Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies (154 visite)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2015 Feb 8; 1854(5): 402-409.
Tipo di articolo: Journal Article,
Impact factor: 5.158, Impact factor a 5 anni: 5.36
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84922879126&partnerID=40&md5=3b16a75c01c8312fc41657ae53bb19d0
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,
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
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.
Tipo di articolo: Journal Article,
Impact factor: 5.158, Impact factor a 5 anni: 5.36
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84922879126&partnerID=40&md5=3b16a75c01c8312fc41657ae53bb19d0
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,
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
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
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.
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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 (171 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2010 Oct; 17(10): 1296-1299.
Impact Factor: 1.849
Dettagli Esporta in BibTeX Esporta in EndNote
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 (163 visite)
Structure (ISSN: 0969-2126, 1878-4186), 2010 Sep 8; 18(9): 1184-1190.
Impact Factor: 6.337
Dettagli Esporta in BibTeX Esporta in EndNote
Alberobello AT, D'Esposito V, Marasco D, Doti N, Ruvo M, Bianco R, Tortora G, Esposito I, Fiory F, Miele C, Beguinot F, Formisano P
* Selective Disruption of Insulin-like Growth Factor-1 (IGF-1) Signaling via Phosphoinositide-dependent Kinase-1 Prevents the Protective Effect of IGF-1 on Human Cancer Cell Death (182 visite)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2010 Feb 26; 285(9): 6563-6572.
Impact Factor: 5.328
Dettagli Esporta in BibTeX Esporta in EndNote
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 (148 visite)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2009 Sep 28; 4(9): e7191-e7191.
Impact Factor: 4.351
Dettagli Esporta in BibTeX Esporta in EndNote
Limauro D, Saviano M, Galdi I, Rossi M, Bartolucci S, Pedone E
* Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites (108 visite)
Protein Engineering Design & Selection (ISSN: 1741-0126), 2009 Jan; 22(1): 19-26.
Impact Factor: 2.596
Dettagli Esporta in BibTeX Esporta in EndNote
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 (139 visite)
Critical Care Medicine (ISSN: 0090-3493), 2008 Sep; 36(9): 2629-2633.
Impact Factor: 6.594
Dettagli Esporta in BibTeX Esporta in EndNote
Prato S, Vitale RM, Contursi P, Lipps G, Saviano M, Rossi M, Bartolucci S
* Molecular modeling and functional characterization of the monomeric primase-polymerase domain from the Sulfolobus solfataricus plasmid pIT3 (175 visite)
Febs J (ISSN: 1742-464x), 2008; 275(17): 4389-4402.
Impact Factor: 3.139
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 (140 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
Pedone E, Saviano M, Bartolucci S, Rossi M, Ausili A, Scire A, Bertoli E, Tanfani F
* Temperature-, SDS-, and pH-induced conformational changes in protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: A dynamic simulation and fourier transform infrared spectroscopic study (130 visite)
J Proteome Res (ISSN: 1535-3893), 2005 Nov; 4(6): 1972-1980.
Impact Factor: 6.901
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 (143 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
Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
* Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus (171 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2003 Dec 16; 42(49): 14397-14407.
Impact Factor: 3.922
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 (113 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 (127 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
Spalletti-cernia D, Sorrentino R, Di Gaetano S, Arciello A, Garbi C, Piccoli R, D'Alessio G, Vecchio G, Laccetti P, Santoro M
* Antineoplastic ribonucleases selectively kill thyroid carcinoma cells via caspase-mediated induction of apoptosis (170 visite)
Journal Of Clinical Endocrinology & Metabolism (ISSN: 0021-972x), 2003 Jun; 88(6): 2900-2907.
Impact Factor: 5.873
Dettagli Esporta in BibTeX Esporta in EndNote
Esposito L, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
* Crystal Structure Of The Alcohol Dehydrogenase From The Hyperthermophilic Archaeon Sulfolobus Solfataricus At 1. 85 Angstrom Resolution (163 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2002 Apr 26; 318(2): 463-477.
Impact Factor: 5.359
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 (159 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 (181 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
42 Records (40 escludendo Abstract e Conferenze).
Impact factor totale: 169.726 (163.599 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 158.075 (151.729 escludendo Abstract e Conferenze).
Impact factor totale: 169.726 (163.599 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 158.075 (151.729 escludendo Abstract e Conferenze).
Esporta in BibTeX Esporta in EndNote
Ultima modifica di Marco Comerci in data Thursday 19 March 2015, 16:43:12
154 visite. Ultima visita in data Thursday 16 January 2020, 23:34:16
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