Structural insight into the role of the ribosomal tunnel in cellular regulation (375 views)
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 11.579, 5-year impact factor: 13
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0037407668&partnerID=40&md5=a06b97073a8686a4af5da9ba75c33f39
Keywords: Antibiotic Agent, Azithromycin, Erythromycin, Macrolide, Ribosome Protein, Ribosome Rna, Troleandomycin, Article, Biosynthesis, Cell, Crystal Structure, Deinococcus Radiodurans, Drug Binding, Drug Protein Binding, Nonhuman, Priority Journal, Protein Structure, Regulatory Mechanism, Structure Analysis, Amino Acid Sequence, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Conformation, Ribosomal Proteins, Signal Transduction,
Affiliations:
*** IBB - CNR ***
Max-Planck-Res. U. Ribosomal Struct., Hamburg, Germany
Inst. of Biostructure and Bioimaging, CNR, Napoli, Italy
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel
Institute of Biochemistry, Free University, Berlin, Germany
References:
Milligan, R.A., Unwin, P.N., Location of exit channel for nascent protein in 80S ribosome (1986) Nature, 319, pp. 693-69
Yonath, A., Leonard, K.R., Wittmann, H.G., A tunnel in the large ribosomal subunit revealed by three-dimensional image reconstruction (1987) Science, 236, pp. 813-816
Gabashvili, I.S., The polypeptide tunnel system in the ribosome and its gating in erythromycin resistant mutants of L 4 and L22 (2001) Mol. Cell, 8, pp. 181-188
Tenson, T., Ehrenberg, M., Regulatory nascent peptides in the ribosomal tunnel (2002) Cell, 108, pp. S91-S594
Morris, D.R., Geballe, A.P., Upstream open reading frames as regulators of mRNA translation (2000) Mol. Cell. Biol., 20, pp. 8635-8642
Sarker, S., Rudd, K.E., Oliver, D., Revised translation start site for secM defines an atypical signal peptide that regulates E. coli secA expression (2000) J. Bacteriol., 182, pp. 5592-5595
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
Stroud, R.M., Walter, P., Signal sequence recognition and protein targeting (1999) Curr. Opin. Struct. Biol., 9, pp. 754-759
Nissen, P., Hansen, J., Ban, N., Moore, P.B., Steitz, T.A., The structural basis of ribosome activity in peptide bond synthesis (2000) Science, 289, pp. 920-930
Harms, J., High resolution structure of the large ribosomal subunit from a mesophilic eubacterium (2001) Cell, 107, pp. 679-688
Unge, J., The crystal structure of ribosomal protein L22 from Thermus thermophilus: Insights into the mechanism of erythromycin resistance (1998) Structure, 6, pp. 1577-1586
Schluenzen, F., Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria (2001) Nature, 413, pp. 814-821
Hansen, J.L., The structures of four macrolide antibiotics bound to the large ribosomal subunit (2002) Mol. Cell, 10, pp. 117-128
Periti, P., Tonelli, F., Mazzei, T., Ficari, F., Antimicrobial chemoimmunoprophylaxis in colorectal surgery with cefotetan and thymostimulin: Prospective, controlled multicenter study (1993) J. Chemother., 5, pp. 37-42. , Italian Study Group on Antimicrobial Prophylaxis in Abdominal Surgery
Chepkwony, H.K., Roets, E., Hoogmartens, J., Liquid chromatography of troleandomycin (2001) J. Chromatogr. A, 914, pp. 53-58
Tenson, T., Mankin, A.S., Short peptides conferring resistance to macrolide antibiotics (2001) Peptides, 22, pp. 1661-1668
Verdier, L., Gharbi-Benarous, J., Bertho, G., Mauvais, P., Girault, J.P., Antibiotic resistance peptides: Interaction of peptides conferring macrolide and ketolide resistance with Staphylococcus aureus ribosomes: Conformation of bound peptides as determined by transferred NOE experiments (2002) Biochemistry, 41, pp. 4218-4229
Douthwaite, S., Hansen, L.H., Mauvais, P., Macrolide-ketolide inhibition of MLS-resistant ribosomes is improved by alternative drug interaction with domain II of 23S rRNA (2000) Mol. Microbiol., 36, pp. 183-193
Weisblum, B., Erythromycin resistance by ribosome modification. Antimicrob (1995) Agents Chemother., 39, pp. 577-585
Xiong, L., Shah, S., Mauvais, P., Mankin, A.S., A ketolide resistance mutation in domain II of 23S rRNA reveals the proximity of hairpin 35 to the peptidyl transferase centre (1999) Mol. Microbiol., 31, pp. 633-639
Goldman, R.C., Fesik, S.W., Doran, C.C., Role of protonated and neutral forms of macrolides in binding to ribosomes from Gram-positive and Gram-negative bacteria (1990) Antimicrob. Agents Chemother., 34, pp. 426-431
Davydova, N., Streltsov, V., Wilce, M., Liljas, A., Garber, M., L 22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin (2002) J. Mol. Biol., 322, pp. 635-644
Liao, S., Lin, J., Do, H., Johnson, A.E., Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration (1997) Cell, 90, pp. 31-41
Stern, S., Moazed, D., Noller, H.F., Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension (1988) Methods Enzymol., 164, pp. 481-489
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol., 276, pp. 307-326
Bailey, S., The CCP4 suite - Programs for protein crystallography (1994) Acta Crystallogr. D, 50, pp. 760-763
Brunger, A.T., Crystallography & 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, M., 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
Flocco, M.M., Mowbray, S.L., Cα-based torsion angles: A simple tool to analyze protein conformational changes (1995) Protein Sci., 4, pp. 2118-2122
Carson, M., Ribbons (1997) Methods Enzymol., 277, pp. 493-505
Wallace, A.C., Laskowski, R.A., Thornton, J.M., LIGPLOT a program to generate schematic diagrams of protein-ligand interactions (1995) Protein Eng., 8, pp. 127-134
Milligan, R. A., Unwin, P. N., Location of exit channel for nascent protein in 80S ribosome (1986) Nature, 319, pp. 693-69
Gabashvili, I. S., The polypeptide tunnel system in the ribosome and its gating in erythromycin resistant mutants of L 4 and L22 (2001) Mol. Cell, 8, pp. 181-188
Morris, D. R., Geballe, A. P., Upstream open reading frames as regulators of mRNA translation (2000) Mol. Cell. Biol., 20, pp. 8635-8642
Stroud, R. M., Walter, P., Signal sequence recognition and protein targeting (1999) Curr. Opin. Struct. Biol., 9, pp. 754-759
Hansen, J. L., The structures of four macrolide antibiotics bound to the large ribosomal subunit (2002) Mol. Cell, 10, pp. 117-128
Chepkwony, H. K., Roets, E., Hoogmartens, J., Liquid chromatography of troleandomycin (2001) J. Chromatogr. A, 914, pp. 53-58
Goldman, R. C., Fesik, S. W., Doran, C. C., Role of protonated and neutral forms of macrolides in binding to ribosomes from Gram-positive and Gram-negative bacteria (1990) Antimicrob. Agents Chemother., 34, pp. 426-431
Brunger, A. T., Crystallography & 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, M., 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
Flocco, M. M., Mowbray, S. L., C -based torsion angles: A simple tool to analyze protein conformational changes (1995) Protein Sci., 4, pp. 2118-2122
Wallace, A. C., Laskowski, R. A., Thornton, J. M., LIGPLOT a program to generate schematic diagrams of protein-ligand interactions (1995) Protein Eng., 8, pp. 127-134
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 11.579, 5-year impact factor: 13
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0037407668&partnerID=40&md5=a06b97073a8686a4af5da9ba75c33f39
Keywords: Antibiotic Agent, Azithromycin, Erythromycin, Macrolide, Ribosome Protein, Ribosome Rna, Troleandomycin, Article, Biosynthesis, Cell, Crystal Structure, Deinococcus Radiodurans, Drug Binding, Drug Protein Binding, Nonhuman, Priority Journal, Protein Structure, Regulatory Mechanism, Structure Analysis, Amino Acid Sequence, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Conformation, Ribosomal Proteins, Signal Transduction,
Affiliations:
*** IBB - CNR ***
Max-Planck-Res. U. Ribosomal Struct., Hamburg, Germany
Inst. of Biostructure and Bioimaging, CNR, Napoli, Italy
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel
Institute of Biochemistry, Free University, Berlin, Germany
References:
Milligan, R.A., Unwin, P.N., Location of exit channel for nascent protein in 80S ribosome (1986) Nature, 319, pp. 693-69
Yonath, A., Leonard, K.R., Wittmann, H.G., A tunnel in the large ribosomal subunit revealed by three-dimensional image reconstruction (1987) Science, 236, pp. 813-816
Gabashvili, I.S., The polypeptide tunnel system in the ribosome and its gating in erythromycin resistant mutants of L 4 and L22 (2001) Mol. Cell, 8, pp. 181-188
Tenson, T., Ehrenberg, M., Regulatory nascent peptides in the ribosomal tunnel (2002) Cell, 108, pp. S91-S594
Morris, D.R., Geballe, A.P., Upstream open reading frames as regulators of mRNA translation (2000) Mol. Cell. Biol., 20, pp. 8635-8642
Sarker, S., Rudd, K.E., Oliver, D., Revised translation start site for secM defines an atypical signal peptide that regulates E. coli secA expression (2000) J. Bacteriol., 182, pp. 5592-5595
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
Stroud, R.M., Walter, P., Signal sequence recognition and protein targeting (1999) Curr. Opin. Struct. Biol., 9, pp. 754-759
Nissen, P., Hansen, J., Ban, N., Moore, P.B., Steitz, T.A., The structural basis of ribosome activity in peptide bond synthesis (2000) Science, 289, pp. 920-930
Harms, J., High resolution structure of the large ribosomal subunit from a mesophilic eubacterium (2001) Cell, 107, pp. 679-688
Unge, J., The crystal structure of ribosomal protein L22 from Thermus thermophilus: Insights into the mechanism of erythromycin resistance (1998) Structure, 6, pp. 1577-1586
Schluenzen, F., Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria (2001) Nature, 413, pp. 814-821
Hansen, J.L., The structures of four macrolide antibiotics bound to the large ribosomal subunit (2002) Mol. Cell, 10, pp. 117-128
Periti, P., Tonelli, F., Mazzei, T., Ficari, F., Antimicrobial chemoimmunoprophylaxis in colorectal surgery with cefotetan and thymostimulin: Prospective, controlled multicenter study (1993) J. Chemother., 5, pp. 37-42. , Italian Study Group on Antimicrobial Prophylaxis in Abdominal Surgery
Chepkwony, H.K., Roets, E., Hoogmartens, J., Liquid chromatography of troleandomycin (2001) J. Chromatogr. A, 914, pp. 53-58
Tenson, T., Mankin, A.S., Short peptides conferring resistance to macrolide antibiotics (2001) Peptides, 22, pp. 1661-1668
Verdier, L., Gharbi-Benarous, J., Bertho, G., Mauvais, P., Girault, J.P., Antibiotic resistance peptides: Interaction of peptides conferring macrolide and ketolide resistance with Staphylococcus aureus ribosomes: Conformation of bound peptides as determined by transferred NOE experiments (2002) Biochemistry, 41, pp. 4218-4229
Douthwaite, S., Hansen, L.H., Mauvais, P., Macrolide-ketolide inhibition of MLS-resistant ribosomes is improved by alternative drug interaction with domain II of 23S rRNA (2000) Mol. Microbiol., 36, pp. 183-193
Weisblum, B., Erythromycin resistance by ribosome modification. Antimicrob (1995) Agents Chemother., 39, pp. 577-585
Xiong, L., Shah, S., Mauvais, P., Mankin, A.S., A ketolide resistance mutation in domain II of 23S rRNA reveals the proximity of hairpin 35 to the peptidyl transferase centre (1999) Mol. Microbiol., 31, pp. 633-639
Goldman, R.C., Fesik, S.W., Doran, C.C., Role of protonated and neutral forms of macrolides in binding to ribosomes from Gram-positive and Gram-negative bacteria (1990) Antimicrob. Agents Chemother., 34, pp. 426-431
Davydova, N., Streltsov, V., Wilce, M., Liljas, A., Garber, M., L 22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin (2002) J. Mol. Biol., 322, pp. 635-644
Liao, S., Lin, J., Do, H., Johnson, A.E., Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration (1997) Cell, 90, pp. 31-41
Stern, S., Moazed, D., Noller, H.F., Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension (1988) Methods Enzymol., 164, pp. 481-489
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol., 276, pp. 307-326
Bailey, S., The CCP4 suite - Programs for protein crystallography (1994) Acta Crystallogr. D, 50, pp. 760-763
Brunger, A.T., Crystallography & 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, M., 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
Flocco, M.M., Mowbray, S.L., Cα-based torsion angles: A simple tool to analyze protein conformational changes (1995) Protein Sci., 4, pp. 2118-2122
Carson, M., Ribbons (1997) Methods Enzymol., 277, pp. 493-505
Wallace, A.C., Laskowski, R.A., Thornton, J.M., LIGPLOT a program to generate schematic diagrams of protein-ligand interactions (1995) Protein Eng., 8, pp. 127-134
Milligan, R. A., Unwin, P. N., Location of exit channel for nascent protein in 80S ribosome (1986) Nature, 319, pp. 693-69
Gabashvili, I. S., The polypeptide tunnel system in the ribosome and its gating in erythromycin resistant mutants of L 4 and L22 (2001) Mol. Cell, 8, pp. 181-188
Morris, D. R., Geballe, A. P., Upstream open reading frames as regulators of mRNA translation (2000) Mol. Cell. Biol., 20, pp. 8635-8642
Stroud, R. M., Walter, P., Signal sequence recognition and protein targeting (1999) Curr. Opin. Struct. Biol., 9, pp. 754-759
Hansen, J. L., The structures of four macrolide antibiotics bound to the large ribosomal subunit (2002) Mol. Cell, 10, pp. 117-128
Chepkwony, H. K., Roets, E., Hoogmartens, J., Liquid chromatography of troleandomycin (2001) J. Chromatogr. A, 914, pp. 53-58
Goldman, R. C., Fesik, S. W., Doran, C. C., Role of protonated and neutral forms of macrolides in binding to ribosomes from Gram-positive and Gram-negative bacteria (1990) Antimicrob. Agents Chemother., 34, pp. 426-431
Brunger, A. T., Crystallography & 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, M., 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
Flocco, M. M., Mowbray, S. L., C -based torsion angles: A simple tool to analyze protein conformational changes (1995) Protein Sci., 4, pp. 2118-2122
Wallace, A. C., Laskowski, R. A., Thornton, J. M., LIGPLOT a program to generate schematic diagrams of protein-ligand interactions (1995) Protein Eng., 8, pp. 127-134
Structural insight into the role of the ribosomal tunnel in cellular regulation
Nascent proteins emerge out of ribosomes through an exit tunnel, which was assumed to be a firmly built passive path. Recent biochemical results, however, indicate that the tunnel plays an active role in sequence-specific gating of nascent chains and in responding to cellular signals. Consistently, modulation of the tunnel shape, caused by the binding of the semi-synthetic macrolide troleandomycin to the large ribosomal subunit from Deinococcus radiodurans, was revealed crystallographically. The results provide insights into the tunnel dynamics at high resolution. Here we show that, in addition to the typical steric blockage of the ribosomal tunnel by macrolides, troleandomycin induces a conformational rearrangement in a wall constituent, protein L22, flipping the tip of its highly conserved β-hairpin across the tunnel. On the basis of mutations that alleviate elongation arrest, the tunnel motion could be correlated with sequence discrimination and gating, suggesting that specific arrest motifs within nascent chain sequences may induce a similar gating mechanism.
Nascent proteins emerge out of ribosomes through an exit tunnel, which was assumed to be a firmly built passive path. Recent biochemical results, however, indicate that the tunnel plays an active role in sequence-specific gating of nascent chains and in responding to cellular signals. Consistently, modulation of the tunnel shape, caused by the binding of the semi-synthetic macrolide troleandomycin to the large ribosomal subunit from Deinococcus radiodurans, was revealed crystallographically. The results provide insights into the tunnel dynamics at high resolution. Here we show that, in addition to the typical steric blockage of the ribosomal tunnel by macrolides, troleandomycin induces a conformational rearrangement in a wall constituent, protein L22, flipping the tip of its highly conserved β-hairpin across the tunnel. On the basis of mutations that alleviate elongation arrest, the tunnel motion could be correlated with sequence discrimination and gating, suggesting that specific arrest motifs within nascent chain sequences may induce a similar gating mechanism.
Structural insight into the role of the ribosomal tunnel in cellular regulation
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Structural insight into the role of the ribosomal tunnel in cellular regulation
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Ronga L, Langella E, Palladino P, Marasco D, Tizzano B, Saviano M, Pedone C, Improta R, Ruvo M
* Does Tetracycline Bind Helix 2 Of Prion? An Integrated Spectroscopical And Computational Study Of The Interaction Between The Antibiotic And Alpha Helix 2 Human Prion Protein Fragments (512 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Feb 15; 66(3): 707-715.
Impact Factor: 3.354
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Ronga L, Palladino P, Costantini S, Facchiano A, Ruvo M, Benedetti E, Ragone R, Rossi F
* Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides (553 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2007 Feb; 8(1): 83-90.
Impact Factor: 3.259
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Berisio R, Corti N, Pfister P, Yonath A, Böttger EC
* 23S rRNA 2058A→G alteration mediates ketolide resistance in combination with deletion in L22 (400 views)
Antimicrob Agents Ch (ISSN: 0066-4804, 1098-6596), 2006 Nov; 50(11): 3816-3823.
Impact Factor: 4.153
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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 (312 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2004 Jun 1; 567(1): 20-26.
Impact Factor: 3.843
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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 (544 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
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Berisio R, Harms J, Schluenzen F, Zarivach R, Hansen HAS, Fucini P, Yonath A
* Structural insight into the antibiotic action of telithromycin against resistant mutants (418 views)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2003 Jul; 185(14): 4276-4279.
Impact Factor: 4.175
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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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Monti SM, Fogliano V, Logrieco A, Ferracane R, Ritieni A
Simultaneous determination of beauvericin, enniatins, and fusaproliferin by high performance liquid chromatography (493 views)
J Agric Food Chem (ISSN: 0021-8561), 2000 Sep; 48(8): 3317-3320.
Impact Factor: 1.56
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* Lung structure and function similarities between primary ciliary dyskinesia and mild cystic fibrosis: a pilot study (1926 views)
Ital J Pediatr (ISSN: 1720-8424, 1824-7288), 2017 Apr; 43(1): 34-34.
Impact Factor: 1.776
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Galdiero S, Falanga A, Berisio R, Grieco P, Morelli G, Galdiero M
* Antimicrobial peptides as an opportunity against bacterial diseases (733 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2015 Mar 11; 22(14): 1665-1677.
Impact Factor: 3.455
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Berisio R
* Editorial: Molecular determinants of bacterial diseases (354 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2015; 22(14): 1640-1641.
Impact Factor: 3.455
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Malgieri G, Avitabile C, Palmieri M, D'Andrea LD, Isernia C, Romanelli A, Fattorusso R
* Structural basis of a temporin 1b analogue antimicrobial activity against gram negative bacteria determined by CD and NMR techniques in cellular environment (541 views)
Acs Chem Biol (ISSN: 1554-8929), 2015; 10(4): 965-969.
Impact Factor: 5.09
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Notomista E, Falanga A, Fusco S, Pirone L, Zanfardino A, Galdiero S, Varcamonti M, Pedone E, Contursi P
* The identification of a novel Sulfolobus islandicus CAMP-like peptide points to archaeal microorganisms as cell factories for the production of antimicrobial molecules (465 views)
Microb Cell Fact (ISSN: 1475-2859), 2015; 14(1): N/D-N/D.
Impact Factor: 3.744
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Morelli G, Saviano M, Grieco P
* The renaissance era of peptides in drug discovery at the 14th Naples workshop on bioactive peptides (413 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617linking), 2015; 21(5): 321-322.
Impact Factor: 1.951
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Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S
* Structural insights into and activity analysis of the antimicrobial peptide myxinidin (683 views)
Antimicrob Agents Ch (ISSN: 0066-4804, 1098-6596), 2014 Sep; 58(9): 5280-5290.
Impact Factor: 4.476
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Rai M, Kon K, Ingle A, Duran N, Galdiero S, Galdiero M
* Broad-spectrum bioactivities of silver nanoparticles: the emerging trends and future prospects (727 views)
Appl Microbiol Biot (ISSN: 0175-7598), 2014 Mar; 98(5): 1951-1961.
Impact Factor: 3.337
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Cantisani M, Leone M, Mignogna E, Kampanaraki K, Falanga A, Morelli G, Galdiero M, Galdiero S
* Structure-Activity Relations of Myxinidin, an Antibacterial Peptide Derived from the Epidermal Mucus of Hagfish (599 views)
Antimicrob Agents Ch (ISSN: 0066-4804, 1098-6596), 2013 Nov; 57(11): 5665-5673.
Impact Factor: 4.451
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Galdiero S, Falanga A, Cantisani M, Vitiello M, Morelli G, Galdiero M
* Peptide-Lipid Interactions: Experiments and Applications (1013 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2013 Sep; 14(9): 18758-18789.
Impact Factor: 2.339
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Avitabile C, Capparelli R, Rigano MM, Fulgione A, Barone A, Pedone C, Romanelli A
* Antimicrobial peptides from plants: Stabilization of the γ core of a tomato defensin by intramolecular disulfide bond (755 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2013 Apr; 19(4): 240-245.
Impact Factor: 1.862
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Galdiero S, Falanga A, Tarallo R, Russo L, Galdiero E, Cantisani M, Morelli G, Galdiero M
* Peptide inhibitors against herpes simplex virus infections (888 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2013 Mar; 19(3): 148-158.
Impact Factor: 1.862
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Galdiero S, Falanga A, Cantisani M, Tarallo R, della Pepa ME, D'Oriano V, Galdiero M
* Microbe-Host Interactions: Structure and Role of Gram-Negative Bacterial Porins (629 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 843-854.
Impact Factor: 2.326
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Berisio R
* Editorial: cell processes in bacterial diseases (409 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2012 Oct; 19(10): 1011-1012.
Impact Factor: 1.994
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De Simone G
* Editorial: Zinc Metallo-Enzymes As Target For Drug Design (423 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2012 Feb; 19(6): 820-1012.
Impact Factor: 4.07
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Galdiero S, Vitiello M, Falanga A, Cantisani M, Incoronato N, Galdiero M
* Intracellular Delivery: Exploiting Viral Membranotropic Peptides (853 views)
Current Drug Metabolism (ISSN: 1389-2002), 2012 Jan; 13(1): 93-104.
Impact Factor: 4.405
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Cantisani M, Vitiello M, Falanga A, Finamore E, Galdiero M, Galdiero S
* Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity (510 views)
Int J Nanomed (ISSN: 1178-2013, 1176-9114, 1178-2013electronic), 2012; 7: 2361-2371.
Impact Factor: 3.463
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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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Capparelli R, Romanelli A, Iannaccone M, Nocerino N, Ripa R, Pensato S, Pedone C, Iannelli D
* Synergistic antibacterial and anti-inflammatory activity of temporin A and modified temporin B in vivo (452 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2009 Sep 28; 4(9): e7191-e7191.
Impact Factor: 4.351
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Wekselman I, Davidovich C, Agmon I, Zimmerman E, Rozenberg H, Bashan A, Berisio R, Yonath A
* Ribosome's mode of function: Myths, facts and recent results (394 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 122-130.
Impact Factor: 1.807
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Sciacca MFM, Pappalardo M, Milardi D, Grasso DM, La Rosa C
* Calcium-Activated Membrane Interaction Of The Islet Amyloid Polypeptide: Implications In The Pathogenesis Of Type Ii Diabetes Mellitus (962 views)
Arch Biochem Biophys, 2008 Sep 15; 65(1-2): 291-298.
Impact Factor: 3.043
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Dalla Serra M, Cirioni O, Vitale RM, Renzone G, Coraiola M, Giacometti A, Potrich C, Baroni E, Guella G, Sanseverino M, De Luca S, Scalise G, Amodeo P, Scaloni A
* Structural features of distinctin affecting peptide biological and biochemical properties (529 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 29; 47(30): 7888-7899.
Impact Factor: 3.379
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Chambery A, Pisante M, Di Maro A, Di Zazzo E, Ruvo M, Costantini S, Colonna G, Parente A
* Invariant Ser211 is involved in the catalysis of PD-L4, type I RIP from Phytolacca dioica leaves (364 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Apr 1; 67(1): 209-218.
Impact Factor: 3.354
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Ronga L, Langella E, Palladino P, Marasco D, Tizzano B, Saviano M, Pedone C, Improta R, Ruvo M
* Does Tetracycline Bind Helix 2 Of Prion? An Integrated Spectroscopical And Computational Study Of The Interaction Between The Antibiotic And Alpha Helix 2 Human Prion Protein Fragments (512 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Feb 15; 66(3): 707-715.
Impact Factor: 3.354
View Export to BibTeX Export to EndNote
Ronga L, Palladino P, Costantini S, Facchiano A, Ruvo M, Benedetti E, Ragone R, Rossi F
* Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides (553 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2007 Feb; 8(1): 83-90.
Impact Factor: 3.259
View Export to BibTeX Export to 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 (400 views)
Antimicrob Agents Ch (ISSN: 0066-4804, 1098-6596), 2006 Nov; 50(11): 3816-3823.
Impact Factor: 4.153
View Export to BibTeX Export to 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 (312 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2004 Jun 1; 567(1): 20-26.
Impact Factor: 3.843
View Export to BibTeX Export to 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 (544 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
View Export to BibTeX Export to EndNote
Berisio R, Harms J, Schluenzen F, Zarivach R, Hansen HAS, Fucini P, Yonath A
* Structural insight into the antibiotic action of telithromycin against resistant mutants (418 views)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2003 Jul; 185(14): 4276-4279.
Impact Factor: 4.175
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
Monti SM, Fogliano V, Logrieco A, Ferracane R, Ritieni A
Simultaneous determination of beauvericin, enniatins, and fusaproliferin by high performance liquid chromatography (493 views)
J Agric Food Chem (ISSN: 0021-8561), 2000 Sep; 48(8): 3317-3320.
Impact Factor: 1.56
View Export to BibTeX Export to EndNote
32 Records (30 excluding Abstracts).
Total impact factor: 116.419 (110.292 excluding Abstracts).
Total 5 year impact factor: 121.53 (115.184 excluding Abstracts).
Total impact factor: 116.419 (110.292 excluding Abstracts).
Total 5 year impact factor: 121.53 (115.184 excluding Abstracts).
375 views. Last view on Wednesday 01 March 2023, 0:33:09
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