A crevice adjoining the ribosome tunnel: Hints for cotranslational folding (388 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2005 Jun 13; 579(15): 3207-3213.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.415, 5-year impact factor: 3.47
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-20444368456&partnerID=40&md5=31b03359939e6d76030d38e63247a910
Keywords: Cotranslational Folding, Macrolide Binding Pocket, Nascent Chain, Rapamycin, Ribosome, Tunnel Crevice, Ketolide, Membrane Protein, Polyketide, Article, Binding Site, Controlled Study, Crystal Structure, Deinococcus Radiodurans, Dna Footprinting, Nonhuman, Priority Journal, Protein Binding, Protein Folding, Protein Localization, Ribosome Subunit, Base Sequence, Crystallography, X-Ray, Models, Molecular, Molecular Structure, Nucleic Acid Conformation, Protein Biosynthesis, 23s, Sirolimus,
Affiliations:
*** IBB - CNR ***
Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel
Institute of Biostructure and Bioimaging, CNR, 80138 Napoli, Italy
Max-Planck Research Unit for Ribosomal Structure, Hamburg 22603, Germany
References:
Ban, N., Nissen, P., Hansen, J., Moore, P.B., Steitz, T.A., The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution (2000) Science, 289, pp. 905-92
Harms, J., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Yonath, A., High resolution structure of the large ribosomal subunit from a mesophilic eubacterium (2001) Cell, 107, pp. 679-688
Walter, P., Johnson, A.E., Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane (1994) Annu. Rev. Cell Biol., 10, pp. 87-119
Stroud, R.M., Walter, P., Signal sequence recognition and protein targeting (1999) Curr. Opin. Struct. Biol., 9, pp. 754-759
Tenson, T., Ehrenberg, M., Regulatory nascent peptides in the ribosomal tunnel (2002) Cell, 108, pp. 591-594
White, S.H., Von Heijne, G., The machinery of membrane protein assembly (2004) Curr. Opin. Struct. Biol., 14, pp. 397-404
Etchells, S.A., Hartl, F.U., The dynamic tunnel (2004) Nat. Struct. Mol. Biol., 11, pp. 391-392
Johnson, A.E., The co-translational folding and interactions of nascent protein chains: A new approach using fluorescence resonance energy transfer (2005) FEBS Lett., 579, pp. 916-920
Berisio, R., Schluenzen, F., Harms, J., Bashan, A., Auerbach, T., Baram, D., Yonath, A., Structural insight into the role of the ribosomal tunnel in cellular regulation (2003) Nat. Struct. Biol., 10, pp. 366-370
Nakatogawa, H., Ito, K., The ribosomal exit tunnel functions as a discriminating gate (2002) Cell, 108, pp. 629-636
Gong, F., Yanofsky, C., Instruction of translating ribosome by nascent peptide (2002) Science, 297, pp. 1864-1867
Bashan, A., Agmon, I., Zarivach, R., Schluenzen, F., Harms, J., Berisio, R., Bartels, H., Yonath, A., Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression (2003) Mol. Cell, 11, pp. 91-102
Bashan, A., Zarivach, R., Schluenzen, F., Agmon, I., Harms, J., Auerbach, T., Baram, D., Yonath, A., Ribosomal crystallography: Peptide bond formation and its inhibition (2003) Biopolymers, 70, pp. 19-41
Agmon, I., Auerbach, T., Baram, D., Bartels, H., Bashan, A., Berisio, R., Fucini, P., Zarivach, R., On peptide bond formation, translocation, nascent protein progression and the regulatory properties of ribosomes (2003) Eur. J. Biochem., 270, pp. 2543-2556
Berisio, R., Harms, J., Schluenzen, F., Zarivach, R., Hansen, H.A., Fucini, P., Yonath, A., Structural insight into the antibiotic action of telithromycin against resistant mutants (2003) J. Bacteriol., 185, pp. 4276-4279
Auerbach, T., Bashan, A., Yonath, A., Ribosomal antibiotics: Structural basis for resistance, synergism and selectivity (2004) Trends Biotechnol., 22, pp. 570-576
Wittmann, H.G., Stoffler, G., Apirion, D., Rosen, L., Tanaka, K., Tamaki, M., Takata, R., Otaka, E., Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins (1973) Mol. Gen. Genet., 127, pp. 175-189
Davydova, N., Streltsov, V., Wilce, M., Liljas, A., Garber, M., L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin (2002) J. Mol. Biol., 322, pp. 635-644
Gabashvili, I.S., Gregory, S.T., Valle, M., Grassucci, R., Worbs, M., Wahl, M.C., Dahlberg, A.E., Frank, J., The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22 (2001) Mol. Cell, 8, pp. 181-188
Ranganathan, A., Timoney, M., Bycroft, M., Cortes, J., Thomas, I.P., Wilkinson, B., Kellenberger, L., Leadlay, P.F., Knowledge-based design of bimodular and trimodular polyketide synthases based on domain and module swaps: A route to simple statin analogues (1999) Chem. Biol., 6, pp. 731-741
Rowe, C.J., Bohm, I.U., Thomas, I.P., Wilkinson, B., Rudd, B.A., Foster, G., Blackaby, A.P., Leadlay, P.F., Engineering a polyketide with a longer chain by insertion of an extra module into the erythromycin-producing polyketide synthase (2001) Chem. Biol., 8, pp. 475-485
Raught, B., Gingras, A.C., Sonenberg, N., The target of rapamycin (TOR) proteins (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 7037-7044
Powers, T., Walter, P., Regulation of ribosome biogenesis by the rapamycin-sensitive TOR-signaling pathway in Saccharomyces cerevisiae (1999) Mol. Biol. Cell, 10, pp. 987-1000
Zaragoza, D., Ghavidel, A., Heitman, J., Schultz, M.C., Rapamycin induces the G0 program of transcriptional repression in yeast by interfering with the TOR signaling pathway (1998) Mol. Cell. Biol., 18, pp. 4463-4470
Martin, D.E., Soulard, A., Hall, M.N., TOR regulates ribosomal protein gene expression via PKA and the Forkhead transcription factor FHL1 (2004) Cell, 119, pp. 969-979
Preiss, T., Baron-Benhamou, J., Ansorge, W., Hentze, M.W., Homodirectional changes in transcriptome composition and mRNA translation induced by rapamycin and heat shock (2003) Nat. Struct. Biol., 10, pp. 1039-1047
Dennis, P.B., Jaeschke, A., Saitoh, M., Fowler, B., Kozma, S.C., Thomas, G., Mammalian TOR: A homeostatic ATP sensor (2001) Science, 294, pp. 1102-1105
Kim, W.S., Xu, L., Souw, D., Fang, A., Demain, A.L., An unexpected inhibitory effect of rapamycin against germination of spores of Bacillus brevis strain Nagano (2002) J. Antibiot., 55, pp. 650-654
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods in Enzymology Macromolecular Crystallography, Part A, 276, pp. 307-326. , C.W. Carter Jr. R.M. Sweet Academic Press London
Brunger, A.T., Adams, P.D., Clore, G.M., Delano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Warren, G.L., Crystallography and NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr. D, 54, pp. 905-921
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. a, 47, pp. 110-119
Bailey, S., The CCP4 suite - Programs for protein crystallography (1994) Acta Crystallogr. D, 50, pp. 760-763
Carson, M., Ribbons (1997) Methods in Enzymology, Macromol. Crystallogr. B, 277, pp. 493-505. , R.M. Sweet C.W. Carter Academic Press New York
Merryman, C., Noller, H.F., Footprinting and modification-interference analysis of binding sites on RNA (1998) RNA:Protein Interactions, pp. 237-253. , C.W.J. Smith Oxford University Press UK, Oxford
Yusupov, M.M., Yusupova, G.Z., Baucom, A., Lieberman, K., Earnest, T.N., Cate, J.H., Noller, H.F., Crystal structure of the ribosome at 5.5 Å resolution (2001) Science, 292, pp. 883-896
Weisblum, B., Erythromycin resistance by ribosome modification (1995) Antimicrob. Agents Chemother., 39, pp. 577-585
Douthwaite, S., Champney, W.S., Structures of ketolides and macrolides determine their mode of interaction with the ribosomal target site (2001) J. Antimicrob. Chemother., 48, pp. 1-8
Woolhead, C.A., McCormick, P.J., Johnson, A.E., Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins (2004) Cell, 116, pp. 725-736
Pfister, P., Corti, N., Hobbie, S., Bruell, C., Zarivach, R., Yonath, A., Bottger, E.C., 23S rRNA base-pair 2057-2611 determines ketolide susceptibility and fitness cost of the macrolide resistance mutation 2058A → G (2005) Proc. Natl. Acad. Sci. USA, , in press
Gilbert, R.J., Fucini, P., Connell, S., Fuller, S.D., Nierhaus, K.H., Robinson, C.V., Dobson, C.M., Stuart, D.I., Three-dimensional structures of translating ribosomes by Cryo-EM (2004) Mol. Cell, 14, pp. 57-66
Hansen, J.L., Ippolito, J.A., Ban, N., Nissen, P., Moore, P.B., Steitz, T.A., The structures of four macrolide antibiotics bound to the large ribosomal subunit (2002) Mol. Cell, 10, pp. 117-128
Stroud, R. M., Walter, P., Signal sequence recognition and protein targeting (1999) Curr. Opin. Struct. Biol., 9, pp. 754-759
White, S. H., Von Heijne, G., The machinery of membrane protein assembly (2004) Curr. Opin. Struct. Biol., 14, pp. 397-404
Etchells, S. A., Hartl, F. U., The dynamic tunnel (2004) Nat. Struct. Mol. Biol., 11, pp. 391-392
Johnson, A. E., The co-translational folding and interactions of nascent protein chains: A new approach using fluorescence resonance energy transfer (2005) FEBS Lett., 579, pp. 916-920
Wittmann, H. G., Stoffler, G., Apirion, D., Rosen, L., Tanaka, K., Tamaki, M., Takata, R., Otaka, E., Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins (1973) Mol. Gen. Genet., 127, pp. 175-189
Gabashvili, I. S., Gregory, S. T., Valle, M., Grassucci, R., Worbs, M., Wahl, M. C., Dahlberg, A. E., Frank, J., The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22 (2001) Mol. Cell, 8, pp. 181-188
Rowe, C. J., Bohm, I. U., Thomas, I. P., Wilkinson, B., Rudd, B. A., Foster, G., Blackaby, A. P., Leadlay, P. F., Engineering a polyketide with a longer chain by insertion of an extra module into the erythromycin-producing polyketide synthase (2001) Chem. Biol., 8, pp. 475-485
Martin, D. E., Soulard, A., Hall, M. N., TOR regulates ribosomal protein gene expression via PKA and the Forkhead transcription factor FHL1 (2004) Cell, 119, pp. 969-979
Dennis, P. B., Jaeschke, A., Saitoh, M., Fowler, B., Kozma, S. C., Thomas, G., Mammalian TOR: A homeostatic ATP sensor (2001) Science, 294, pp. 1102-1105
Kim, W. S., Xu, L., Souw, D., Fang, A., Demain, A. L., An unexpected inhibitory effect of rapamycin against germination of spores of Bacillus brevis strain Nagano (2002) J. Antibiot., 55, pp. 650-654
Brunger, A. T., Adams, P. D., Clore, G. M., Delano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Warren, G. L., Crystallography and NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr. D, 54, pp. 905-921
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. a, 47, pp. 110-119
Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H., Noller, H. F., Crystal structure of the ribosome at 5. 5 resolution (2001) Science, 292, pp. 883-896
Woolhead, C. A., McCormick, P. J., Johnson, A. E., Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins (2004) Cell, 116, pp. 725-736
Gilbert, R. J., Fucini, P., Connell, S., Fuller, S. D., Nierhaus, K. H., Robinson, C. V., Dobson, C. M., Stuart, D. I., Three-dimensional structures of translating ribosomes by Cryo-EM (2004) Mol. Cell, 14, pp. 57-66
Hansen, J. L., Ippolito, J. A., Ban, N., Nissen, P., Moore, P. B., Steitz, T. A., The structures of four macrolide antibiotics bound to the large ribosomal subunit (2002) Mol. Cell, 10, pp. 117-128
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2005 Jun 13; 579(15): 3207-3213.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.415, 5-year impact factor: 3.47
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-20444368456&partnerID=40&md5=31b03359939e6d76030d38e63247a910
Keywords: Cotranslational Folding, Macrolide Binding Pocket, Nascent Chain, Rapamycin, Ribosome, Tunnel Crevice, Ketolide, Membrane Protein, Polyketide, Article, Binding Site, Controlled Study, Crystal Structure, Deinococcus Radiodurans, Dna Footprinting, Nonhuman, Priority Journal, Protein Binding, Protein Folding, Protein Localization, Ribosome Subunit, Base Sequence, Crystallography, X-Ray, Models, Molecular, Molecular Structure, Nucleic Acid Conformation, Protein Biosynthesis, 23s, Sirolimus,
Affiliations:
*** IBB - CNR ***
Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel
Institute of Biostructure and Bioimaging, CNR, 80138 Napoli, Italy
Max-Planck Research Unit for Ribosomal Structure, Hamburg 22603, Germany
References:
Ban, N., Nissen, P., Hansen, J., Moore, P.B., Steitz, T.A., The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution (2000) Science, 289, pp. 905-92
Harms, J., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Yonath, A., High resolution structure of the large ribosomal subunit from a mesophilic eubacterium (2001) Cell, 107, pp. 679-688
Walter, P., Johnson, A.E., Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane (1994) Annu. Rev. Cell Biol., 10, pp. 87-119
Stroud, R.M., Walter, P., Signal sequence recognition and protein targeting (1999) Curr. Opin. Struct. Biol., 9, pp. 754-759
Tenson, T., Ehrenberg, M., Regulatory nascent peptides in the ribosomal tunnel (2002) Cell, 108, pp. 591-594
White, S.H., Von Heijne, G., The machinery of membrane protein assembly (2004) Curr. Opin. Struct. Biol., 14, pp. 397-404
Etchells, S.A., Hartl, F.U., The dynamic tunnel (2004) Nat. Struct. Mol. Biol., 11, pp. 391-392
Johnson, A.E., The co-translational folding and interactions of nascent protein chains: A new approach using fluorescence resonance energy transfer (2005) FEBS Lett., 579, pp. 916-920
Berisio, R., Schluenzen, F., Harms, J., Bashan, A., Auerbach, T., Baram, D., Yonath, A., Structural insight into the role of the ribosomal tunnel in cellular regulation (2003) Nat. Struct. Biol., 10, pp. 366-370
Nakatogawa, H., Ito, K., The ribosomal exit tunnel functions as a discriminating gate (2002) Cell, 108, pp. 629-636
Gong, F., Yanofsky, C., Instruction of translating ribosome by nascent peptide (2002) Science, 297, pp. 1864-1867
Bashan, A., Agmon, I., Zarivach, R., Schluenzen, F., Harms, J., Berisio, R., Bartels, H., Yonath, A., Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression (2003) Mol. Cell, 11, pp. 91-102
Bashan, A., Zarivach, R., Schluenzen, F., Agmon, I., Harms, J., Auerbach, T., Baram, D., Yonath, A., Ribosomal crystallography: Peptide bond formation and its inhibition (2003) Biopolymers, 70, pp. 19-41
Agmon, I., Auerbach, T., Baram, D., Bartels, H., Bashan, A., Berisio, R., Fucini, P., Zarivach, R., On peptide bond formation, translocation, nascent protein progression and the regulatory properties of ribosomes (2003) Eur. J. Biochem., 270, pp. 2543-2556
Berisio, R., Harms, J., Schluenzen, F., Zarivach, R., Hansen, H.A., Fucini, P., Yonath, A., Structural insight into the antibiotic action of telithromycin against resistant mutants (2003) J. Bacteriol., 185, pp. 4276-4279
Auerbach, T., Bashan, A., Yonath, A., Ribosomal antibiotics: Structural basis for resistance, synergism and selectivity (2004) Trends Biotechnol., 22, pp. 570-576
Wittmann, H.G., Stoffler, G., Apirion, D., Rosen, L., Tanaka, K., Tamaki, M., Takata, R., Otaka, E., Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins (1973) Mol. Gen. Genet., 127, pp. 175-189
Davydova, N., Streltsov, V., Wilce, M., Liljas, A., Garber, M., L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin (2002) J. Mol. Biol., 322, pp. 635-644
Gabashvili, I.S., Gregory, S.T., Valle, M., Grassucci, R., Worbs, M., Wahl, M.C., Dahlberg, A.E., Frank, J., The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22 (2001) Mol. Cell, 8, pp. 181-188
Ranganathan, A., Timoney, M., Bycroft, M., Cortes, J., Thomas, I.P., Wilkinson, B., Kellenberger, L., Leadlay, P.F., Knowledge-based design of bimodular and trimodular polyketide synthases based on domain and module swaps: A route to simple statin analogues (1999) Chem. Biol., 6, pp. 731-741
Rowe, C.J., Bohm, I.U., Thomas, I.P., Wilkinson, B., Rudd, B.A., Foster, G., Blackaby, A.P., Leadlay, P.F., Engineering a polyketide with a longer chain by insertion of an extra module into the erythromycin-producing polyketide synthase (2001) Chem. Biol., 8, pp. 475-485
Raught, B., Gingras, A.C., Sonenberg, N., The target of rapamycin (TOR) proteins (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 7037-7044
Powers, T., Walter, P., Regulation of ribosome biogenesis by the rapamycin-sensitive TOR-signaling pathway in Saccharomyces cerevisiae (1999) Mol. Biol. Cell, 10, pp. 987-1000
Zaragoza, D., Ghavidel, A., Heitman, J., Schultz, M.C., Rapamycin induces the G0 program of transcriptional repression in yeast by interfering with the TOR signaling pathway (1998) Mol. Cell. Biol., 18, pp. 4463-4470
Martin, D.E., Soulard, A., Hall, M.N., TOR regulates ribosomal protein gene expression via PKA and the Forkhead transcription factor FHL1 (2004) Cell, 119, pp. 969-979
Preiss, T., Baron-Benhamou, J., Ansorge, W., Hentze, M.W., Homodirectional changes in transcriptome composition and mRNA translation induced by rapamycin and heat shock (2003) Nat. Struct. Biol., 10, pp. 1039-1047
Dennis, P.B., Jaeschke, A., Saitoh, M., Fowler, B., Kozma, S.C., Thomas, G., Mammalian TOR: A homeostatic ATP sensor (2001) Science, 294, pp. 1102-1105
Kim, W.S., Xu, L., Souw, D., Fang, A., Demain, A.L., An unexpected inhibitory effect of rapamycin against germination of spores of Bacillus brevis strain Nagano (2002) J. Antibiot., 55, pp. 650-654
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods in Enzymology Macromolecular Crystallography, Part A, 276, pp. 307-326. , C.W. Carter Jr. R.M. Sweet Academic Press London
Brunger, A.T., Adams, P.D., Clore, G.M., Delano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Warren, G.L., Crystallography and NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr. D, 54, pp. 905-921
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. a, 47, pp. 110-119
Bailey, S., The CCP4 suite - Programs for protein crystallography (1994) Acta Crystallogr. D, 50, pp. 760-763
Carson, M., Ribbons (1997) Methods in Enzymology, Macromol. Crystallogr. B, 277, pp. 493-505. , R.M. Sweet C.W. Carter Academic Press New York
Merryman, C., Noller, H.F., Footprinting and modification-interference analysis of binding sites on RNA (1998) RNA:Protein Interactions, pp. 237-253. , C.W.J. Smith Oxford University Press UK, Oxford
Yusupov, M.M., Yusupova, G.Z., Baucom, A., Lieberman, K., Earnest, T.N., Cate, J.H., Noller, H.F., Crystal structure of the ribosome at 5.5 Å resolution (2001) Science, 292, pp. 883-896
Weisblum, B., Erythromycin resistance by ribosome modification (1995) Antimicrob. Agents Chemother., 39, pp. 577-585
Douthwaite, S., Champney, W.S., Structures of ketolides and macrolides determine their mode of interaction with the ribosomal target site (2001) J. Antimicrob. Chemother., 48, pp. 1-8
Woolhead, C.A., McCormick, P.J., Johnson, A.E., Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins (2004) Cell, 116, pp. 725-736
Pfister, P., Corti, N., Hobbie, S., Bruell, C., Zarivach, R., Yonath, A., Bottger, E.C., 23S rRNA base-pair 2057-2611 determines ketolide susceptibility and fitness cost of the macrolide resistance mutation 2058A → G (2005) Proc. Natl. Acad. Sci. USA, , in press
Gilbert, R.J., Fucini, P., Connell, S., Fuller, S.D., Nierhaus, K.H., Robinson, C.V., Dobson, C.M., Stuart, D.I., Three-dimensional structures of translating ribosomes by Cryo-EM (2004) Mol. Cell, 14, pp. 57-66
Hansen, J.L., Ippolito, J.A., Ban, N., Nissen, P., Moore, P.B., Steitz, T.A., The structures of four macrolide antibiotics bound to the large ribosomal subunit (2002) Mol. Cell, 10, pp. 117-128
Stroud, R. M., Walter, P., Signal sequence recognition and protein targeting (1999) Curr. Opin. Struct. Biol., 9, pp. 754-759
White, S. H., Von Heijne, G., The machinery of membrane protein assembly (2004) Curr. Opin. Struct. Biol., 14, pp. 397-404
Etchells, S. A., Hartl, F. U., The dynamic tunnel (2004) Nat. Struct. Mol. Biol., 11, pp. 391-392
Johnson, A. E., The co-translational folding and interactions of nascent protein chains: A new approach using fluorescence resonance energy transfer (2005) FEBS Lett., 579, pp. 916-920
Wittmann, H. G., Stoffler, G., Apirion, D., Rosen, L., Tanaka, K., Tamaki, M., Takata, R., Otaka, E., Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins (1973) Mol. Gen. Genet., 127, pp. 175-189
Gabashvili, I. S., Gregory, S. T., Valle, M., Grassucci, R., Worbs, M., Wahl, M. C., Dahlberg, A. E., Frank, J., The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22 (2001) Mol. Cell, 8, pp. 181-188
Rowe, C. J., Bohm, I. U., Thomas, I. P., Wilkinson, B., Rudd, B. A., Foster, G., Blackaby, A. P., Leadlay, P. F., Engineering a polyketide with a longer chain by insertion of an extra module into the erythromycin-producing polyketide synthase (2001) Chem. Biol., 8, pp. 475-485
Martin, D. E., Soulard, A., Hall, M. N., TOR regulates ribosomal protein gene expression via PKA and the Forkhead transcription factor FHL1 (2004) Cell, 119, pp. 969-979
Dennis, P. B., Jaeschke, A., Saitoh, M., Fowler, B., Kozma, S. C., Thomas, G., Mammalian TOR: A homeostatic ATP sensor (2001) Science, 294, pp. 1102-1105
Kim, W. S., Xu, L., Souw, D., Fang, A., Demain, A. L., An unexpected inhibitory effect of rapamycin against germination of spores of Bacillus brevis strain Nagano (2002) J. Antibiot., 55, pp. 650-654
Brunger, A. T., Adams, P. D., Clore, G. M., Delano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Warren, G. L., Crystallography and NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr. D, 54, pp. 905-921
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. a, 47, pp. 110-119
Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H., Noller, H. F., Crystal structure of the ribosome at 5. 5 resolution (2001) Science, 292, pp. 883-896
Woolhead, C. A., McCormick, P. J., Johnson, A. E., Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins (2004) Cell, 116, pp. 725-736
Gilbert, R. J., Fucini, P., Connell, S., Fuller, S. D., Nierhaus, K. H., Robinson, C. V., Dobson, C. M., Stuart, D. I., Three-dimensional structures of translating ribosomes by Cryo-EM (2004) Mol. Cell, 14, pp. 57-66
Hansen, J. L., Ippolito, J. A., Ban, N., Nissen, P., Moore, P. B., Steitz, T. A., The structures of four macrolide antibiotics bound to the large ribosomal subunit (2002) Mol. Cell, 10, pp. 117-128
A crevice adjoining the ribosome tunnel: Hints for cotranslational folding
RNA protection experiments and the crystal structure of a complex of the large ribosomal subunit from the eubacterium Deinococcus radiodurans with rapamycin, a polyketide compound resembling macrolides and ketolides, showed that rapamycin binds to a crevice located at the boundaries of the nascent protein exit tunnel, near its entrance. At this location rapamycin cannot occlude the ribosome exit tunnel, consistent with its failure to act as a ribosomal antibiotic drug. In accord with recent biochemical data, this crevice may play a role in facilitating local cotranslational folding of nascent chains, in particular for transmembrane proteins. © 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
RNA protection experiments and the crystal structure of a complex of the large ribosomal subunit from the eubacterium Deinococcus radiodurans with rapamycin, a polyketide compound resembling macrolides and ketolides, showed that rapamycin binds to a crevice located at the boundaries of the nascent protein exit tunnel, near its entrance. At this location rapamycin cannot occlude the ribosome exit tunnel, consistent with its failure to act as a ribosomal antibiotic drug. In accord with recent biochemical data, this crevice may play a role in facilitating local cotranslational folding of nascent chains, in particular for transmembrane proteins. © 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
A crevice adjoining the ribosome tunnel: Hints for cotranslational folding
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A crevice adjoining the ribosome tunnel: Hints for cotranslational folding
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Impact Factor: 3.582
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Galdiero S, Vitiello M, Falanga A, Cantisani M, Incoronato N, Galdiero M
* Intracellular Delivery: Exploiting Viral Membranotropic Peptides (868 views)
Current Drug Metabolism (ISSN: 1389-2002), 2012 Jan; 13(1): 93-104.
Impact Factor: 4.405
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Barile E, Leone M, Barile E, Dahl R, Pellecchia M
* Design and NMR Studies of Cyclic Peptides Targeting the N-Terminal Domain of the Protein Tyrosine Phosphatase YopH (2177 views)
Chem Biol Drug Des (ISSN: 1747-0277, 1747-0285), 2011 Jan; 77(1): 12-19.
Impact Factor: 2.282
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Verardi R, Traaseth NJ, Shi L, Porcelli F, Monfregola L, De Luca S, Amodeo P, Veglia G, Scaloni A
* Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers (486 views)
Bba-Gen Subjects (ISSN: 0005-2736, 0006-3002, 0925-4439), 2011 Jan; 1808(1): 34-40.
Impact Factor: 3.99
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Leone M, Barile E, Vazquez J, Mei A, Guiney D, Dahl R, Pellecchia M
* NMR-based design and evaluation of novel bidentate inhibitors of the protein tyrosine phosphatase YopH (519 views)
Chem Biol Drug Des (ISSN: 1747-0277, 1747-0285), 2010 Jul; 76(1): 10-16.
Impact Factor: 2.527
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Calvanese L, Saporito A, Oliva R, D'Auria G, Pedone C, Paolillo L, Ruvo M, Marasco D, Falcigno L
* Structural insights into the interaction between the Cripto CFC domain and the ALK4 receptor (457 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 175-183.
Impact Factor: 1.807
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Hilvo M, Baranauskiene L, Salzano AM, Scaloni A, Matulis D, Innocenti A, Scozzafava A, Monti SM, Di Fiore A, De Simone G, Lindfors M, Janis J, Valjakka J, Pastorekova S, Pastorek J, Kulomaa MS, Nordlund HR, Supuran CT, Parkkila S
* Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymes (459 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 10; 283(41): 27799-27809.
Impact Factor: 5.52
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Merlino A, Varriale S, Coscia MR, Mazzarella L, Oreste U
* Structure and dimerization of the teleost transmembrane immunoglobulin region (377 views)
Journal Of Molecular Graphics & Modelling (ISSN: 1093-3263), 2008 Oct; 27(3): 401-407.
Impact Factor: 2.347
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Goldfine ID, Maddux BA, Youngren JF, Reaven G, Accili D, Trischitta V, Vigneri R, Frittitta L
* The role of membrane glycoprotein plasma cell antigen 1 ectonucleotide pyrophosphatase phosphodiesterase 1 in the pathogenesis of insulin resistance and related abnormalities (874 views)
Endocrine Reviews (ISSN: 0163-769x), 2008 Feb; 29(1): 62-75.
Impact Factor: 18.562
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Galdiero S, Falanga A, Vitiello M, D'Isanto M, Collins C, Orrei V, Browne H, Pedone C, Galdiero M
* Evidence for a role of the membrane-proximal region of herpes simplex virus type 1 glycoprotein H in membrane fusion and virus inhibition (584 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2007 May 25; 8(8): 885-895.
Impact Factor: 3.446
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Vitagliano L, Ruggiero A, Pedone C, Berisio R
* A Molecular Dynamics Study of Pilus Subunits: Insights into Pilus Biogenesis (447 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2007 Apr 6; 367(4): 935-941.
Impact Factor: 4.472
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Galdiero S, Galdiero M, Pedone C
* Beta-Barrel Membrane Bacterial Proteins: Structure, Function, Assembly And Interaction With Lipids (438 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2007 Feb; 8(1): 63-82.
Impact Factor: 3.259
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Calvanese L, Saporito A, Marasco D, D'Auria G, Minchiotti G, Pedone C, Paolillo L, Falcigno L, Ruvo M
* Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala (474 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Nov 30; 49(24): 7054-7062.
Impact Factor: 5.115
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Galdiero S, Gouaux E
* High Resolution Crystallographic Studies Of Alpha-Hemolysin-Phospholipid Complexes Define Heptamer-Lipid Head Group Interactions: Implication For Understanding Protein-Lipid Interactions (320 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2004 Jun; 13(6): 1503-1511.
Impact Factor: 4.116
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Galdiero M, Vitiello M, Galdiero S
* Eukaryotic cell signaling and transcriptional activation induced by bacterial porins (491 views)
Fems Microbiology Letters (ISSN: 0378-1097), 2003 Sep 12; 226(1): 57-64.
Impact Factor: 1.932
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Galdiero S, Capasso D, Vitiello M, D'Isanto M, Pedone C, Galdiero M
* Protein P2 from Haemophilus influenzae: The role of its surface exposed loops on the mitogen-activated protein kinase cascade (376 views)
Infection And Immunity (ISSN: 0019-9567), 2003 May; 71(5): 2798-2809.
Impact Factor: 3.875
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Bashan A, Agmon I, Zarivach R, Schluenzen F, Harms J, Berisio R, Bartels H, Franceschi F, Auerbach T, Hansen HAS, Kossoy E, Kessler M, Yonath A
* Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression (461 views)
Mol Cell (ISSN: 1097-2765, 1097-4164), 2003 Jan; 11(1): 91-102.
Impact Factor: 16.835
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Cardone L, de Cristofaro T, Affaitati A, Garbi C, Ginsberg MD, Saviano M, Varrone S, Rubin CS, Gottesman ME, Avvedimento EV, Feliciello A
* A-kinase anchor protein 84/121 are targeted to mitochondria and mitotic spindles by overlapping amino-terminal motifs (670 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2002 Jul 12; 320(3): 663-675.
Impact Factor: 5.359
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Del Vecchio S, Ciarmiello A, Salvatore M
Clinical imaging of multidrug resistance in cancer (361 views)
Q J Nucl Med (ISSN: 1124-3937, 1125-0135), 1999 Jun; 43(2): 125-131.
Impact Factor: 2.125
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Scala S, Pacelli R, Iaffaioli RV, Normanno N, Pepe S, Frasci G, Genua G, Tsuruo T, Tagliaferri P, Bianco AR
Reversal of adriamycin resistance by recombinant α-interferon in multidrug-resistant human colon carcinoma LoVo-doxorubicin cells (559 views)
Cancer Res (ISSN: 0008-5472, 1538-7445, 1538-7445electronic), 1991 Sep 15; 51(18): 4898-4902.
Impact Factor: 8.426
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38 Records (37 excluding Abstracts).
Total impact factor: 239.079 (229.736 excluding Abstracts).
Total 5 year impact factor: 242.306 (232.685 excluding Abstracts).
Total impact factor: 239.079 (229.736 excluding Abstracts).
Total 5 year impact factor: 242.306 (232.685 excluding Abstracts).
388 views. Last view on Friday 24 March 2023, 7:31:50
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