year impact factor Impact factor a 5 anni: 1.41
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-8344271978&partnerID=40&md5=eabd2a9549b57ed38dc49e6e3b7b41c6
Keywords Parole chiave: D-Amino Acids, Elongation Arrest, Peptide-Bond Formation, Positional-Catalysis, Protein Ctc, Protein L22, Ribosomes, Tunnel Dynamics, Biosynthesis, Crystal Structure, Crystallography, Molecular Weight, Polymerization, Polypeptides, Ribosomal Architecture,
Affiliations Affiliazioni:
*** IBB - CNR ***
Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel
Max-Planck-Res. U. Ribosomal Struct., 22603 Hamburg, Germany
Inst. of Biostructure and Bioimaging, CNR, 80138 Napoli, Italy
References Riferimenti:
Yonath, A., Muessig, J., Tesche, B., Lorenz, S., Erdmann, V.A., Wittmann, H.G., (1980) Biochem. Int., 1, pp. 428-43
Ban, N., Nissen, P., Hansen, J., Moore, P.B., Steitz, T.A., (2000) Science, 289, pp. 905-920
Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janeil, D., Bashan, A., Yonath, A., (2000) Cell, 102, pp. 615-623
Wimberly, B.T., Brodersen, D.E., Clemons Jr., W.M., Morgan-Warren, R.J., Carter, A.P., Vonrhein, C., Hartsch, T., Ramakrishnan, V., (2000) Nature, 407, pp. 327-339
Yusupov, M.M., Yusupova, G.Z., Baucom, A., Lieberman, K., Earnest, T.N., Gate, J.H., Noller, H.F., (2001) Science, 292, pp. 883-896
Harms, J., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Yonath, A., (2001) Cell, 107, pp. 679-688
Bashan, A., Agmon, I., Zarivach, R., Schluenzen, F., Harms, J., Berisio, R., Bartels, H., Yonath, A., (2003) Mol. Cell, 11, pp. 91-102
Bashan, A., Zarivach, R., Schluenzen, F., Agmon, I., Harms, J., Auerbach, T., Baram, D., Yonath, A., (2003) Biopolymers, 70, pp. 19-41
Agmon, I., Auerbach, T., Baram, D., Bartels, H., Bashan, A., Berisio, R., Fucini, P., Zarivach, R., (2003) Eur. J. Biochem., 270, pp. 2543-2556
Harms, J.M., Schluenzen, F., Fucini, P., Bartels, H., Yonath, A., (2004) BMC Biol., 2 (4), pp. 1-10
Berisio, R., Schluenzen, F., Harms, J., Bashan, A., Auerbach, T., Baram, D., Yonath, A., (2003) Nat. Struct. Biol., 10, pp. 366-370
Berisio, R., Harms, J., Schluenzen, F., Zarivach, R., Hansen, H.A., Fucini, P., Yonath, A., (2003) J. Bacterial., 185, pp. 4276-4279
Stark, H., Orlova, E.V., Rinke-Appel, J., Junke, N., Mueller, F., Rodnina, M., Wintermeyer, W., Van Heel, M., (1997) Cell, 88, pp. 19-28
Gabashvili, I.S., Agrawal, R.K., Grassucci, R., Squires, C.L., Dahlberg, A.E., Frank, J., (1999) Embo. J., 18, pp. 6501-6507
Pioletti, M., Schluenzen, F., Harms, J., Zarivach, R., Gluehmann, M., Avila, H., Bashan, A., Franceschi, F., (2001) Embo. J., 20, pp. 1829-1839
Yonath, A., (2002) Annu. Rev. Biophys. Biomol. Struct., 31, pp. 257-273
Kim, D.F., Green, R., (1999) Mol. Cell, 4, pp. 859-864
Wilson, K.S., Noller, H.F., (1998) Cell, 92, pp. 337-349
Moazed, D., Noller, H.F., (1989) Nature, 342, pp. 142-148
Green, R., Noller, H.F., (1997) Annu. Rev. Biochem., 66, pp. 679-716
Malkin, L.I., Rich, A., (1967) J. Mol. Biol., 26, pp. 329-346
Sabatini, D.D., Blobel, G., (1970) J. Cell. Biol., 45, pp. 146-157
Milligan, R.A., Unwin, P.N., (1986) Nature, 319, pp. 693-695
Yonath, A., Leonard, K.R., Wittmann, H.G., (1987) Science, 236, pp. 813-816
Frank, J., Zhu, J., Penczek, P., Li, Y., Srivastava, S., Verschoor, A., Radermacher, M., Agrawal, R.K., (1995) Nature, 376, pp. 441-444
Stark, H., Mueller, F., Orlova, E.V., Schatz, M., Dube, P., Erdemir, T., Zemlin, F., Van Heel, M., (1995) Structure, 3, pp. 815-821
Eisenstein, M., Hardesty, B., Odom, O.W., Kudlicki, W., Kramer, G., Arad, T., Franceschi, F., Yonath, A., (1994) Supramolecular Structure and Function, pp. 213-246. , Pifat G (ed). Balaban Press: Rehovot
Kurzchalia, T.V., Wiedmann, M., Breter, H., Zimmermann, W., Bauschke, E., Rapoport, T.A., (1988) Eur. J. Biochem., 172, pp. 663-668
Nakatogawa, H., Ito, K., (2002) Cell, 108, pp. 629-636
Nierhaus, K.H., Schulze, H., Cooperman, B.S., (1980) Biochem. Int., 1, pp. 185-192
Katunin, V., Muth, G., Strobel, S., Wintermeyer, W., Mol, R.M., (2002) Cell., 10, pp. 339-346
Rodnina, M.V., Wintermeyer, W., (2001) Trends. Biochem. Sci., 26, pp. 124-130
Schmeing, T.M., Seila, A.C., Hansen, J.L., Freeborn, B., Soukup, J.K., Scaringe, S.A., Strobel, S.A., Steitz, T.A., (2002) Nat. Struct. Biol., 9, pp. 225-230
Hansen, J.L., Schmeing, T.M., Moore, P.B., Steitz, T.A., (2002) Proc. Natl. Acad. Sci. USA, 99, pp. 11670-11675
Yonath, A., (2003) Chem. Bio. Chem., 4, pp. 1008-1017
Miskin, R., Zamir, A., Biochem, E.D., (1968) Biophys. Res. Commun., 33, pp. 551-557
Vogel, Z., Vogel, T., Zamir, A., Elson, D., (1971) J. Mol. Biol., 60, pp. 339-346
Zamir, A., Miskin, R., Vogel, Z., Elson, D., (1974) Methods Enzymol., 30, pp. 406-426
Bayfield, M.A., Dahlberg, A.E., Schulmeister, U., Dorner, S., Barta, A., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 10096-10101
Agrawal, R.K., Penczek, P., Grassucci, R.A., Burkhardt, N., Nierhaus, K.H., Frank, J., (1999) J. Biol. Chem., 274, pp. 8723-8729
Calendar, R., Berg, P., (1967) J. Mol. Biol., 26, pp. 39-54
Briza, P., Ellinger, A., Winkler, G., Breitenbach, M., (1990) J. Biol. Chem., 265, pp. 15118-15123
Cosloy, S.D., McFall, E., (1973) J. Bacteriol., 114, pp. 685-694
Soutourina, J., Blanquet, S., Plateau, P., (2000) J. Biol. Chem., 275, pp. 11626-11630
Yamane, T., Miller, D.L., Hopfield, J.J., (1981) Biochemistry, 20, pp. 7059-7064
Heckler, T.G., Roesser, J.R., Xu, C., Chang, P.I., Hecht, S.M., (1988) Biochemistry, 27, pp. 7254-7262
Bain, J.D., Diala, E.S., Glabe, C.G., Wacker, D.A., Lyttle, M.H., Dix, T.A., Chamberlin, A.R., (1991) Biochemistry, 30, pp. 5411-5421
Dedkova, L.M., Fahmi, N.E., Golovine, S.Y., Hecht, S.M., (2003) J. Am. Chem. Soc., 125, pp. 6616-6617
Gabashvili, I.S., Gregory, S.T., Valle, M., Grassucci, R., Worbs, M., Wahl, M.C., Dahlberg, A.E., Frank, J., (2001) Mol. Cell., 8, pp. 181-188
Tenson, T., Ehrenberg, M., (2002) Cell, 108, pp. 591-594
Gong, F., Yanofsky, C., (2002) Science, 297, pp. 1864-1867
Liao, S., Lin, J., Do, H., Johnson, A.E., (1997) Cell, 90, pp. 31-41
Stroud, R.M., Walter, P., (1999) Curr. Opin. Struct. Biol., 9, pp. 754-759
Morris, D.R., Geballe, A.P., (2000) Mol. Cell. Biol., 20, pp. 8635-8642
Chepkwony, H.K., Roets, E., Hoogmartens, J., (2001) J. Chromatogr. A, 914, pp. 53-58
Auerbach, T., Bashan, A., Harms, J., Schluenzen, F., Zarivach, R., Bartels, H., Agmon, I., Yonath, A., (2002) Curr. Drug Targets-infect. Disord., 2, pp. 169-186
Unge, J., Berg, A., Al-Kharadaghi, S., Nikulin, A., Nikonov, S., Davydova, N., Nevskaya, N., Liljas, A., (1998) Structure, 6, pp. 1577-1586
Davydova, N., Streltsov, V., Wilce, M., Liljas, A., Garber, M., (2002) J. Mol. Biol., 322, pp. 635-644
White, O., Eisen, J.A., Heidelberg, J.F., Hickey, E.K., Peterson, J.D., Dodson, R.J., Haft, D.H., Fraser, C.L., (1999) Science, 286, pp. 1571-1577
Levin-Zaidman, S., Englander, A., Shimoni, E., Sharma, A., Minton, W., Minsky, A., (2003) Science, 299, pp. 254-256
Lu, M., Steitz, T.A., (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 2023-2028
Fedorov, R., Meshcheryakov, V., Gongadze, G., Fomenkova, N., Nevskaya, N., Seimer, M., Laurberg, M., Nikonov, S., (2001) Acta Crystallogr. D. Biol. Crystallogr., 57, pp. 968-976
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Functional aspects of ribosomal architecture: Symmetry, chirality and regulation
The functional aspects of ribosomal architecture were studied. The ribosome possesses three tRNA binding sites named according to their function. It was observed that the small ribosomal subunit facilitates the initiation of the translation process and is involved in choosing the frame to be translated. The high-resolution structures of both ribosomal subunits revealed that most stages of protein biosynthesis including decoding of genetic information are navigated and controlled by the elaborate ribosomal architectural design.
The functional aspects of ribosomal architecture were studied. The ribosome possesses three tRNA binding sites named according to their function. It was observed that the small ribosomal subunit facilitates the initiation of the translation process and is involved in choosing the frame to be translated. The high-resolution structures of both ribosomal subunits revealed that most stages of protein biosynthesis including decoding of genetic information are navigated and controlled by the elaborate ribosomal architectural design.
Functional aspects of ribosomal architecture: Symmetry, chirality and regulation
No results. Nessun risultato. |
Functional aspects of ribosomal architecture: Symmetry, chirality and regulation
Ruggiero A, Garcia-ortega L, Ragucci S, Russo R, Landi N, Berisio R, Di Maro A
* Structural and enzymatic properties of Ageritin, a novel metal-dependent ribotoxin-like protein with antitumor activity (208 visite)
Bba-Gen Subjects (ISSN: 1872-8006electronic, 0304-4165linking, 0304-4165print), 2018 Sep 18; 1862(12): 2888-2894.
Impact Factor: 3.679
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Corti N, Pfister P, Yonath A, Böttger EC
* 23S rRNA 2058A→G alteration mediates ketolide resistance in combination with deletion in L22 (276 visite)
Antimicrob Agents Ch (ISSN: 0066-4804, 1098-6596), 2006 Nov; 50(11): 3816-3823.
Impact Factor: 4.153
Dettagli Esporta in BibTeX Esporta in EndNote
Falcigno L, Oliva R, D'Auria G, Maletta M, Dettin M, Pasquato A, Di Bello C, Paolillo L
* Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site 3: Role of site-specific mutations (298 visite)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2004 Dec 3; 5(12): 1653-1661.
Impact Factor: 3.474
Dettagli Esporta in BibTeX Esporta in EndNote
Agmon I, Amit M, Auerbach T, Bashan A, Baram D, Bartels H, Berisio R, Greenberg I, Harms J, Hansen HAS, Kessler M, Pyetan E, Schluenzen F, Sittner A, Yonath A, Zarivach R
* Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism (257 visite)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2004 Jun 1; 567(1): 20-26.
Impact Factor: 3.843
Dettagli Esporta in BibTeX Esporta in EndNote
Bashan A, Zarivach R, Schluenzen F, Agmon I, Harms J, Auerbach T, Baram D, Berisio R, Bartels H, Hansen HAS, Fucini P, Wilson D, Peretz M, Kessler M, Yonath A
* Ribosomal crystallography: Peptide bond formation and its inhibition (423 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
Dettagli Esporta in BibTeX Esporta in EndNote
Agmon I, Auerbach T, Baram D, Bartels H, Bashan A, Berisio R, Fucini P, Hansen HA, Harms J, Kessler M, Peretz M, Schluenzen F, Yonath A, Zarivach R
* On Peptide Bond Formation, Translocation, Nascent Protein Progression And The Regulatory Properties Of Ribosomes. Derived On 20 October 2002 At The 28th Febs Meeting In Istanbul (243 visite)
Chembiochem, 2003 Jun; 270(12): 2543-2556.
Impact Factor: 3.06
Dettagli Esporta in BibTeX Esporta in EndNote
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Ruggiero A, Garcia-ortega L, Ragucci S, Russo R, Landi N, Berisio R, Di Maro A
* Structural and enzymatic properties of Ageritin, a novel metal-dependent ribotoxin-like protein with antitumor activity (208 visite)
Bba-Gen Subjects (ISSN: 1872-8006electronic, 0304-4165linking, 0304-4165print), 2018 Sep 18; 1862(12): 2888-2894.
Impact Factor: 3.679
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Corti N, Pfister P, Yonath A, Böttger EC
* 23S rRNA 2058A→G alteration mediates ketolide resistance in combination with deletion in L22 (276 visite)
Antimicrob Agents Ch (ISSN: 0066-4804, 1098-6596), 2006 Nov; 50(11): 3816-3823.
Impact Factor: 4.153
Dettagli Esporta in BibTeX Esporta in EndNote
Falcigno L, Oliva R, D'Auria G, Maletta M, Dettin M, Pasquato A, Di Bello C, Paolillo L
* Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site 3: Role of site-specific mutations (298 visite)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2004 Dec 3; 5(12): 1653-1661.
Impact Factor: 3.474
Dettagli Esporta in BibTeX Esporta in EndNote
Agmon I, Amit M, Auerbach T, Bashan A, Baram D, Bartels H, Berisio R, Greenberg I, Harms J, Hansen HAS, Kessler M, Pyetan E, Schluenzen F, Sittner A, Yonath A, Zarivach R
* Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism (257 visite)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2004 Jun 1; 567(1): 20-26.
Impact Factor: 3.843
Dettagli Esporta in BibTeX Esporta in EndNote
Bashan A, Zarivach R, Schluenzen F, Agmon I, Harms J, Auerbach T, Baram D, Berisio R, Bartels H, Hansen HAS, Fucini P, Wilson D, Peretz M, Kessler M, Yonath A
* Ribosomal crystallography: Peptide bond formation and its inhibition (423 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
Dettagli Esporta in BibTeX Esporta in EndNote
Agmon I, Auerbach T, Baram D, Bartels H, Bashan A, Berisio R, Fucini P, Hansen HA, Harms J, Kessler M, Peretz M, Schluenzen F, Yonath A, Zarivach R
* On Peptide Bond Formation, Translocation, Nascent Protein Progression And The Regulatory Properties Of Ribosomes. Derived On 20 October 2002 At The 28th Febs Meeting In Istanbul (243 visite)
Chembiochem, 2003 Jun; 270(12): 2543-2556.
Impact Factor: 3.06
Dettagli Esporta in BibTeX Esporta in EndNote
6 Records (6 escludendo Abstract e Conferenze).
Impact factor totale: 20.942 (20.942 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 22.167 (22.167 escludendo Abstract e Conferenze).
Impact factor totale: 20.942 (20.942 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 22.167 (22.167 escludendo Abstract e Conferenze).
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