Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies (423 views)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2015 Feb 8; 1854(5): 402-409.
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Paper type: Journal Article,
Impact factor: 5.158, 5-year impact factor: 5.36
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84922879126&partnerID=40&md5=3b16a75c01c8312fc41657ae53bb19d0
Keywords: 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:
*** 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:
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 BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.158, 5-year impact factor: 5.36
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84922879126&partnerID=40&md5=3b16a75c01c8312fc41657ae53bb19d0
Keywords: 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:
*** 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:
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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* High-level expression of Aliciclobacillus acidocaldarius thioredoxin in Pichia pastoris and Bacillus subtilis (233 views)
Protein Expr Purif (ISSN: 1046-5928), 2003 Sep; 30(2): 179-184.
Impact Factor: 1.47
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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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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 (425 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2001 Nov 30; 314(3): 507-518.
Impact Factor: 5.826
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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 (574 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2000 Nov 10; 303(5): 761-771.
Impact Factor: 5.388
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* Rational Design of a User-Friendly Aptamer/Peptide-Based Device for the Detection of Staphylococcus aureus (84 views)
Sensors (ISSN: 1424-8220linking, 1424-3210), 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 (1926 views)
Ital J Pediatr (ISSN: 1720-8424, 1824-7288), 2017 Apr; 43(1): 34-34.
Impact Factor: 1.776
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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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Calce E, Mignogna E, Bugatti V, Galdiero M, Vittoria V, De Luca S
* Pectin functionalized with natural fatty acids as antimicrobial agent (389 views)
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 (363 views)
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 (425 views)
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 (420 views)
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 (488 views)
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 (505 views)
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 (496 views)
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 (477 views)
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 (371 views)
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 (1515 views)
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 (662 views)
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 (1011 views)
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 (510 views)
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
* 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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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 (321 views)
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 (379 views)
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 (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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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 (315 views)
Critical Care Medicine (ISSN: 0090-3493), 2008 Sep; 36(9): 2629-2633.
Impact Factor: 6.594
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Galdiero S, Galdiero M, Pedone C
* Beta-Barrel Membrane Bacterial Proteins: Structure, Function, Assembly And Interaction With Lipids (438 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2007 Feb; 8(1): 63-82.
Impact Factor: 3.259
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Galdiero S, Gouaux E
* High Resolution Crystallographic Studies Of Alpha-Hemolysin-Phospholipid Complexes Define Heptamer-Lipid Head Group Interactions: Implication For Understanding Protein-Lipid Interactions (320 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2004 Jun; 13(6): 1503-1511.
Impact Factor: 4.116
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Digilio Filomena A, Morra R, Pedone E, Bartolucci S, Rossi M
* High-level expression of Aliciclobacillus acidocaldarius thioredoxin in Pichia pastoris and Bacillus subtilis (233 views)
Protein Expr Purif (ISSN: 1046-5928), 2003 Sep; 30(2): 179-184.
Impact Factor: 1.47
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
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 (425 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2001 Nov 30; 314(3): 507-518.
Impact Factor: 5.826
View Export to BibTeX Export to 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 (574 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2000 Nov 10; 303(5): 761-771.
Impact Factor: 5.388
View Export to BibTeX Export to EndNote
27 Records (25 excluding Abstracts).
Total impact factor: 103.926 (97.799 excluding Abstracts).
Total 5 year impact factor: 98.412 (92.066 excluding Abstracts).
Total impact factor: 103.926 (97.799 excluding Abstracts).
Total 5 year impact factor: 98.412 (92.066 excluding Abstracts).
423 views. Last view on Monday 27 March 2023, 17:47:08
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