Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies (311 views visite)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2015 Feb 8; 1854(5): 402-409.
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Paper type Tipo di articolo: Journal Article,
Impact factor: 5.158, 5-year impact factor Impact factor a 5 anni: 5.36
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84922879126&partnerID=40&md5=3b16a75c01c8312fc41657ae53bb19d0
Keywords Parole chiave: Dsc, Eukaryotic-Type Serine Threonine Kinases, Thermal Unfolding Of Multi-Domain Proteins, Bacillus Subtilis, Posibacteria, Staphylococcus Aureus, Bacterial Enzyme, Protein Serine Threonine Kinase, Article, Calorimetry, Circular Dichroism, Differential Scanning Calorimetry, Enzyme Analysis, Extracellular Space, Melting Point, Nonhuman, Priority Journal, Protein Folding, Protein Unfolding, Thermodynamics, Protein Kinase C, Amino Acid Sequence, Chemistry, Enzymology, Models, Molecular, Molecular Sequence Data, Protein Stability, Protein Structure, Tertiary, Sequence Homology,
Affiliations Affiliazioni:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, CNR, via Mezzocannone 16Napoli, Italy
Department of Chemical Sciences, University of Naples Federico II, via CintiaNapoli, Italy
Consiglio Nazionale delle Ricerche
Universita degli Studi di Napoli Federico II
References Riferimenti:
Madec, E., Laszkiewicz, A., Iwanicki, A., Obuchowski, M., Seror, S., Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes (2002) Mol. Microbiol., 46, pp. 571-58
Fiuza, M., Canova, M.J., Zanella-Cleon, I., Becchi, M., Cozzone, A.J., Mateos, L.M., Kremer, L., Molle, V., From the characterization of the four serine/threonine protein kinases (PknA/B/G/L) of Corynebacterium glutamicum toward the role of PknA and PknB in cell division (2008) J. Biol. Chem., 283, pp. 18099-18112
Madec, E., Stensballe, A., Kjellstrom, S., Cladiere, L., Obuchowski, M., Jensen, O.N., Seror, S.J., Mass spectrometry and site-directed mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis (2003) J. Mol. Biol., 330, pp. 459-472
Absalon, C., Obuchowski, M., Madec, E., Delattre, D., Holland, I.B., Seror, S.J., CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis (2009) Microbiology, 155, pp. 932-943
Ruggiero, A., De Simone, P., Smaldone, G., Squeglia, F., Berisio, R., Bacterial cell division regulation by Ser/Thr kinases: A structural perspective (2012) Curr. Protein Pept. Sci., 13, pp. 756-766
Molle, V., Kremer, L., Division and cell envelope regulation by Ser/Thr phosphorylation: Mycobacterium shows the way (2010) Mol. Microbiol., 75, pp. 1064-1077
Beltramini, A.M., Mukhopadhyay, C.D., Pancholi, V., Modulation of cell wall structure and antimicrobial susceptibility by a Staphylococcus aureus eukaryote-like serine/ threonine kinase and phosphatase (2009) Infect. Immun., 77, pp. 1406-1416
Hempel, A.M., Cantlay, S., Molle, V., Wang, S.B., Naldrett, M.J., Parker, J.L., Richards, D.M., Flardh, K., The Ser/Thr protein kinase AfsK regulates polar growth and hyphal branching in the filamentous bacteria Streptomyces (2012) Proc. Natl. Acad. Sci. U. S. A., 109, pp. E2371-E2379
Shah, I.M., Laaberki, M.H., Popham, D.L., Dworkin, J., A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments (2008) Cell, 135, pp. 486-496
Shah, I.M., Dworkin, J., Induction and regulation of a secreted peptidoglycan hydrolase by a membrane Ser/Thr kinase that detects muropeptides (2010) Mol. Microbiol., 75 (5), pp. 1232-1243
Kana, B.D., Mizrahi, V., Resuscitation-promoting factors as lytic enzymes for bacterial growth and signaling (2010) FEMS Immunol. Med. Microbiol., 58, pp. 39-50
Warner, D.F., Mizrahi, V., The survival kit of Mycobacterium tuberculosis (2007) Nat. Med., 13, pp. 282-284
Keep, N.H., Ward, J.M., Cohen-Gonsaud, M., Henderson, B., Wake up! Peptidoglycan lysis and bacterial non-growth states (2006) Trends Microbiol., 14, pp. 271-276
Hett, E.C., Rubin, E.J., Bacterial growth and cell division: A mycobacterial perspective (2008) Microbiol. Mol. Biol. Rev., 72, pp. 126-156
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 (2010) Structure, 18, pp. 1184-1190
Squeglia, F., Marchetti, R., Ruggiero, A., Lanzetta, R., Marasco, D., Dworkin, J., Petoukhov, M., Silipo, A., Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy (2011) J. Am. Chem. Soc., 133, pp. 20676-20679
McGahee, W., Lowy, F.D., Staphylococcal infections in the intensive care unit (2000) Semin. Respir. Infect., 15, pp. 308-313
Ohlsen, K., Donat, S., The impact of serine/threonine phosphorylation in Staphylococcus aureus (2010) Int. J. Med. Microbiol., 300, pp. 137-141
Cotter, P.D., Hill, C., Surviving the acid test: Responses of gram-positive bacteria to low pH (2003) Microbiol. Mol. Biol. Rev., 67, pp. 429-453. , table of contents
Magill, N.G., Cowan, A.E., Koppel, D.E., Setlow, P., The internal pH of the forespore compartment of Bacillus megaterium decreases by about 1 pH unit during sporulation (1994) J. Bacteriol., 176, pp. 2252-2258
Yeats, C., Finn, R.D., Bateman, A., The PASTA domain: A beta-lactam-binding domain (2002) Trends Biochem. Sci., 27, p. 438
Ruggiero, A., Squeglia, F., Marasco, D., Marchetti, R., Molinaro, A., Berisio, R., X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus (2011) Biochem. J., 435, pp. 33-41
Privalov, P.L., Stability of proteins. Proteinswhich do not present a single cooperative system (1982) Adv. Protein Chem., 35, pp. 1-104
Gill, S.C., Von Hippel, P.H., Calculation of protein extinction coefficients from amino acid sequence data (1989) Anal. Biochem., 182, pp. 319-326
Eswar, N., Eramian, D., Webb, B., Shen, M.Y., Sali, A., Protein structure modeling with MODELLER (2008) Methods Mol. Biol., 426, pp. 145-159
Pronk, S., Pall, S., Schulz, R., Larsson, P., Bjelkmar, P., Apostolov, R., Shirts, M.R., Lindahl, E., GROMACS 4.5: A high-throughput and highly parallel open source molecular simulation toolkit (2013) Bioinformatics, 29, pp. 845-854
Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK: A programto check the stereochemical quality of protein structures (1993) J. Appl. Crystallogr., 26, pp. 283-291
Johnson, C.M., Differential scanning calorimetry as a tool for protein folding and stability (2013) Arch. Biochem. Biophys., 531, pp. 100-109
Privalov, P.L., Microcalorimetry of proteins and their complexes (2009) Methods Mol. Biol., 490, pp. 1-39
Apic, G., Gough, J., Teichmann, S.A., Domain combinations in archaeal, eubacterial and eukaryotic proteomes (2001) J. Mol. Biol., 310, pp. 311-325
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2015 Feb 8; 1854(5): 402-409.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 5.158, 5-year impact factor Impact factor a 5 anni: 5.36
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84922879126&partnerID=40&md5=3b16a75c01c8312fc41657ae53bb19d0
Keywords Parole chiave: Dsc, Eukaryotic-Type Serine Threonine Kinases, Thermal Unfolding Of Multi-Domain Proteins, Bacillus Subtilis, Posibacteria, Staphylococcus Aureus, Bacterial Enzyme, Protein Serine Threonine Kinase, Article, Calorimetry, Circular Dichroism, Differential Scanning Calorimetry, Enzyme Analysis, Extracellular Space, Melting Point, Nonhuman, Priority Journal, Protein Folding, Protein Unfolding, Thermodynamics, Protein Kinase C, Amino Acid Sequence, Chemistry, Enzymology, Models, Molecular, Molecular Sequence Data, Protein Stability, Protein Structure, Tertiary, Sequence Homology,
Affiliations Affiliazioni:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, CNR, via Mezzocannone 16Napoli, Italy
Department of Chemical Sciences, University of Naples Federico II, via CintiaNapoli, Italy
Consiglio Nazionale delle Ricerche
Universita degli Studi di Napoli Federico II
References Riferimenti:
Madec, E., Laszkiewicz, A., Iwanicki, A., Obuchowski, M., Seror, S., Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes (2002) Mol. Microbiol., 46, pp. 571-58
Fiuza, M., Canova, M.J., Zanella-Cleon, I., Becchi, M., Cozzone, A.J., Mateos, L.M., Kremer, L., Molle, V., From the characterization of the four serine/threonine protein kinases (PknA/B/G/L) of Corynebacterium glutamicum toward the role of PknA and PknB in cell division (2008) J. Biol. Chem., 283, pp. 18099-18112
Madec, E., Stensballe, A., Kjellstrom, S., Cladiere, L., Obuchowski, M., Jensen, O.N., Seror, S.J., Mass spectrometry and site-directed mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis (2003) J. Mol. Biol., 330, pp. 459-472
Absalon, C., Obuchowski, M., Madec, E., Delattre, D., Holland, I.B., Seror, S.J., CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis (2009) Microbiology, 155, pp. 932-943
Ruggiero, A., De Simone, P., Smaldone, G., Squeglia, F., Berisio, R., Bacterial cell division regulation by Ser/Thr kinases: A structural perspective (2012) Curr. Protein Pept. Sci., 13, pp. 756-766
Molle, V., Kremer, L., Division and cell envelope regulation by Ser/Thr phosphorylation: Mycobacterium shows the way (2010) Mol. Microbiol., 75, pp. 1064-1077
Beltramini, A.M., Mukhopadhyay, C.D., Pancholi, V., Modulation of cell wall structure and antimicrobial susceptibility by a Staphylococcus aureus eukaryote-like serine/ threonine kinase and phosphatase (2009) Infect. Immun., 77, pp. 1406-1416
Hempel, A.M., Cantlay, S., Molle, V., Wang, S.B., Naldrett, M.J., Parker, J.L., Richards, D.M., Flardh, K., The Ser/Thr protein kinase AfsK regulates polar growth and hyphal branching in the filamentous bacteria Streptomyces (2012) Proc. Natl. Acad. Sci. U. S. A., 109, pp. E2371-E2379
Shah, I.M., Laaberki, M.H., Popham, D.L., Dworkin, J., A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments (2008) Cell, 135, pp. 486-496
Shah, I.M., Dworkin, J., Induction and regulation of a secreted peptidoglycan hydrolase by a membrane Ser/Thr kinase that detects muropeptides (2010) Mol. Microbiol., 75 (5), pp. 1232-1243
Kana, B.D., Mizrahi, V., Resuscitation-promoting factors as lytic enzymes for bacterial growth and signaling (2010) FEMS Immunol. Med. Microbiol., 58, pp. 39-50
Warner, D.F., Mizrahi, V., The survival kit of Mycobacterium tuberculosis (2007) Nat. Med., 13, pp. 282-284
Keep, N.H., Ward, J.M., Cohen-Gonsaud, M., Henderson, B., Wake up! Peptidoglycan lysis and bacterial non-growth states (2006) Trends Microbiol., 14, pp. 271-276
Hett, E.C., Rubin, E.J., Bacterial growth and cell division: A mycobacterial perspective (2008) Microbiol. Mol. Biol. Rev., 72, pp. 126-156
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 (2010) Structure, 18, pp. 1184-1190
Squeglia, F., Marchetti, R., Ruggiero, A., Lanzetta, R., Marasco, D., Dworkin, J., Petoukhov, M., Silipo, A., Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy (2011) J. Am. Chem. Soc., 133, pp. 20676-20679
McGahee, W., Lowy, F.D., Staphylococcal infections in the intensive care unit (2000) Semin. Respir. Infect., 15, pp. 308-313
Ohlsen, K., Donat, S., The impact of serine/threonine phosphorylation in Staphylococcus aureus (2010) Int. J. Med. Microbiol., 300, pp. 137-141
Cotter, P.D., Hill, C., Surviving the acid test: Responses of gram-positive bacteria to low pH (2003) Microbiol. Mol. Biol. Rev., 67, pp. 429-453. , table of contents
Magill, N.G., Cowan, A.E., Koppel, D.E., Setlow, P., The internal pH of the forespore compartment of Bacillus megaterium decreases by about 1 pH unit during sporulation (1994) J. Bacteriol., 176, pp. 2252-2258
Yeats, C., Finn, R.D., Bateman, A., The PASTA domain: A beta-lactam-binding domain (2002) Trends Biochem. Sci., 27, p. 438
Ruggiero, A., Squeglia, F., Marasco, D., Marchetti, R., Molinaro, A., Berisio, R., X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus (2011) Biochem. J., 435, pp. 33-41
Privalov, P.L., Stability of proteins. Proteinswhich do not present a single cooperative system (1982) Adv. Protein Chem., 35, pp. 1-104
Gill, S.C., Von Hippel, P.H., Calculation of protein extinction coefficients from amino acid sequence data (1989) Anal. Biochem., 182, pp. 319-326
Eswar, N., Eramian, D., Webb, B., Shen, M.Y., Sali, A., Protein structure modeling with MODELLER (2008) Methods Mol. Biol., 426, pp. 145-159
Pronk, S., Pall, S., Schulz, R., Larsson, P., Bjelkmar, P., Apostolov, R., Shirts, M.R., Lindahl, E., GROMACS 4.5: A high-throughput and highly parallel open source molecular simulation toolkit (2013) Bioinformatics, 29, pp. 845-854
Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK: A programto check the stereochemical quality of protein structures (1993) J. Appl. Crystallogr., 26, pp. 283-291
Johnson, C.M., Differential scanning calorimetry as a tool for protein folding and stability (2013) Arch. Biochem. Biophys., 531, pp. 100-109
Privalov, P.L., Microcalorimetry of proteins and their complexes (2009) Methods Mol. Biol., 490, pp. 1-39
Apic, G., Gough, J., Teichmann, S.A., Domain combinations in archaeal, eubacterial and eukaryotic proteomes (2001) J. Mol. Biol., 310, pp. 311-325
Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies
Eukaryotic-type Ser/Thr protein-kinases are critical mediators of developmental changes and host pathogen interactions in bacteria. Although with lower abundance compared to their homologues from eukaryotes, Ser/Thr protein-kinases (STPK) are widespread in gram positive bacteria, where they regulate several cellular functions. STPKs belong to the protein kinase family named as one-component signal transduction systems,which combine both sensing and regulating properties. Thermodynamic investigations of sensing extra-cellular portions of two important Ser-Thr kinases, PrkC, from Staphylococcus aureus and Bacillus subtilis were conducted by differential scanning calorimetry (DSC) and circular dichroism(CD) melting measurements, coupled with modelling studies. The study of thermodynamic properties of the two domains is challenging since they share a modular domain organization. Consistently, DSC and CD data show that they present similar thermodynamic behaviours and that folding/unfolding transitions do not fit a two-state folding model. However, the thermal unfolding of the two proteins is differentially sensitive to pH. In particular, their unfolding is characteristic of modular structures at the neutral pH, with independent contributions of individual domains to folding. Differently, a cooperative unfolding is evidenced at acidic pH for the B. subtilis member, suggesting that a significant interaction between domains becomes valuable. © 2015 Elsevier B.V. All rights reserved.
Eukaryotic-type Ser/Thr protein-kinases are critical mediators of developmental changes and host pathogen interactions in bacteria. Although with lower abundance compared to their homologues from eukaryotes, Ser/Thr protein-kinases (STPK) are widespread in gram positive bacteria, where they regulate several cellular functions. STPKs belong to the protein kinase family named as one-component signal transduction systems,which combine both sensing and regulating properties. Thermodynamic investigations of sensing extra-cellular portions of two important Ser-Thr kinases, PrkC, from Staphylococcus aureus and Bacillus subtilis were conducted by differential scanning calorimetry (DSC) and circular dichroism(CD) melting measurements, coupled with modelling studies. The study of thermodynamic properties of the two domains is challenging since they share a modular domain organization. Consistently, DSC and CD data show that they present similar thermodynamic behaviours and that folding/unfolding transitions do not fit a two-state folding model. However, the thermal unfolding of the two proteins is differentially sensitive to pH. In particular, their unfolding is characteristic of modular structures at the neutral pH, with independent contributions of individual domains to folding. Differently, a cooperative unfolding is evidenced at acidic pH for the B. subtilis member, suggesting that a significant interaction between domains becomes valuable. © 2015 Elsevier B.V. All rights reserved.
Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies
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Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies
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Curr Protein Pept Sci (ISSN: 1389-2037), 2007 Feb; 8(1): 63-82.
Impact Factor: 3.259
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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 (302 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2004 Jun; 13(6): 1503-1511.
Impact Factor: 4.116
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Digilio Filomena A, Morra R, Pedone E, Bartolucci S, Rossi M
* High-level expression of Aliciclobacillus acidocaldarius thioredoxin in Pichia pastoris and Bacillus subtilis (201 visite)
Protein Expr Purif (ISSN: 1046-5928), 2003 Sep; 30(2): 179-184.
Impact Factor: 1.47
Dettagli Esporta in BibTeX Esporta in 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 (398 visite)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2003 Jul; 185(14): 4276-4279.
Impact Factor: 4.175
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De Simone G, Menchise V, Manco G, Mandrich L, Sorrentino N, Lang D, Rossi M, Pedone C
* The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus (339 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2001 Nov 30; 314(3): 507-518.
Impact Factor: 5.826
Dettagli Esporta in BibTeX Esporta in EndNote
De Simone G, Galdiero S, Manco G, Lang D, Rossi M, Pedone C
A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase (422 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2000 Nov 10; 303(5): 761-771.
Impact Factor: 5.388
Dettagli Esporta in BibTeX Esporta in EndNote
27 Records (25 escludendo Abstract e Conferenze).
Impact factor totale: 103.926 (97.799 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 98.412 (92.066 escludendo Abstract e Conferenze).
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Ronda L, Tonelli A, Sogne E, Autiero I, Spyrakis F, Pellegrino S, Abbiati G, Maffioli E, Schulte C, Piano R, Cozzini P, Mozzarelli A, Bettati S, Clerici F, Milani P, Lenardi C, Tedeschi G, Gelmi ML
* Rational Design of a User-Friendly Aptamer/Peptide-Based Device for the Detection of Staphylococcus aureus (59 visite)
Sensors (ISSN: 1424-8220linking), 2020 Sep 2; 20(17): N/D-N/D.
Impact Factor: 3.275
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Maglione M, Montella S, Mollica C, Carnovale V, Iacotucci P, De Gregorio F, Tosco A, Cervasio M, Raia V, Santamaria F
* Lung structure and function similarities between primary ciliary dyskinesia and mild cystic fibrosis: a pilot study (733 visite)
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Impact Factor: 1.776
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Berisio R
* Editorial: Molecular determinants of bacterial diseases (322 visite)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2015; 22(14): 1640-1641.
Impact Factor: 3.455
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Calce E, Mignogna E, Bugatti V, Galdiero M, Vittoria V, De Luca S
* Pectin functionalized with natural fatty acids as antimicrobial agent (315 visite)
Int J Biol Macromol (ISSN: 0141-8130, 0141-8130linking, 1879-0003electronic), 2014 Jul; 68: 28-32.
Impact Factor: 2.858
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Graziano G, Merlino A
* Molecular bases of protein halotolerance (322 visite)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2014 Apr; 1844(4): 850-858.
Impact Factor: 4.882
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Lin L-L, Chen Y-Y, Chi M-C, Merlino A
* Low resolution X-ray structure of γ-glutamyltranspeptidase from Bacillus licheniformis: Opened active site cleft and a cluster of acid residues potentially involved in the recognition of a metal ion (306 visite)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2014; 1844(9): 1523-1529.
Impact Factor: 4.882
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Del Giudice I, Limauro D, Pedone E, Bartolucci S, Fiorentino G
* A novel arsenate reductase from the bacterium Thermus thermophilus HB27: Its role in arsenic detoxification (362 visite)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Oct; 1834(10): 2071-2079.
Impact Factor: 3.191
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Avitabile C, Netti F, Orefice G, Palmieri M, Nocerino N, Malgieri G, D'Andrea LD, Capparelli R, Fattorusso R, Romanelli A
* Design, structural and functional characterization of a Temporin-1b analog active against Gram-negative bacteria (395 visite)
Bba-Gen Subjects (ISSN: 0304-4165, 0006-3002, 0925-4439), 2013 Jun; 1830(6): 3767-3775.
Impact Factor: 3.829
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Simonetti O, Cirioni O, Ghiselli R, Goteri G, Orlando F, Monfregola L, De Luca S, Zizzi A, Silvestri C, Veglia G, Giacometti A, Guerrieri M, Offidani A, Scaloni A
* Antimicrobial properties of distinctin in an experimental model of MRSA-infected wounds (460 visite)
Eur J Clin Microbiol Infect Dis (ISSN: 0934-9723), 2012 Nov; 31(11): 3047-3055.
Impact Factor: 3.024
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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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Berisio R, Ciccarelli L, Squeglia F, De Simone A, Vitagliano L
* Structural and Dynamic properties of incomplete immunoglobulin-like fold domains (410 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2012 Oct; 19(10): 1045-1053.
Impact Factor: 1.994
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Squeglia F, Marchetti R, Ruggiero A, Lanzetta R, Marasco D, Dworkin J, Petoukhov M, Molinaro A, Berisio R, Silipo A
* Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy (348 visite)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2011 Dec 28; 133(51): 20676-20679.
Impact Factor: 9.907
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Romanelli A, Moggio L, Montella RC, Campiglia P, Iannaccone M, Capuano F, Pedone C, Capparelli R
* Peptides from Royal Jelly: studies on the antimicrobial activity of jelleins, jelleins analogs and synergy with temporins (1391 visite)
J Pept Sci (ISSN: 1099-1387, 1075-2617, 1075-2617print), 2011 Dec 2; 17(5): 348-352.
Impact Factor: 1.799
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Vitagliano L, Berisio R, De Simone A
* Role of hydration in collagen recognition by bacterial adhesins (536 visite)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2011 May 4; 100(9): 2253-2261.
Impact Factor: 3.653
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Contursi P, D'Ambrosio K, Pirone L, Pedone E, Aucelli T, She Q, De Simone G, Bartolucci S
* C68 from the Sulfolobus islandicus plasmid-virus pSSVx is a novel member of the AbrB-like transcription factor family (967 visite)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2011 Apr 1; 435(1): 157-166.
Impact Factor: 4.897
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Ruggiero A, Squeglia F, Marasco D, Marchetti R, Molinaro A, Berisio R
* X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus (383 visite)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2011 Apr 1; 435(1): 33-41.
Impact Factor: 4.897
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Verardi R, Traaseth NJ, Shi L, Porcelli F, Monfregola L, De Luca S, Amodeo P, Veglia G, Scaloni A
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Bba-Gen Subjects (ISSN: 0005-2736, 0006-3002, 0925-4439), 2011 Jan; 1808(1): 34-40.
Impact Factor: 3.99
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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, Squeglia F, Izzo V, Silipo A, Vitagliano L, Molinaro A, Berisio R
* Expression, purification, crystallization and preliminary x-ray crystallographic analysis of the peptidoglycan binding region of the ser/thr kinase PrkC from staphylococcus aureus (335 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2010 Oct; 17(10): 1296-1299.
Impact Factor: 1.849
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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 (408 visite)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2009 Sep 28; 4(9): e7191-e7191.
Impact Factor: 4.351
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Cirioni O, Ghiselli R, Orlando F, Silvestri C, De Luca S, Salzano AM, Mocchegiani F, Saba V, Scalise G, Scaloni A, Giacometti A
* Efficacy of the amphibian peptide distinctin in a neutropenic mouse model of staphylococcal sepsis (272 visite)
Critical Care Medicine (ISSN: 0090-3493), 2008 Sep; 36(9): 2629-2633.
Impact Factor: 6.594
Dettagli Esporta in BibTeX Esporta in EndNote
Galdiero S, Galdiero M, Pedone C
* Beta-Barrel Membrane Bacterial Proteins: Structure, Function, Assembly And Interaction With Lipids (374 visite)
Curr Protein Pept Sci (ISSN: 1389-2037), 2007 Feb; 8(1): 63-82.
Impact Factor: 3.259
Dettagli Esporta in BibTeX Esporta in EndNote
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 (302 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2004 Jun; 13(6): 1503-1511.
Impact Factor: 4.116
Dettagli Esporta in BibTeX Esporta in EndNote
Digilio Filomena A, Morra R, Pedone E, Bartolucci S, Rossi M
* High-level expression of Aliciclobacillus acidocaldarius thioredoxin in Pichia pastoris and Bacillus subtilis (201 visite)
Protein Expr Purif (ISSN: 1046-5928), 2003 Sep; 30(2): 179-184.
Impact Factor: 1.47
Dettagli Esporta in BibTeX Esporta in 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 (398 visite)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2003 Jul; 185(14): 4276-4279.
Impact Factor: 4.175
Dettagli Esporta in BibTeX Esporta in EndNote
De Simone G, Menchise V, Manco G, Mandrich L, Sorrentino N, Lang D, Rossi M, Pedone C
* The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus (339 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2001 Nov 30; 314(3): 507-518.
Impact Factor: 5.826
Dettagli Esporta in BibTeX Esporta in EndNote
De Simone G, Galdiero S, Manco G, Lang D, Rossi M, Pedone C
A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase (422 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2000 Nov 10; 303(5): 761-771.
Impact Factor: 5.388
Dettagli Esporta in BibTeX Esporta in EndNote
27 Records (25 escludendo Abstract e Conferenze).
Impact factor totale: 103.926 (97.799 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 98.412 (92.066 escludendo Abstract e Conferenze).
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