Structural determinants in prion protein folding and stability (596 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 0022-2836linking), 2014 Nov 11; 426(22): 3796-3810.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 4.333, 5-year impact factor: 3.702
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84908192029&partnerID=40&md5=958c192b126bdb6ba8d6c9e76cc7b65d
Keywords: Disulfide Bond, Energy Landscape, Intermediate State, N-Terminal Domain, Prion-Susceptible Species, Octapeptide, Prion Protein, Article, Dielectric Constant, Enthalpy, Human, Nonhuman, Protein Analysis, Protein Folding, Protein Function, Protein Stability, Protein Structure, Simulation, Animals, Calorimetry, Differential Scanning, Disulfides Chemistry Metabolism, Molecular Dynamics Simulation, Mutation, Prions Chemistry Genetics Metabolism, Protein Isoforms, Protein Processing, Post-Translational, Spectrometry, Fluorescence,
Affiliations:
*** IBB - CNR ***
Department of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati, Via Bonomea 265Trieste, Italy
Italian Institute of Technology, Scuola Internazionale Superiore di Studi Avanzati Unit, Via Bonomea 265Trieste, Italy
Department of Physics, Scuola Internazionale Superiore di Studi AvanzatiTrieste, Italy
National Research Council, Institute of Biostructures and Bioimaging, Viale Andrea Doria 6Catania, Italy
Elettra - Sincrotrone Trieste S.C.p.A., AREA Science ParkBasovizza Trieste, Italy
European Center for the Sustainable Impact of Nanotechnology, Veneto Nanotech S.C.p.A.Rovigo, Italy
Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull, Via Augusta 390Barcelona, Spain
References:
Prusiner, S.B., Prions (1998) Proc Natl Acad Sci USA, 95, pp. 13363-1338
Prusiner, S.B., Novel proteinaceous infectious particles cause scrapie (1982) Science, 216, pp. 136-144
Premzl, M., Delbridge, M., Gready, J.E., Wilson, P., Johnson, M., Davis, J., The prion protein gene: Identifying regulatory signals using marsupial sequence (2005) Gene, 349, pp. 121-134
Wopfner, F., Weidenhofer, G., Schneider, R., Von Brunn, A., Gilch, S., Schwarz, T.F., Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein (1999) J Mol Biol, 289, pp. 1163-1178
Aguzzi, A., Baumann, F., Bremer, J., The prion's elusive reason for being (2008) Annu Rev Neurosci, 31, pp. 439-477
Damberger, F.F., Christen, B., Perez, D.R., Hornemann, S., Wuthrich, K., Cellular prion protein conformation and function (2011) Proc Natl Acad Sci USA, 108, pp. 17308-17313
Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R., Wuthrich, K., NMR structure of the mouse prion protein domain PrP(121-231) (1996) Nature, 382, pp. 180-182
Arena, G., La Mendola, D., Pappalardo, G., Sóvágó, I., Rizzarelli, E., Interactions of Cu2+ with prion family peptide fragments: Considerations on affinity, speciation and coordination (2012) Coord Chem Rev, 256, pp. 2202-2218
Hornshaw, M.P., McDermott, J.R., Candy, J.M., Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein (1995) BiochemBiophys Res Commun, 207, pp. 621-629
Brown, D.R., Hafiz, F., Glasssmith, L.L., Wong, B.S., Jones, I.M., Clive, C., Consequences of manganese replacement of copper for prion protein function and proteinase resistance (2000) EMBO J, 19, pp. 1180-1186
Jackson, G.S., Murray, I., Hosszu, L.L., Gibbs, N., Waltho, J.P., Clarke, A.R., Location and properties of metal-binding sites on the human prion protein (2001) Proc Natl Acad Sci USA, 98, pp. 8531-8535
Jones, C.E., Klewpatinond, M., Abdelraheim, S.R., Brown, D.R., Viles, J.H., Probing copper2+ binding to the prion protein using diamagnetic nickel2+ and 1H NMR: The unstructured N terminus facilitates the coordination of six copper2+ ions at physiological concentrations (2005) J Mol Biol, 346, pp. 1393-1407
Singh, N., Das, D., Singh, A., Mohan, M.L., Prion protein and metal interaction: Physiological and pathological implications (2010) Curr Issues Mol Biol, 12, pp. 99-107
Benetti, F., Legname, G., De novo mammalian prion synthesis (2009) Prion, 3, pp. 213-219
Pan, K.M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins (1993) Proc Natl Acad Sci USA, 90, pp. 10962-10966
Pergami, P., Jaffe, H., Safar, J., Semipreparative chromatographic method to purify the normal cellular isoform of the prion protein in nondenatured form (1996) Anal Biochem, 236, pp. 63-73
Kuwata, K., Li, H., Yamada, H., Legname, G., Prusiner, S.B., Akasaka, K., Locally disordered conformer of the hamster prion protein: A crucial intermediate to PrPSc? (2002) Biochemistry, 41, pp. 12277-12283
Cohen, F.E., Prusiner, S.B., Pathologic conformations of prion proteins (1998) Annu Rev Biochem, 67, pp. 793-819
Hill, A.F., Antoniou, M., Collinge, J., Protease-resistant prion protein produced in vitro lacks detectable infectivity (1999) J Gen Virol, 80, pp. 11-14
Colby, D.W., Prusiner, S.B., Prions (2011) Cold Spring Harbor Perspect Biol, 3, p. a006833
McKinley, M.P., Bolton, D.C., Prusiner, S.B., A protease-resistant protein is a structural component of the scrapie prion (1983) Cell, 35, pp. 57-62
Zanusso, G., Farinazzo, A., Prelli, F., Fiorini, M., Gelati, M., Ferrari, S., Identification of distinct N-terminal truncated forms of prion protein in different Creutzfeldt-Jakob disease subtypes (2004) J Biol Chem, 279, pp. 38936-38942
Zou, W.Q., Capellari, S., Parchi, P., Sy, M.S., Gambetti, P., Chen, S.G., Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease (2003) J Biol Chem, 278, pp. 40429-40436
Legname, G., Baskakov, I.V., Nguyen, H.O., Riesner, D., Cohen, F.E., DeArmond, S.J., Synthetic mammalian prions (2004) Science, 305, pp. 673-676
Colby, D.W., Giles, K., Legname, G., Wille, H., Baskakov, I.V., DeArmond, S.J., Design and construction of diverse mammalian prion strains (2009) Proc Natl Acad Sci USA, 106, pp. 20417-20422
Baskakov, I.V., Legname, G., Prusiner, S.B., Cohen, F.E., Folding of prion protein to its native alpha-helical conformation is under kinetic control (2001) J Biol Chem, 276, pp. 19687-19690
Palmer, M.S., Mahal, S.P., Campbell, T.A., Hill, A.F., Sidle, K.C., Laplanche, J.L., Deletions in the prion protein gene are not associated with CJD (1993) Hum Mol Genet, 2, pp. 541-544
Giachin, G., Biljan, I., Ilc, G., Plavec, J., Legname, G., Probing early misfolding events in prion protein mutants by NMR spectroscopy (2013) Molecules, 18, pp. 9451-9476
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Morrissey, M.P., Shakhnovich, E.I., Evidence for the role of PrP(C) helix 1 in the hydrophilic seeding of prion aggregates (1999) Proc Natl Acad Sci USA, 96, pp. 11293-11298
Speare, J.O., Rush, T.S., Bloom, M.E., Caughey, B., The role of helix 1 aspartates and salt bridges in the stability and conversion of prion protein (2003) J Biol Chem, 278, pp. 12522-12529
Watzlawik, J., Skora, L., Frense, D., Griesinger, C., Zweckstetter, M., Schulz-Schaeffer, W.J., Prion protein helix1 promotes aggregation but is not converted into beta-sheet (2006) J Biol Chem, 281, pp. 30242-30250
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Chianini, F., Sisó, S., Ricci, E., Eaton, S.L., Finlayson, J., Pang, Y., Pathogenesis of scrapie in ARQ/ARQ sheep after subcutaneous infection: Effect of lymphadenectomy and immune cell subset changes in relation to prion protein accumulation (2013) Vet Immunol Immunopathol, 152, pp. 348-358
Kiss, R.S., Ryan, R.O., Hicks, L.D., Oikawa, K., Kay, C.M., Physical properties of apolipoprotein A-I from the chicken, Gallus domesticus (1993) Biochemistry, 32, pp. 7872-7878
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Maiti, N.R., Surewicz, W.K., The role of disulfide bridge in the folding and stability of the recombinant human prion protein (2001) J Biol Chem, 276, pp. 2427-2431
Jaffrey, S.R., Snyder, S.H., The biotin switch method for the detection of S-nitrosylated proteins (2001) Sci STKE, 2001, p. l1
Ning, L., Guo, J., Jin, N., Liu, H., Yao, X., The role of Cys179- Cys214 disulfide bond in the stability and folding of prion protein: Insights from molecular dynamics simulations (2014) J Mol Model, 20, p. 2106
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McDonald, A.J., Millhauser, G.L., PrP overdrive: Does inhibition of alpha-cleavage contribute to PrP toxicity and prion disease? (2014) Prion, 8. , Epub 2014 Apr 10
Legname, G., Early structural features in mammalian prion conformation conversion (2012) Prion, 6, pp. 37-39
Govaerts, C., Wille, H., Prusiner, S.B., Cohen, F.E., Evidence for assembly of prions with left-handed beta-helices into trimers (2004) Proc Natl Acad Sci USA, 101, pp. 8342-8347
Kosmac, M., Koren, S., Giachin, G., Stoilova, T., Gennaro, R., Legname, G., Epitope mapping of a PrP(Sc)-specific monoclonal antibody: Identification of a novel C-terminally truncated prion fragment (2011) Mol Immunol, 48, pp. 746-750
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Becktel, W.J., Schellman, J.A., Protein stability curves (1987) Biopolymers, 26, pp. 1859-1877
Wang, J., Wolf, R.M., Caldwell, J.W., Kollman, P.A., Case, D.A., Development and testing of a general amber force field (2004) J Comput Chem, 25, pp. 1157-1174
Jorgensen, W.L., Chandrasekhar, J., Madura, J.D., Impey, R.W., Klein, M.L., Comparison of simple potential functions for simulating liquid water (1983) J Chem Phys, 79, pp. 926-935
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Hoover, W.G., Canonical dynamics: Equilibrium phase-space distributions (1985) Phys Rev A, 31, pp. 1695-1697
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Daura, X., Gademann, K., Jaun, B., Seebach, D., Van Gunsteren, W., Mark, A., Peptide folding: When simulation meets experiment (1999) Angew Chem Int Ed, 38, pp. 236-240
Biarnés, X., Pietrucci, F., Marinelli, F., Laio, A., METAGUI. A VMD interface for analyzing metadynamics and molecular dynamics simulations (2012) Comput Phys Commun, 183, pp. 203-211
Humphrey, W., Dalke, A., Schulten, K., VMD: Visual molecular dynamics (1996) J Mol Graphics, 14, pp. 33-38
Noé, F., Horenko, I., Schütte, C., Smith, J., Hierarchical analysis of conformational dynamics in biomolecules: Transition networks of metastable states (2007) J Chem Phys, 126, p. 155102
Prusiner, S. B., Prions (1998) Proc Natl Acad Sci USA, 95, pp. 13363-1338
Prusiner, S. B., Novel proteinaceous infectious particles cause scrapie (1982) Science, 216, pp. 136-144
Damberger, F. F., Christen, B., Perez, D. R., Hornemann, S., Wuthrich, K., Cellular prion protein conformation and function (2011) Proc Natl Acad Sci USA, 108, pp. 17308-17313
Hornshaw, M. P., McDermott, J. R., Candy, J. M., Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein (1995) BiochemBiophys Res Commun, 207, pp. 621-629
Brown, D. R., Hafiz, F., Glasssmith, L. L., Wong, B. S., Jones, I. M., Clive, C., Consequences of manganese replacement of copper for prion protein function and proteinase resistance (2000) EMBO J, 19, pp. 1180-1186
Jackson, G. S., Murray, I., Hosszu, L. L., Gibbs, N., Waltho, J. P., Clarke, A. R., Location and properties of metal-binding sites on the human prion protein (2001) Proc Natl Acad Sci USA, 98, pp. 8531-8535
Jones, C. E., Klewpatinond, M., Abdelraheim, S. R., Brown, D. R., Viles, J. H., Probing copper2+ binding to the prion protein using diamagnetic nickel2+ and 1H NMR: The unstructured N terminus facilitates the coordination of six copper2+ ions at physiological concentrations (2005) J Mol Biol, 346, pp. 1393-1407
Pan, K. M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins (1993) Proc Natl Acad Sci USA, 90, pp. 10962-10966
Cohen, F. E., Prusiner, S. B., Pathologic conformations of prion proteins (1998) Annu Rev Biochem, 67, pp. 793-819
Hill, A. F., Antoniou, M., Collinge, J., Protease-resistant prion protein produced in vitro lacks detectable infectivity (1999) J Gen Virol, 80, pp. 11-14
Colby, D. W., Prusiner, S. B., Prions (2011) Cold Spring Harbor Perspect Biol, 3, p. a006833
McKinley, M. P., Bolton, D. C., Prusiner, S. B., A protease-resistant protein is a structural component of the scrapie prion (1983) Cell, 35, pp. 57-62
Zou, W. Q., Capellari, S., Parchi, P., Sy, M. S., Gambetti, P., Chen, S. G., Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease (2003) J Biol Chem, 278, pp. 40429-40436
Colby, D. W., Giles, K., Legname, G., Wille, H., Baskakov, I. V., DeArmond, S. J., Design and construction of diverse mammalian prion strains (2009) Proc Natl Acad Sci USA, 106, pp. 20417-20422
Baskakov, I. V., Legname, G., Prusiner, S. B., Cohen, F. E., Folding of prion protein to its native alpha-helical conformation is under kinetic control (2001) J Biol Chem, 276, pp. 19687-19690
Palmer, M. S., Mahal, S. P., Campbell, T. A., Hill, A. F., Sidle, K. C., Laplanche, J. L., Deletions in the prion protein gene are not associated with CJD (1993) Hum Mol Genet, 2, pp. 541-544
Morrissey, M. P., Shakhnovich, E. I., Evidence for the role of PrP (C) helix 1 in the hydrophilic seeding of prion aggregates (1999) Proc Natl Acad Sci USA, 96, pp. 11293-11298
Speare, J. O., Rush, T. S., Bloom, M. E., Caughey, B., The role of helix 1 aspartates and salt bridges in the stability and conversion of prion protein (2003) J Biol Chem, 278, pp. 12522-12529
Chianini, F., Sis, S., Ricci, E., Eaton, S. L., Finlayson, J., Pang, Y., Pathogenesis of scrapie in ARQ/ARQ sheep after subcutaneous infection: Effect of lymphadenectomy and immune cell subset changes in relation to prion protein accumulation (2013) Vet Immunol Immunopathol, 152, pp. 348-358
Kiss, R. S., Ryan, R. O., Hicks, L. D., Oikawa, K., Kay, C. M., Physical properties of apolipoprotein A-I from the chicken, Gallus domesticus (1993) Biochemistry, 32, pp. 7872-7878
Maiti, N. R., Surewicz, W. K., The role of disulfide bridge in the folding and stability of the recombinant human prion protein (2001) J Biol Chem, 276, pp. 2427-2431
Jaffrey, S. R., Snyder, S. H., The biotin switch method for the detection of S-nitrosylated proteins (2001) Sci STKE, 2001, p. l1
McDonald, A. J., Millhauser, G. L., PrP overdrive: Does inhibition of alpha-cleavage contribute to PrP toxicity and prion disease? (2014) Prion, 8. , Epub 2014 Apr 10
Van Den Ent, F., L we, J., RF cloning: A restriction-free method for inserting target genes into plasmids (2006) J Biochem Biophys Methods, 67, pp. 67-74
Studier, F. W., Protein production by auto-induction in high density shaking cultures (2005) Protein Expression Purif, 41, pp. 207-234
Becktel, W. J., Schellman, J. A., Protein stability curves (1987) Biopolymers, 26, pp. 1859-1877
Wang, J., Wolf, R. M., Caldwell, J. W., Kollman, P. A., Case, D. A., Development and testing of a general amber force field (2004) J Comput Chem, 25, pp. 1157-1174
Jorgensen, W. L., Chandrasekhar, J., Madura, J. D., Impey, R. W., Klein, M. L., Comparison of simple potential functions for simulating liquid water (1983) J Chem Phys, 79, pp. 926-935
Nos, S., A molecular dynamics method for simulations in the canonical ensemble (2002) Mol Phys, 100, pp. 191-198
Hoover, W. G., Canonical dynamics: Equilibrium phase-space distributions (1985) Phys Rev A, 31, pp. 1695-1697
Biarn s, X., Pietrucci, F., Marinelli, F., Laio, A., METAGUI. A VMD interface for analyzing metadynamics and molecular dynamics simulations (2012) Comput Phys Commun, 183, pp. 203-211
No, F., Horenko, I., Sch tte, C., Smith, J., Hierarchical analysis of conformational dynamics in biomolecules: Transition networks of metastable states (2007) J Chem Phys, 126, p. 155102
J Mol Biol (ISSN: 0022-2836, 1089-8638, 0022-2836linking), 2014 Nov 11; 426(22): 3796-3810.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 4.333, 5-year impact factor: 3.702
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84908192029&partnerID=40&md5=958c192b126bdb6ba8d6c9e76cc7b65d
Keywords: Disulfide Bond, Energy Landscape, Intermediate State, N-Terminal Domain, Prion-Susceptible Species, Octapeptide, Prion Protein, Article, Dielectric Constant, Enthalpy, Human, Nonhuman, Protein Analysis, Protein Folding, Protein Function, Protein Stability, Protein Structure, Simulation, Animals, Calorimetry, Differential Scanning, Disulfides Chemistry Metabolism, Molecular Dynamics Simulation, Mutation, Prions Chemistry Genetics Metabolism, Protein Isoforms, Protein Processing, Post-Translational, Spectrometry, Fluorescence,
Affiliations:
*** IBB - CNR ***
Department of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati, Via Bonomea 265Trieste, Italy
Italian Institute of Technology, Scuola Internazionale Superiore di Studi Avanzati Unit, Via Bonomea 265Trieste, Italy
Department of Physics, Scuola Internazionale Superiore di Studi AvanzatiTrieste, Italy
National Research Council, Institute of Biostructures and Bioimaging, Viale Andrea Doria 6Catania, Italy
Elettra - Sincrotrone Trieste S.C.p.A., AREA Science ParkBasovizza Trieste, Italy
European Center for the Sustainable Impact of Nanotechnology, Veneto Nanotech S.C.p.A.Rovigo, Italy
Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull, Via Augusta 390Barcelona, Spain
References:
Prusiner, S.B., Prions (1998) Proc Natl Acad Sci USA, 95, pp. 13363-1338
Prusiner, S.B., Novel proteinaceous infectious particles cause scrapie (1982) Science, 216, pp. 136-144
Premzl, M., Delbridge, M., Gready, J.E., Wilson, P., Johnson, M., Davis, J., The prion protein gene: Identifying regulatory signals using marsupial sequence (2005) Gene, 349, pp. 121-134
Wopfner, F., Weidenhofer, G., Schneider, R., Von Brunn, A., Gilch, S., Schwarz, T.F., Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein (1999) J Mol Biol, 289, pp. 1163-1178
Aguzzi, A., Baumann, F., Bremer, J., The prion's elusive reason for being (2008) Annu Rev Neurosci, 31, pp. 439-477
Damberger, F.F., Christen, B., Perez, D.R., Hornemann, S., Wuthrich, K., Cellular prion protein conformation and function (2011) Proc Natl Acad Sci USA, 108, pp. 17308-17313
Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R., Wuthrich, K., NMR structure of the mouse prion protein domain PrP(121-231) (1996) Nature, 382, pp. 180-182
Arena, G., La Mendola, D., Pappalardo, G., Sóvágó, I., Rizzarelli, E., Interactions of Cu2+ with prion family peptide fragments: Considerations on affinity, speciation and coordination (2012) Coord Chem Rev, 256, pp. 2202-2218
Hornshaw, M.P., McDermott, J.R., Candy, J.M., Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein (1995) BiochemBiophys Res Commun, 207, pp. 621-629
Brown, D.R., Hafiz, F., Glasssmith, L.L., Wong, B.S., Jones, I.M., Clive, C., Consequences of manganese replacement of copper for prion protein function and proteinase resistance (2000) EMBO J, 19, pp. 1180-1186
Jackson, G.S., Murray, I., Hosszu, L.L., Gibbs, N., Waltho, J.P., Clarke, A.R., Location and properties of metal-binding sites on the human prion protein (2001) Proc Natl Acad Sci USA, 98, pp. 8531-8535
Jones, C.E., Klewpatinond, M., Abdelraheim, S.R., Brown, D.R., Viles, J.H., Probing copper2+ binding to the prion protein using diamagnetic nickel2+ and 1H NMR: The unstructured N terminus facilitates the coordination of six copper2+ ions at physiological concentrations (2005) J Mol Biol, 346, pp. 1393-1407
Singh, N., Das, D., Singh, A., Mohan, M.L., Prion protein and metal interaction: Physiological and pathological implications (2010) Curr Issues Mol Biol, 12, pp. 99-107
Benetti, F., Legname, G., De novo mammalian prion synthesis (2009) Prion, 3, pp. 213-219
Pan, K.M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins (1993) Proc Natl Acad Sci USA, 90, pp. 10962-10966
Pergami, P., Jaffe, H., Safar, J., Semipreparative chromatographic method to purify the normal cellular isoform of the prion protein in nondenatured form (1996) Anal Biochem, 236, pp. 63-73
Kuwata, K., Li, H., Yamada, H., Legname, G., Prusiner, S.B., Akasaka, K., Locally disordered conformer of the hamster prion protein: A crucial intermediate to PrPSc? (2002) Biochemistry, 41, pp. 12277-12283
Cohen, F.E., Prusiner, S.B., Pathologic conformations of prion proteins (1998) Annu Rev Biochem, 67, pp. 793-819
Hill, A.F., Antoniou, M., Collinge, J., Protease-resistant prion protein produced in vitro lacks detectable infectivity (1999) J Gen Virol, 80, pp. 11-14
Colby, D.W., Prusiner, S.B., Prions (2011) Cold Spring Harbor Perspect Biol, 3, p. a006833
McKinley, M.P., Bolton, D.C., Prusiner, S.B., A protease-resistant protein is a structural component of the scrapie prion (1983) Cell, 35, pp. 57-62
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McKinley, M. P., Bolton, D. C., Prusiner, S. B., A protease-resistant protein is a structural component of the scrapie prion (1983) Cell, 35, pp. 57-62
Zou, W. Q., Capellari, S., Parchi, P., Sy, M. S., Gambetti, P., Chen, S. G., Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease (2003) J Biol Chem, 278, pp. 40429-40436
Colby, D. W., Giles, K., Legname, G., Wille, H., Baskakov, I. V., DeArmond, S. J., Design and construction of diverse mammalian prion strains (2009) Proc Natl Acad Sci USA, 106, pp. 20417-20422
Baskakov, I. V., Legname, G., Prusiner, S. B., Cohen, F. E., Folding of prion protein to its native alpha-helical conformation is under kinetic control (2001) J Biol Chem, 276, pp. 19687-19690
Palmer, M. S., Mahal, S. P., Campbell, T. A., Hill, A. F., Sidle, K. C., Laplanche, J. L., Deletions in the prion protein gene are not associated with CJD (1993) Hum Mol Genet, 2, pp. 541-544
Morrissey, M. P., Shakhnovich, E. I., Evidence for the role of PrP (C) helix 1 in the hydrophilic seeding of prion aggregates (1999) Proc Natl Acad Sci USA, 96, pp. 11293-11298
Speare, J. O., Rush, T. S., Bloom, M. E., Caughey, B., The role of helix 1 aspartates and salt bridges in the stability and conversion of prion protein (2003) J Biol Chem, 278, pp. 12522-12529
Chianini, F., Sis, S., Ricci, E., Eaton, S. L., Finlayson, J., Pang, Y., Pathogenesis of scrapie in ARQ/ARQ sheep after subcutaneous infection: Effect of lymphadenectomy and immune cell subset changes in relation to prion protein accumulation (2013) Vet Immunol Immunopathol, 152, pp. 348-358
Kiss, R. S., Ryan, R. O., Hicks, L. D., Oikawa, K., Kay, C. M., Physical properties of apolipoprotein A-I from the chicken, Gallus domesticus (1993) Biochemistry, 32, pp. 7872-7878
Maiti, N. R., Surewicz, W. K., The role of disulfide bridge in the folding and stability of the recombinant human prion protein (2001) J Biol Chem, 276, pp. 2427-2431
Jaffrey, S. R., Snyder, S. H., The biotin switch method for the detection of S-nitrosylated proteins (2001) Sci STKE, 2001, p. l1
McDonald, A. J., Millhauser, G. L., PrP overdrive: Does inhibition of alpha-cleavage contribute to PrP toxicity and prion disease? (2014) Prion, 8. , Epub 2014 Apr 10
Van Den Ent, F., L we, J., RF cloning: A restriction-free method for inserting target genes into plasmids (2006) J Biochem Biophys Methods, 67, pp. 67-74
Studier, F. W., Protein production by auto-induction in high density shaking cultures (2005) Protein Expression Purif, 41, pp. 207-234
Becktel, W. J., Schellman, J. A., Protein stability curves (1987) Biopolymers, 26, pp. 1859-1877
Wang, J., Wolf, R. M., Caldwell, J. W., Kollman, P. A., Case, D. A., Development and testing of a general amber force field (2004) J Comput Chem, 25, pp. 1157-1174
Jorgensen, W. L., Chandrasekhar, J., Madura, J. D., Impey, R. W., Klein, M. L., Comparison of simple potential functions for simulating liquid water (1983) J Chem Phys, 79, pp. 926-935
Nos, S., A molecular dynamics method for simulations in the canonical ensemble (2002) Mol Phys, 100, pp. 191-198
Hoover, W. G., Canonical dynamics: Equilibrium phase-space distributions (1985) Phys Rev A, 31, pp. 1695-1697
Biarn s, X., Pietrucci, F., Marinelli, F., Laio, A., METAGUI. A VMD interface for analyzing metadynamics and molecular dynamics simulations (2012) Comput Phys Commun, 183, pp. 203-211
No, F., Horenko, I., Sch tte, C., Smith, J., Hierarchical analysis of conformational dynamics in biomolecules: Transition networks of metastable states (2007) J Chem Phys, 126, p. 155102
Structural determinants in prion protein folding and stability
Prions are responsible for a heterogeneous group of fatal neurodegenerative diseases, involving post-translational modifications of the cellular prion protein. Epidemiological studies on Creutzfeldt-Jakob disease, a prototype prion disorder, show a majority of cases being sporadic, while the remaining occurrences are either genetic or iatrogenic. The molecular mechanisms by which PrPC is converted into its pathological isoform have not yet been established. While point mutations and seeds trigger the protein to cross the energy barriers, thus causing genetic and infectious transmissible spongiform encephalopathies, respectively, the mechanism responsible for sporadic forms remains unclear. Since prion diseases are protein-misfolding disorders, we investigated prion protein folding and stability as functions of different milieus. Using spectroscopic techniques and atomistic simulations, we dissected the contribution of major structural determinants, also defining the energy landscape of prion protein. In particular, we elucidated (i) the essential role of the octapeptide region in prion protein folding and stability, (ii) the presence of a very enthalpically stable intermediate in prion-susceptible species, and (iii) the role of the disulfide bridge in prion protein folding.
Prions are responsible for a heterogeneous group of fatal neurodegenerative diseases, involving post-translational modifications of the cellular prion protein. Epidemiological studies on Creutzfeldt-Jakob disease, a prototype prion disorder, show a majority of cases being sporadic, while the remaining occurrences are either genetic or iatrogenic. The molecular mechanisms by which PrPC is converted into its pathological isoform have not yet been established. While point mutations and seeds trigger the protein to cross the energy barriers, thus causing genetic and infectious transmissible spongiform encephalopathies, respectively, the mechanism responsible for sporadic forms remains unclear. Since prion diseases are protein-misfolding disorders, we investigated prion protein folding and stability as functions of different milieus. Using spectroscopic techniques and atomistic simulations, we dissected the contribution of major structural determinants, also defining the energy landscape of prion protein. In particular, we elucidated (i) the essential role of the octapeptide region in prion protein folding and stability, (ii) the presence of a very enthalpically stable intermediate in prion-susceptible species, and (iii) the role of the disulfide bridge in prion protein folding.
Structural determinants in prion protein folding and stability
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Structural determinants in prion protein folding and stability
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* Exploring the catalytic mechanism of the first dimeric Bcp: Functional, structural and docking analyses of Bcp4 from Sulfolobus solfataricus (373 views)
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Impact Factor: 3.787
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La Mendola D, Magrì A, Campagna T, Campitiello MA, Raiola L, Isernia C, Hansson O, Bonomo RP, Rizzarelli E
* A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein (1115 views)
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Impact Factor: 5.476
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De Simone G, Supuran CT
* Carbonic anhydrase IX: Biochemical and crystallographic characterization of a novel antitumor target (398 views)
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Impact Factor: 2.773
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Pedone E, Limauro D, Bartolucci S
* The Machinery for Oxidative Protein Folding in Thermophiles (vol 10, pg 157, 2008) (315 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2010 Jan; 12(1): 157-169.
Impact Factor: 8.209
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Ruggiero A, Masullo M, Marasco D, Ruocco MR, Grimaldi P, Arcari P, Zagari A, Vitagliano L
* The dimeric structure of Sulfolobus solfataricus thioredoxin A2 and the basis of its thermostability (316 views)
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Impact Factor: 3.085
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Alterio V, Hilvo M, Di Fiore A, Supuran CT, Pan P, Parkkila S, Scaloni A, Pastorek J, Pastorekova S, Pedone C, Scozzafava A, Monti SM, De Simone G
* Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX (571 views)
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Impact Factor: 9.432
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D'Ambrosio K, Limauro D, Pedone E, Galdi I, Pedone C, Bartolucci S, De Simone G
* Insights into the catalytic mechanism of the Bcp family: functional and structural analysis of Bcp1 from Sulfolobus solfataricus (469 views)
Proteins (ISSN: 1097-0134, 0887-3585, 1097-0134electronic), 2009 Sep; 76(4): 995-1006.
Impact Factor: 3.085
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Accardo A, Tesauro D, Morisco A, Mangiapia G, Vaccaro M, Gianolio E, Heenan RK, Paduano L, Morelli G
* Micelles obtained by aggregation of gemini surfactants containing the CCK8 peptide and a gadolinium complex (398 views)
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Impact Factor: 3.415
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Hilvo M, Baranauskiene L, Salzano AM, Scaloni A, Matulis D, Innocenti A, Scozzafava A, Monti SM, Di Fiore A, De Simone G, Lindfors M, Janis J, Valjakka J, Pastorekova S, Pastorek J, Kulomaa MS, Nordlund HR, Supuran CT, Parkkila S
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Impact Factor: 5.52
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Dalla Serra M, Cirioni O, Vitale RM, Renzone G, Coraiola M, Giacometti A, Potrich C, Baroni E, Guella G, Sanseverino M, De Luca S, Scalise G, Amodeo P, Scaloni A
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Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 29; 47(30): 7888-7899.
Impact Factor: 3.379
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Pedone E, Limauro D, Bartolucci S
* The machinery for oxidative protein folding in thermophiles (337 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2008 Jan; 10(1): 157-169.
Impact Factor: 6.19
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Pedone E, Limauro D, D'Alterio R, Rossi M, Bartolucci S
* Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (328 views)
Febs Journal (ISSN: 1742-464x), 2006 Dec; 273(23): 5407-5420.
Impact Factor: 3.033
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De Simone A, Berisio R, Zagari A, Vitagliano L
* Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation (485 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 740-747.
Impact Factor: 1.801
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Calvanese L, Saporito A, Marasco D, D'Auria G, Minchiotti G, Pedone C, Paolillo L, Falcigno L, Ruvo M
* Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala (444 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Nov 30; 49(24): 7054-7062.
Impact Factor: 5.115
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D'Ambrosio K, Pedone E, Langella E, De Simone G, Rossi M, Pedone C, Bartolucci S
* A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: Structure, function and electrostatics (475 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Sep 29; 362(4): 743-752.
Impact Factor: 4.89
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De Simone G, Vitale RM, Di Fiore A, Pedone C, Scozzafava A, Montero JL, Winum JY, Supuran CT
* Carbonic anhydrase inhibitors: Hypoxia-activatable sulfonamides incorporating disulfide bonds that target the tumor-associated isoform IX (474 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Sep 7; 49(18): 5544-5551.
Impact Factor: 5.115
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Pedone E, D'Ambrosio K, De Simone G, Rossi M, Pedone C, Bartolucci S
* Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus (391 views)
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Impact Factor: 4.89
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Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F
* The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants (441 views)
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Impact Factor: 5.854
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Picone D, Di Fiore A, Ercole C, Franzese M, Sica F, Tomaselli S, Mazzarella L
* The role of the hinge loop in domain swapping - The special case of bovine seminal ribonuclease (365 views)
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Impact Factor: 5.854
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Esposito L, De Simone A, Zagari A, Vitagliano L
* Correlation Between Omega And Psi Dihedral Angles In Protein Structures (592 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2005 Apr 1; 347(3): 483-487.
Impact Factor: 5.229
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Sica F, Di Fiore A, Merlino A, Mazzarella L
* Structure and stability of the non-covalent swapped dimer of bovine seminal ribonuclease - An enzyme tailored to evade ribonuclease protein inhibitor (443 views)
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Impact Factor: 6.355
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Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L
* Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer (384 views)
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Impact Factor: 2.863
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Sica F, Di Fiore A, Zagari A, Mazzarella L
* The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative (355 views)
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Impact Factor: 4.313
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Orru S, Vitagliano L, Esposito L, Mazzarella L, Marino G, Ruoppolo M
Effect of deamidation on folding of ribonuclease (385 views)
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* More Is Always Better Than One: The N-Terminal Domain of the Spike Protein as Another Emerging Target for Hampering the SARS-CoV-2 Attachment to Host Cells (27 views)
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Lanza V, Travaglia A, Malgieri G, Fattorusso R, GrassoG, Di Natale G, Zito V, Arena G, Milardi D, Rizzarelli E
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Sandomenico A, Focà A, Sanguigno L, Caporale A, Focà G, Pignalosa A, Corvino G, Caragnano A, Beltrami AP, Antoniali G, Tell G, Leonardi A, Ruvo M
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Guardiani C, Scorciapino MA, Amodeo GF, Grdadolnik J, Pappalardo G, De Pinto V, Ceccarelli M, Casu M
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Impact Factor: 2.876
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Calce E, Vitale RM, Scaloni A, Amodeo P, De Luca S
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Impact Factor: 3.196
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Ringhieri P, Diaferia C, Galdiero S, Palumbo R, Morelli G, Accardo A
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Limauro D, De Simone G, Pirone L, Bartolucci S, D'Ambrosio K, Pedone E
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Impact Factor: 2.306
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Petruk AA, Varriale S, Coscia MR, Mazzarella L, Merlino A, Oreste U
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Cammisa M, Correra A, Andreotti G, Cubellis MV
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Palmieri M, Malgieri G, Russo L, Baglivo I, Esposito S, Netti F, Del Gatto A, De Paola I, Zaccaro L, Pedone PV, Isernia C, Milardi D, Fattorusso R
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Avitabile C, Capparelli R, Rigano MM, Fulgione A, Barone A, Pedone C, Romanelli A
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Poletto M, Vascotto C, Scognamiglio PL, Lirussi L, Marasco D, Tell G
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Travaglia A, La Mendola D, Magrì A, Nicoletti VG, Pietropaolo A, Rizzarelli E
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Pica A, Russo Krauss I, Castellano I, Rossi M, La Cara F, Graziano G, Sica F, Merlino A
* Exploring The Unfolding Mechanism Of Gamma-Glutamyltranspeptidases: The Case Of The Thermophilic Enzyme From Geobacillus Thermodenitrificans (422 views)
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Esposito L, Ruggiero A, Masullo M, Ruocco MR, Lamberti A, Arcari P, Zagari A, Vitagliano L
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Benetti F, Biarnes X, Attanasio F, Rizzarelli E, Laio A, Legname G
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Travaglia A, Arena G, Fattorusso R, Isernia C, La Mendola D, Malgieri G, Nicoletti VG, Rizzarelli E
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Barile E, Leone M, Barile E, Dahl R, Pellecchia M
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Fantini D, Vascotto C, Marasco D, D'Ambrosio C, Romanello M, Vitagliano L, Pedone C, Poletto M, Cesaratto L, Quadrifoglio F, Scaloni A, Radicella JP, Tell G
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Impact Factor: 7.836
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Di Natale G, Pappalardo G, Milardi D, Sciacca MF, Attanasio F, La Mendola D, Rizzarelli E
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Pedone E, Limauro D, D'Ambrosio K, De Simone G, Bartolucci S
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Impact Factor: 7.047
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Limauro D, D'Ambrosio K, Langella E, De Simone G, Galdi I, Pedone C, Pedone E, Bartolucci S
* Exploring the catalytic mechanism of the first dimeric Bcp: Functional, structural and docking analyses of Bcp4 from Sulfolobus solfataricus (373 views)
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Impact Factor: 3.787
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La Mendola D, Magrì A, Campagna T, Campitiello MA, Raiola L, Isernia C, Hansson O, Bonomo RP, Rizzarelli E
* A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein (1115 views)
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Impact Factor: 5.476
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De Simone G, Supuran CT
* Carbonic anhydrase IX: Biochemical and crystallographic characterization of a novel antitumor target (398 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2010 Feb; 1804(2): 404-409.
Impact Factor: 2.773
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Pedone E, Limauro D, Bartolucci S
* The Machinery for Oxidative Protein Folding in Thermophiles (vol 10, pg 157, 2008) (315 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2010 Jan; 12(1): 157-169.
Impact Factor: 8.209
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Ruggiero A, Masullo M, Marasco D, Ruocco MR, Grimaldi P, Arcari P, Zagari A, Vitagliano L
* The dimeric structure of Sulfolobus solfataricus thioredoxin A2 and the basis of its thermostability (316 views)
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Impact Factor: 3.085
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Alterio V, Hilvo M, Di Fiore A, Supuran CT, Pan P, Parkkila S, Scaloni A, Pastorek J, Pastorekova S, Pedone C, Scozzafava A, Monti SM, De Simone G
* Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX (571 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2009 Sep 22; 106(38): 16233-16238.
Impact Factor: 9.432
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D'Ambrosio K, Limauro D, Pedone E, Galdi I, Pedone C, Bartolucci S, De Simone G
* Insights into the catalytic mechanism of the Bcp family: functional and structural analysis of Bcp1 from Sulfolobus solfataricus (469 views)
Proteins (ISSN: 1097-0134, 0887-3585, 1097-0134electronic), 2009 Sep; 76(4): 995-1006.
Impact Factor: 3.085
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Accardo A, Tesauro D, Morisco A, Mangiapia G, Vaccaro M, Gianolio E, Heenan RK, Paduano L, Morelli G
* Micelles obtained by aggregation of gemini surfactants containing the CCK8 peptide and a gadolinium complex (398 views)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257linking), 2009 May; 14(4): 587-599.
Impact Factor: 3.415
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Hilvo M, Baranauskiene L, Salzano AM, Scaloni A, Matulis D, Innocenti A, Scozzafava A, Monti SM, Di Fiore A, De Simone G, Lindfors M, Janis J, Valjakka J, Pastorekova S, Pastorek J, Kulomaa MS, Nordlund HR, Supuran CT, Parkkila S
* Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymes (459 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 10; 283(41): 27799-27809.
Impact Factor: 5.52
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Dalla Serra M, Cirioni O, Vitale RM, Renzone G, Coraiola M, Giacometti A, Potrich C, Baroni E, Guella G, Sanseverino M, De Luca S, Scalise G, Amodeo P, Scaloni A
* Structural features of distinctin affecting peptide biological and biochemical properties (545 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 29; 47(30): 7888-7899.
Impact Factor: 3.379
View Export to BibTeX Export to EndNote
Pedone E, Limauro D, Bartolucci S
* The machinery for oxidative protein folding in thermophiles (337 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2008 Jan; 10(1): 157-169.
Impact Factor: 6.19
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Pedone E, Limauro D, D'Alterio R, Rossi M, Bartolucci S
* Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (328 views)
Febs Journal (ISSN: 1742-464x), 2006 Dec; 273(23): 5407-5420.
Impact Factor: 3.033
View Export to BibTeX Export to EndNote
De Simone A, Berisio R, Zagari A, Vitagliano L
* Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation (485 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 740-747.
Impact Factor: 1.801
View Export to BibTeX Export to EndNote
Calvanese L, Saporito A, Marasco D, D'Auria G, Minchiotti G, Pedone C, Paolillo L, Falcigno L, Ruvo M
* Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala (444 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Nov 30; 49(24): 7054-7062.
Impact Factor: 5.115
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D'Ambrosio K, Pedone E, Langella E, De Simone G, Rossi M, Pedone C, Bartolucci S
* A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: Structure, function and electrostatics (475 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Sep 29; 362(4): 743-752.
Impact Factor: 4.89
View Export to BibTeX Export to EndNote
De Simone G, Vitale RM, Di Fiore A, Pedone C, Scozzafava A, Montero JL, Winum JY, Supuran CT
* Carbonic anhydrase inhibitors: Hypoxia-activatable sulfonamides incorporating disulfide bonds that target the tumor-associated isoform IX (474 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Sep 7; 49(18): 5544-5551.
Impact Factor: 5.115
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Pedone E, D'Ambrosio K, De Simone G, Rossi M, Pedone C, Bartolucci S
* Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus (391 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Feb 10; 356(1): 155-164.
Impact Factor: 4.89
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Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F
* The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants (441 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 May 6; 280(18): 17953-17960.
Impact Factor: 5.854
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Picone D, Di Fiore A, Ercole C, Franzese M, Sica F, Tomaselli S, Mazzarella L
* The role of the hinge loop in domain swapping - The special case of bovine seminal ribonuclease (365 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Apr 8; 280(14): 13771-13778.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Esposito L, De Simone A, Zagari A, Vitagliano L
* Correlation Between Omega And Psi Dihedral Angles In Protein Structures (592 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2005 Apr 1; 347(3): 483-487.
Impact Factor: 5.229
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Sica F, Di Fiore A, Merlino A, Mazzarella L
* Structure and stability of the non-covalent swapped dimer of bovine seminal ribonuclease - An enzyme tailored to evade ribonuclease protein inhibitor (443 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2004 Sep 27; 279(35): 36753-36760.
Impact Factor: 6.355
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Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L
* Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer (384 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 689-695.
Impact Factor: 2.863
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Sica F, Di Fiore A, Zagari A, Mazzarella L
* The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative (355 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2003 Sep 1; 52(2): 263-271.
Impact Factor: 4.313
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Orru S, Vitagliano L, Esposito L, Mazzarella L, Marino G, Ruoppolo M
Effect of deamidation on folding of ribonuclease (385 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2000 Dec; 9(12): 2577-2582.
Impact Factor: 3.869
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45 Records (43 excluding Abstracts).
Total impact factor: 202.068 (195.26 excluding Abstracts).
Total 5 year impact factor: 194.343 (185.98 excluding Abstracts).
Total impact factor: 202.068 (195.26 excluding Abstracts).
Total 5 year impact factor: 194.343 (185.98 excluding Abstracts).
596 views. Last view on Saturday 25 March 2023, 21:38:10
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