Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis (441 views visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2014 Jul; 101(7): 712-719.
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Paper type Tipo di articolo: Journal Article,
Impact factor: 2.385, 5-year impact factor Impact factor a 5 anni: 2.498
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84898955995&partnerID=40&md5=e09d6c40b41e0fa7eb75d7512c6a52b9
Keywords Parole chiave: Binding, Structure, Tuberculosis, Antibiotics, Polymers, Proteins, Structure (composition), Antibiotic Binding, Binding Properties, Mycobacterium Tuberculosis, Penicillin-Binding Proteins, Solution Structures, Structural Similarity, Binding Energy, Beta Lactam, Penicillin Binding Protein, Peptidoglycan, Pona2 Protein, Unclassified Drug, Alpha Helix, Article, Carboxy Terminal Sequence, Centrifugation, Complex Formation, Controlled Study, Dormancy, Enzyme Active Site, Heteronuclear Nuclear Magnetic Resonance, Heteronuclear Single Quantum Coherence, Isothermal Titration Calorimetry, Ligand Binding, Nonhuman, Nuclear Overhauser Effect, Pasta Domain, Protein Binding, Protein Conformation, Protein Domain, Protein Expression, Protein Secondary Structure, Sequence Analysis, Surface Plasmon Resonance, Surface Property,
Affiliations Affiliazioni:
*** IBB - CNR ***
CIRPeB, University of Naples Federico II, Naples, Italy
Department of Pharmacy, University of Naples Federico II, via Mezzocannone 16, 80134 Naples, Italy
Institute of Biostructures and Bioimaging-CNR, via Mezzocannone 16, 80134 Naples, Italy
Department of Chemical Sciences, University of Naples Federico II, via Cintia 45, 80126 Naples, Italy
References Riferimenti:
Morandi, M., Sali, M., Manganelli, R., Delogu, G., (2013) J Infect Dev Ctries, 7, pp. 169-18
Ruggiero, A., Marchant, J., Squeglia, F., Makarov, V., De Simone, A., Berisio, R., (2013) J Biomol Struct Dyn, 31, pp. 195-205
Ruggiero, A., De Simone, P., Smaldone, G., Squeglia, F., Berisio, R., (2012) Curr Protein Pept Sci, 13, pp. 756-766
Ruggiero, A., Marasco, D., Squeglia, F., Soldini, S., Pedone, E., Pedone, C., Berisio, R., (2010) Structure, 18, pp. 1184-1190
Ruggiero, A., Tizzano, B., Pedone, E., Pedone, C., Wilmanns, M., Berisio, R., (2009) J Mol Biol, 385, pp. 153-162
Correale, S., Ruggiero, A., Capparelli, R., Pedone, E., Berisio, R., (2013) Acta Crystallogr D Biol Crystallogr, 69, pp. 1697-1706
Sauvage, E., Kerff, F., Terrak, M., Ayala, J. A., Charlier, P., (2008) FEMS Microbiol Rev, 32, pp. 234-258
Mukamolova, G. V., Turapov, O. A., Young, D. I., Kaprelyants, A. S., Kell, D. B., Young, M., (2002) Mol Microbiol, 46, pp. 623-635
Van Gunsteren, W. F., Berendsen, H. J., Hermans, J., Hol, W. G., Postma, J. P., (1983) Proc Natl Acad Sci USA, 80, pp. 4315-4319
Chao, M. C., Kieser, K. J., Minami, S., Mavrici, D., Aldridge, B. B., Fortune, S. M., Alber, T., Rubin, E., (2013) J. PLOS Pathogens, 9, pp. e1003197
Chao, M. C., Rubin, E., (2010) J. Annu Rev Microbiol, 64, pp. 293-311
Sung, M. T., Lai, Y. T., Huang, C. Y., Chou, L. Y., Shih, H. W., Cheng, W. C., Wong, C. H., Ma, C., (2009) Proc Natl Acad Sci USA, 106, pp. 8824-8829
Dessen, A., Mouz, N., Gordon, E., Hopkins, J., Dideberg, O., (2001) J Biol Chem, 276, pp. 45106-45112
Yeats, C., Finn, R. D., Bateman, A., (2002) Trends Biochem Sci, 27, p. 438
Shah, I. M., Laaberki, M. H., Popham, D. L., Dworkin, (2008) J. Cell, 135, pp. 486-496
Squeglia, F., Marchetti, R., Ruggiero, A., Lanzetta, R., Marasco, D., Dworkin, J., Petoukhov, M., Silipo, A., (2011) J Am Chem Soc, 133, pp. 20676-20679
Mir, M., Asong, J., Li, X., Cardot, J., Boons, G. J., Husson, R. N., (2011) PLOS Pathogens, 7, pp. e1002182
Maestro, B., Novakova, L., Hesek, D., Lee, M., Leyva, E., Mobashery, S., Sanz, J. M., Branny, P., (2011) FEBS Lett, 585, pp. 357-363
Vandal, O. H., Pierini, L. M., Schnappinger, D., Nathan, C. F., Ehrt, S., (2008) Nat Med, 14, pp. 849-854
Patru, M. M., Pavelka, Jr. M. S., (2010) J Bacteriol, 192, pp. 3043-3054
Ruggiero, A., Squeglia, F., Marasco, D., Marchetti, R., Molinaro, A., Berisio, R., (2011) Biochem J, 435, pp. 33-41
Gordon, E., Mouz, N., Duee, E., Dideberg, O., (2000) J Mol Biol, 299, pp. 477-485
Hildebrand, A., Remmert, M., Biegert, A., Soding, (2009) J. Proteins, 77 (SUPPL. 9), pp. 128-132
Mathur, A., Shankaracharya, Vidyarthi, A. S., (2012) J Mol Model, 18, pp. 3021-3023
Cheng, T. J., Sung, M. T., Liao, H. Y., Chang, Y. F., Chen, C. W., Huang, C. Y., Chou, L. Y., Cheng, W. C., (2008) Proc Natl Acad Sci USA, 105, pp. 431-436
Hett, E. C., Chao, M. C., Steyn, A. J., Fortune, S. M., Deng, L. L., Rubin, E., (2007) J. Mol Microbiol, 66, pp. 658-668
Rodriguez, R., Chinea, G., Lopez, N., Pons, T., Vriend, G., (1998) Bioinformatics, 14, pp. 523-528
Koradi, R., Billeter, M., Wuthrich, K., (1996) J Mol Graph, 14, pp. 51-55. , 29-32
Poletto, M., Vascotto, C., Scognamiglio, P. L., Lirussi, L., Marasco, D., Tell, G., (2013) Biochem J, 452, pp. 545-557
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2014 Jul; 101(7): 712-719.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 2.385, 5-year impact factor Impact factor a 5 anni: 2.498
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84898955995&partnerID=40&md5=e09d6c40b41e0fa7eb75d7512c6a52b9
Keywords Parole chiave: Binding, Structure, Tuberculosis, Antibiotics, Polymers, Proteins, Structure (composition), Antibiotic Binding, Binding Properties, Mycobacterium Tuberculosis, Penicillin-Binding Proteins, Solution Structures, Structural Similarity, Binding Energy, Beta Lactam, Penicillin Binding Protein, Peptidoglycan, Pona2 Protein, Unclassified Drug, Alpha Helix, Article, Carboxy Terminal Sequence, Centrifugation, Complex Formation, Controlled Study, Dormancy, Enzyme Active Site, Heteronuclear Nuclear Magnetic Resonance, Heteronuclear Single Quantum Coherence, Isothermal Titration Calorimetry, Ligand Binding, Nonhuman, Nuclear Overhauser Effect, Pasta Domain, Protein Binding, Protein Conformation, Protein Domain, Protein Expression, Protein Secondary Structure, Sequence Analysis, Surface Plasmon Resonance, Surface Property,
Affiliations Affiliazioni:
*** IBB - CNR ***
CIRPeB, University of Naples Federico II, Naples, Italy
Department of Pharmacy, University of Naples Federico II, via Mezzocannone 16, 80134 Naples, Italy
Institute of Biostructures and Bioimaging-CNR, via Mezzocannone 16, 80134 Naples, Italy
Department of Chemical Sciences, University of Naples Federico II, via Cintia 45, 80126 Naples, Italy
References Riferimenti:
Morandi, M., Sali, M., Manganelli, R., Delogu, G., (2013) J Infect Dev Ctries, 7, pp. 169-18
Ruggiero, A., Marchant, J., Squeglia, F., Makarov, V., De Simone, A., Berisio, R., (2013) J Biomol Struct Dyn, 31, pp. 195-205
Ruggiero, A., De Simone, P., Smaldone, G., Squeglia, F., Berisio, R., (2012) Curr Protein Pept Sci, 13, pp. 756-766
Ruggiero, A., Marasco, D., Squeglia, F., Soldini, S., Pedone, E., Pedone, C., Berisio, R., (2010) Structure, 18, pp. 1184-1190
Ruggiero, A., Tizzano, B., Pedone, E., Pedone, C., Wilmanns, M., Berisio, R., (2009) J Mol Biol, 385, pp. 153-162
Correale, S., Ruggiero, A., Capparelli, R., Pedone, E., Berisio, R., (2013) Acta Crystallogr D Biol Crystallogr, 69, pp. 1697-1706
Sauvage, E., Kerff, F., Terrak, M., Ayala, J. A., Charlier, P., (2008) FEMS Microbiol Rev, 32, pp. 234-258
Mukamolova, G. V., Turapov, O. A., Young, D. I., Kaprelyants, A. S., Kell, D. B., Young, M., (2002) Mol Microbiol, 46, pp. 623-635
Van Gunsteren, W. F., Berendsen, H. J., Hermans, J., Hol, W. G., Postma, J. P., (1983) Proc Natl Acad Sci USA, 80, pp. 4315-4319
Chao, M. C., Kieser, K. J., Minami, S., Mavrici, D., Aldridge, B. B., Fortune, S. M., Alber, T., Rubin, E., (2013) J. PLOS Pathogens, 9, pp. e1003197
Chao, M. C., Rubin, E., (2010) J. Annu Rev Microbiol, 64, pp. 293-311
Sung, M. T., Lai, Y. T., Huang, C. Y., Chou, L. Y., Shih, H. W., Cheng, W. C., Wong, C. H., Ma, C., (2009) Proc Natl Acad Sci USA, 106, pp. 8824-8829
Dessen, A., Mouz, N., Gordon, E., Hopkins, J., Dideberg, O., (2001) J Biol Chem, 276, pp. 45106-45112
Yeats, C., Finn, R. D., Bateman, A., (2002) Trends Biochem Sci, 27, p. 438
Shah, I. M., Laaberki, M. H., Popham, D. L., Dworkin, (2008) J. Cell, 135, pp. 486-496
Squeglia, F., Marchetti, R., Ruggiero, A., Lanzetta, R., Marasco, D., Dworkin, J., Petoukhov, M., Silipo, A., (2011) J Am Chem Soc, 133, pp. 20676-20679
Mir, M., Asong, J., Li, X., Cardot, J., Boons, G. J., Husson, R. N., (2011) PLOS Pathogens, 7, pp. e1002182
Maestro, B., Novakova, L., Hesek, D., Lee, M., Leyva, E., Mobashery, S., Sanz, J. M., Branny, P., (2011) FEBS Lett, 585, pp. 357-363
Vandal, O. H., Pierini, L. M., Schnappinger, D., Nathan, C. F., Ehrt, S., (2008) Nat Med, 14, pp. 849-854
Patru, M. M., Pavelka, Jr. M. S., (2010) J Bacteriol, 192, pp. 3043-3054
Ruggiero, A., Squeglia, F., Marasco, D., Marchetti, R., Molinaro, A., Berisio, R., (2011) Biochem J, 435, pp. 33-41
Gordon, E., Mouz, N., Duee, E., Dideberg, O., (2000) J Mol Biol, 299, pp. 477-485
Hildebrand, A., Remmert, M., Biegert, A., Soding, (2009) J. Proteins, 77 (SUPPL. 9), pp. 128-132
Mathur, A., Shankaracharya, Vidyarthi, A. S., (2012) J Mol Model, 18, pp. 3021-3023
Cheng, T. J., Sung, M. T., Liao, H. Y., Chang, Y. F., Chen, C. W., Huang, C. Y., Chou, L. Y., Cheng, W. C., (2008) Proc Natl Acad Sci USA, 105, pp. 431-436
Hett, E. C., Chao, M. C., Steyn, A. J., Fortune, S. M., Deng, L. L., Rubin, E., (2007) J. Mol Microbiol, 66, pp. 658-668
Rodriguez, R., Chinea, G., Lopez, N., Pons, T., Vriend, G., (1998) Bioinformatics, 14, pp. 523-528
Koradi, R., Billeter, M., Wuthrich, K., (1996) J Mol Graph, 14, pp. 51-55. , 29-32
Poletto, M., Vascotto, C., Scognamiglio, P. L., Lirussi, L., Marasco, D., Tell, G., (2013) Biochem J, 452, pp. 545-557
Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis
PonA2 is one of the two class A penicillin binding proteins of Mycobacterium tuberculosis, the etiologic agent of tuberculosis. It plays a complex role in mycobacterial physiology and is spotted as a promising target for inhibitors. PonA2 is involved in adaptation of M. tuberculosis to dormancy, an ability which has been attributed to the presence in its sequence of a C-terminal PASTA domain. Since PASTA modules are typically considered as beta-lactam antibiotic binding domains, we determined the solution structure of the PASTA domain from PonA2 and analyzed its binding properties versus a plethora of potential binders, including the beta-lactam antibiotics, two typical muropeptide mimics, and polymeric peptidoglycan. We show that, despite a high structural similarity with other PASTA domains, the PASTA domain of PonA2 displays different binding properties, as it is not able to bind muropeptides, or beta-lactams, or polymeric peptidoglycan. These results indicate that the role of PASTA domains cannot be generalized, as their specific binding properties strongly depend on surface residues, which are widely variable. (c) 2013 Wiley Periodicals, Inc. Biopolymers 101: 712-719, 2014.
PonA2 is one of the two class A penicillin binding proteins of Mycobacterium tuberculosis, the etiologic agent of tuberculosis. It plays a complex role in mycobacterial physiology and is spotted as a promising target for inhibitors. PonA2 is involved in adaptation of M. tuberculosis to dormancy, an ability which has been attributed to the presence in its sequence of a C-terminal PASTA domain. Since PASTA modules are typically considered as beta-lactam antibiotic binding domains, we determined the solution structure of the PASTA domain from PonA2 and analyzed its binding properties versus a plethora of potential binders, including the beta-lactam antibiotics, two typical muropeptide mimics, and polymeric peptidoglycan. We show that, despite a high structural similarity with other PASTA domains, the PASTA domain of PonA2 displays different binding properties, as it is not able to bind muropeptides, or beta-lactams, or polymeric peptidoglycan. These results indicate that the role of PASTA domains cannot be generalized, as their specific binding properties strongly depend on surface residues, which are widely variable. (c) 2013 Wiley Periodicals, Inc. Biopolymers 101: 712-719, 2014.
Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis
Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis
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Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2013 Sep; 69(Pt9): 1697-1706.
Impact Factor: 7.232
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Squeglia F, Romano M, Ruggiero A, Vitagliano L, De Simone A, Berisio R
* Carbohydrate recognition by RpfB from mycobacterium tuberculosis unveiled by crystallographic and molecular dynamics analyses (387 visite)
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Impact Factor: 3.832
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Falciani C, Brunetti J, Lelli B, Accardo A, Tesauro D, Morelli G, Bracci L
* Nanoparticles exposing neurotensin tumor-specific drivers (399 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2013 Apr; 19(4): 198-204.
Impact Factor: 1.862
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Accardo A, Mangiapia G, Paduano L, Morelli G, Tesauro D
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Impact Factor: 1.862
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Correale S, Ruggiero A, Pedone E, Berisio R
* Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the l, d-transpeptidase LdtMt1 from Mycobacterium tuberculosis (342 visite)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2013 Mar 1; 69(3): 253-256.
Impact Factor: 0.568
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Ruggiero A, Marchant J, Squeglia F, Makarov V, De Simone A, Berisio R
* Molecular determinants of inactivation of the resuscitation promoting factor B from Mycobacterium tuberculosis (364 visite)
J Biomol Struct Dyn (ISSN: 0739-1102, 1538-0254electronic, 0739-1102linking), 2013 Feb 1; 31(2): 195-205.
Impact Factor: 2.983
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Coppola D, Abbruzzetti S, Nicoletti F, Merlino A, Gambacurta A, Giordano D, Howes BD, De Sanctis G, Vitagliano L, Bruno S, di Prisco G, Mazzarella L, Smulevich G, Coletta M, Viappiani C, Vergara A, Verde C
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Impact Factor: 3.35
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Impact Factor: 3.914
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Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2012 Oct; 19(10): 1026-1034.
Impact Factor: 1.994
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Ziaco B, Diana D, Capasso D, Palumbo R, Celentano V, Di Stasi R, Fattorusso R, D'Andrea LD
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Biochem Biophys Res Commun (ISSN: 0006-291x), 2012 Jul 27; 424(2): 290-294.
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Castellano I, Merlino A
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Cell Mol Life Sci (ISSN: 1420-682x), 2012; 69(20): 3381-3394.
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Impact Factor: 2.484
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Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2011 Jan 1; 67(1): 164-168.
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Impact Factor: 2.561
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Torres Martin De Rosales R, Faiella M, Farquhar E, Que L, J , Andreozzi C, Pavone V, Maglio O, Nastri F, Lombardi A
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J Biol Inorg Chem (ISSN: 1432-1327electronic, 0949-8257linking, 0949-8257print), 2010 Jun; 15(5): 717-728.
Impact Factor: 3.287
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Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2010 Jan; 17(1): 70-73.
Impact Factor: 1.849
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Sandomenico A, Monti SM, Marasco D, Dathan N, Palumbo R, Saviano M, Ruvo M
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Mol Immunol (ISSN: 0161-5890), 2009 Oct; 46(16): 3300-3309.
Impact Factor: 3.202
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Ruggiero A, Tizzano B, Pedone E, Pedone C, Wilmanns M, Berisio R
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J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009 Jan 9; 385(1): 153-162.
Impact Factor: 3.871
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J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2008 Jul; 190(13): 4749-4753.
Impact Factor: 3.636
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Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2007 Oct 1; 63(10): 870-873.
Impact Factor: 0.645
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Febs Journal (ISSN: 1742-464x), 2007 Sep; 274(16): 4199-4210.
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* Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism (286 visite)
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Cimino P, Improta R, Bifulco G, Riccio R, Gomez-paloma L, Barone V
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Yonath A, Bashan A, Zarivach R, Franceschi F, Schluenzen F, Harms J, Albrecht R, Berisio R
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International Publication Number, 2003; N/D: N/D-N/D.
Impact Factor: 4.622
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Ciarmiello A, Del Vecchio S, Silvestro P, Potena MI, Carriero MV, Thomas R, Botti G, D'Aiuto G, Salvatore M
Tumor clearance of technetium 99m-sestamibi as a predictor of response to neoadjuvant chemotherapy for locally advanced breast cancer (385 visite)
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Impact Factor: 8.228
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62 Records (61 escludendo Abstract e Conferenze).
Impact factor totale: 233.42 (231.558 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 226.382 (224.667 escludendo Abstract e Conferenze).
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De Maio F, Salustri A, Battah B, Palucci I, Marchionni F, Bellesi S, Palmieri V, Papi M, Kramarska E, Sanguinetti M, Sali M, Berisio R, Delogu G
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Impact Factor: 2.385
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Impact Factor: 1.862
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Impact Factor: 7.232
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Squeglia F, Romano M, Ruggiero A, Vitagliano L, De Simone A, Berisio R
* Carbohydrate recognition by RpfB from mycobacterium tuberculosis unveiled by crystallographic and molecular dynamics analyses (387 visite)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2013 Jun 4; 104(11): 2530-2539.
Impact Factor: 3.832
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Falciani C, Brunetti J, Lelli B, Accardo A, Tesauro D, Morelli G, Bracci L
* Nanoparticles exposing neurotensin tumor-specific drivers (399 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2013 Apr; 19(4): 198-204.
Impact Factor: 1.862
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Accardo A, Mangiapia G, Paduano L, Morelli G, Tesauro D
* Octreotide labeled aggregates containing platinum complexes as nanovectors for drug delivery (362 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2013 Apr; 19(4): 190-197.
Impact Factor: 1.862
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Correale S, Ruggiero A, Pedone E, Berisio R
* Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the l, d-transpeptidase LdtMt1 from Mycobacterium tuberculosis (342 visite)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2013 Mar 1; 69(3): 253-256.
Impact Factor: 0.568
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Ruggiero A, Marchant J, Squeglia F, Makarov V, De Simone A, Berisio R
* Molecular determinants of inactivation of the resuscitation promoting factor B from Mycobacterium tuberculosis (364 visite)
J Biomol Struct Dyn (ISSN: 0739-1102, 1538-0254electronic, 0739-1102linking), 2013 Feb 1; 31(2): 195-205.
Impact Factor: 2.983
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Coppola D, Abbruzzetti S, Nicoletti F, Merlino A, Gambacurta A, Giordano D, Howes BD, De Sanctis G, Vitagliano L, Bruno S, di Prisco G, Mazzarella L, Smulevich G, Coletta M, Viappiani C, Vergara A, Verde C
* ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus (306 visite)
Molecular Biosystems (ISSN: 1742-206x), 2012 Oct 30; 8(12): 3295-3304.
Impact Factor: 3.35
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Roviello GN, Roviello G, Musumeci D, Bucci EM, Pedone C
* Dakin-West reaction on 1-thyminyl acetic acid for the synthesis of 1, 3-bis(1-thyminyl)-2-propanone, a heteroaromatic compound with nucleopeptide-binding properties (393 visite)
Amino Acids (ISSN: 1438-2199, 0939-4451, 1438-2199electronic), 2012 Oct; 43(4): 1615-1623.
Impact Factor: 3.914
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Kaprelyants AS, Mukamolova GV, Ruggiero A, Makarov VA, Demina GR, Shleeva MO, Potapov VD, Shramko PA
* Resuscitation-promoting Factors (Rpf): In Search of Inhibitors (428 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2012 Oct; 19(10): 1026-1034.
Impact Factor: 1.994
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Ziaco B, Diana D, Capasso D, Palumbo R, Celentano V, Di Stasi R, Fattorusso R, D'Andrea LD
* C-terminal truncation of Vascular Endothelial Growth Factor mimetic helical peptide preserves structural and receptor binding properties (333 visite)
Biochem Biophys Res Commun (ISSN: 0006-291x), 2012 Jul 27; 424(2): 290-294.
Impact Factor: 2.406
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Esposito C, Cantisani M, D'Auria G, Falcigno L, Pedone E, Galdiero S, Berisio R
* Mapping key interactions in the dimerization process of HBHA from Mycobacterium tuberculosis, insights into bacterial agglutination (385 visite)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2012 Mar 23; 586(6): 659-667.
Impact Factor: 3.582
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Castellano I, Merlino A
* γ-glutamyltranspeptidases: Sequence, structure, biochemical properties, and biotechnological applications (381 visite)
Cell Mol Life Sci (ISSN: 1420-682x), 2012; 69(20): 3381-3394.
Impact Factor: 5.615
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Esposito C, Marasco D, Delogu G, Pedone E, Berisio R
* Heparin-binding hemagglutinin HBHA from Mycobacterium tuberculosis affects actin polymerisation (323 visite)
Biochem Biophys Res Commun (ISSN: 0006-291x), 2011 Jul 1; 410(2): 339-344.
Impact Factor: 2.484
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Ruggiero A, Squeglia F, Pirone L, Correale S, Berisio R
* Expression, purification, crystallization and preliminary X-ray crystallographic analysis of a major fragment of the resuscitation-promoting factor RpfB from Mycobacterium tuberculosis (361 visite)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2011 Jan 1; 67(1): 164-168.
Impact Factor: 0.506
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D'Auria G, Esposito C, Falcigno L, Calvanese L, Iaccarino E, Ruggiero A, Pedone C, Pedone E, Berisio R
* Dynamical properties of cold shock protein A from Mycobacterium tuberculosis (285 visite)
Biochem Biophys Res Commun (ISSN: 0006-291x, 1090-2104, 1090-2104electronic), 2010 Nov 26; 402(4): 693-698.
Impact Factor: 2.595
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Ruggiero A, Marasco D, Squeglia F, Soldini S, Pedone E, Pedone C, Berisio R
* Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation (361 visite)
Structure (ISSN: 0969-2126, 1878-4186, 0969-2126linking), 2010 Sep 8; 18(9): 1184-1190.
Impact Factor: 6.337
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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 (435 visite)
Chem Biol Drug Des (ISSN: 1747-0277, 1747-0285), 2010 Jul; 76(1): 10-16.
Impact Factor: 2.527
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Berisio R, Ruggiero A, Vitagliano L
* Elongation Factors Efia And Ef-Tu: Their Role In Translation And Beyond (506 visite)
Israel Journal Of Chemistry, 2010 Jun; 50(1): 71-79.
Impact Factor: 2.561
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Torres Martin De Rosales R, Faiella M, Farquhar E, Que L, J , Andreozzi C, Pavone V, Maglio O, Nastri F, Lombardi A
* Spectroscopic and metal-binding properties of DF3: an artificial protein able to accommodate different metal ions (287 visite)
J Biol Inorg Chem (ISSN: 1432-1327electronic, 0949-8257linking, 0949-8257print), 2010 Jun; 15(5): 717-728.
Impact Factor: 3.287
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Esposito C, Carullo C, Pedone E, Graziano G, Del Vecchio P, Berisio R
* Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: Implications for bacterial agglutination (480 visite)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 0014-5793linking), 2010 Mar 19; 584(6): 1091-1096.
Impact Factor: 3.601
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Ruggiero A, Squeglia F, Esposito C, Marasco D, Pedone E, Pedone C, Berisio R
* Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the resuscitation promoting factor interacting protein RipA from M. tuberculosis (323 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2010 Jan; 17(1): 70-73.
Impact Factor: 1.849
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Sandomenico A, Monti SM, Marasco D, Dathan N, Palumbo R, Saviano M, Ruvo M
* Ige-Binding Properties And Selectivity Of Peptide Mimics Of The Fcvarepsilonri Binding Site (1608 visite)
Mol Immunol (ISSN: 0161-5890), 2009 Oct; 46(16): 3300-3309.
Impact Factor: 3.202
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Giordano D, Boechi L, Vergara A, Marti MA, Samuni U, Dantsker D, Grassi L, Estrin DA, Friedman JM, Mazzarella L, Di Prisco G, Verde C
* The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - oxygen-binding equilibria, kinetics and molecular dynamics (657 visite)
Febs Journal (ISSN: 1742-464x), 2009 Apr; 276(8): 2266-2277.
Impact Factor: 3.042
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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 (366 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 122-130.
Impact Factor: 1.807
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Ruggiero A, Tizzano B, Pedone E, Pedone C, Wilmanns M, Berisio R
* Crystal Structure of the Resuscitation-Promoting Factor (Delta DUF)RpfB from M. tuberculosis (477 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009 Jan 9; 385(1): 153-162.
Impact Factor: 3.871
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Esposito C, Pethoukov MV, Svergun DI, Ruggiero A, Pedone C, Pedone E, Berisio R
* Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis (387 visite)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2008 Jul; 190(13): 4749-4753.
Impact Factor: 3.636
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Ruggiero A, Tizzano B, Geerlof A, Pedone E, Pedone C, Wilmanns M, Berisio R
* Expression, purification, crystallization and preliminary X-ray crystallographic analysis of a resuscitation-promoting factor from Mycobacterium tuberculosis (354 visite)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2007 Oct 1; 63(10): 870-873.
Impact Factor: 0.645
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Pastore C, Franzese M, Sica F, Temussi P, Pastore A
* Understanding the binding properties of an unusual metal-binding protein - a study of bacterial frataxin (309 visite)
Febs Journal (ISSN: 1742-464x), 2007 Sep; 274(16): 4199-4210.
Impact Factor: 3.396
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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 (286 visite)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2004 Jun 1; 567(1): 20-26.
Impact Factor: 3.843
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Cimino P, Improta R, Bifulco G, Riccio R, Gomez-paloma L, Barone V
* Nucleophilic Cyclopropane Ring Opening in Duocarmycin SA Derivatives by Methanol under Acid Conditions: A Quantum Mechanical Study in the Gas-Phase and in Solution (395 visite)
J Org Chem (ISSN: 0022-3263, 0022-3263linking), 2004; 69(8): 2816-2824.
Impact Factor: 3.462
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Yonath A, Bashan A, Zarivach R, Franceschi F, Schluenzen F, Harms J, Albrecht R, Berisio R
* Methods Of Growing Crystals Of Free, Antibiotic-Complexed, And Substrate-Complexed Large Ribosomal Subunits, And Methods Of Rational Designing Or Identifying Antibiotics Using Structure Coordinate Data Derived From Such Crystals (260 visite)
International Publication Number, 2003; N/D: N/D-N/D.
Impact Factor: 4.622
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Oliva R, Falcigno L, D'Auria G, Zanotti G, Paolillo L
Conformation and calcium-binding properties of a bicyclic nonapeptide (330 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2000; 56(1): 27-36.
Impact Factor: 2.405
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Ciarmiello A, Del Vecchio S, Silvestro P, Potena MI, Carriero MV, Thomas R, Botti G, D'Aiuto G, Salvatore M
Tumor clearance of technetium 99m-sestamibi as a predictor of response to neoadjuvant chemotherapy for locally advanced breast cancer (385 visite)
Journal Of Clinical Oncology (ISSN: 0732-183x), 1998 May; 16(5): 1677-1683.
Impact Factor: 8.228
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62 Records (61 escludendo Abstract e Conferenze).
Impact factor totale: 233.42 (231.558 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 226.382 (224.667 escludendo Abstract e Conferenze).
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