Copper-triggered aggregation of ubiquitin (533 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2009 Sep 16; 4(9): e7052-e7052.
Export to BibTeX Export to EndNote
Paper type: Abstract, Conference, Research Support, Non-U. S. Gov'T,
Impact factor: 4.351, 5-year impact factor: 4.383
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-75549083286&partnerID=40&md5=accc07268418c75867b98dca8bd31941
Keywords: 2 Oleoyl 1 Palmitoylphosphatidylcholine, Amyloid, Copper, Cupric Ion, Dimer, Oligomer, Ubiquitin, Article, Atomic Force Microscopy, Beta Sheet, Bilayer Membrane, Chelation, Circular Dichroism, Controlled Study, Dielectric Constant, Gel Electrophoresis, Human, Incubation Time, Infrared Spectroscopy, Protein Aggregation, Structure Analysis, Transmission Electron Microscopy, Alzheimer Disease, Cell Membrane, Chelating Agents, Electrochemistry, Molecular Conformation, Proteasome Endopeptidase Complex, Protein Binding, Protein Structure, Secondary, Tertiary, Solvents, Fourier Transform Infrared, Metabolism, Methods,
Affiliations:
*** IBB - CNR ***
Dipartimento Farmaco-Chimico, University of Bari A. Moro, Bari, Italy.
Consorzio Interuniversitario di Ricerca in Chimica dei Metalli nei Sistemi Biologici (CIRCMSB), Bari, Italy
Dipartimento di Chimica, University of Bari A. Moro, Bari, Italy
National Nanotechnology Laboratory of CNR-INFM, IIT Research Unit, University of Salento, Lecce, Italy
Dipartimento di Scienze Chimiche, University of Catania, Catania, Italy
References:
McClellan, A.J., Tam, S., Kaganovich, D., Frydman, J., Protein quality control: Chaperones culling corrupt conformations (2005) Nat Cell Biol, 7, pp. 736-74
Hershko, A., Ciechanover, A., The ubiquitin system (1998) Annu Rev Biochem, 67, pp. 425-479
Pickart, C.M., Fushman, D., Polyubiquitin chains: Polymeric protein signals (2004) Curr Opin Chem Biol, 8, pp. 610-616
Soto, C., Unfolding the role of protein misfolding in neurodegenerative diseases (2003) Nat Rev Neurosci, 4, pp. 49-60
Chiti, F., Dobson, C.M., Protein misfolding, functional amyloid, and human disease (2006) Annu Rev Biochem, 75, pp. 333-366
Brown, D.R., Qin, K., Herms, J.W., Madlung, A., Manson, J., The cellular prion protein binds copper in vivo (1997) Nature, 390, pp. 684-687
Atwood, C.S., Moir, R.D., Huang, X., Scarpa, R.C., Bacarra, N.M., Dramatic aggregation of Alzheimer Ab by Cu(II) is induced by conditions representing physiological acidosis (1998) J Biol Chem, 273, pp. 12817-12826
Paik, S.R., Shin, H.J., Lee, J.H., Chang, C.S., Kim, J., Copper(II)-induced self-oligomerization of alpha-synuclein (1999) Biochem J, 340, pp. 821-828
Morgan, C.J., Gelfand, M., Atreya, C., Miranker, A.D., Kidney dialysis-associated amyloidosis: A molecular role for copper in fiber formation (2001) J Mol Biol, 309, pp. 339-345
Amici, M., Forti, K., Nobili, C., Lupidi, G., Angeletti, M., Effect of neurotoxic metal ions on the proteolytic activities of the 20S proteasome from bovine brain (2002) J Biol Inorg Chem, 7, pp. 750-756
Lowe, J., Blanchard, A., Morrell, K., Lennox, G., Reynolds, L., Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease (1988) J Pathol, 155, pp. 9-15
Ciechanover, A., Brundin, P., The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg (2003) Neuron, 40, pp. 427-446
Ross, C.A., Pickart, C.M., The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases (2004) Trends Cell Biol, 14, pp. 703-711
Lowe, J., Hand, N., Mayer, R.J., Application of ubiquitin immunohistochemistry to the diagnosis of disease (2005) Methods Enzymol, 399, pp. 86-119
Wakabayashi, K., Tanji, K., Mori, F., Takahashi, H., The Lewy body in Parkinson's disease: Molecules implicated in the formation and degradation of alpha-synuclein aggregates (2007) Neuropathology, 27, pp. 494-506
Uversky, V.N., Li, J., Fink, A.L., Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular link between Parkinson's disease and heavy metal exposure (2001) J Biol Chem, 276, pp. 44284-44296
Binolfi, A., Rasia, R.M., Bertoncini, C.W., Ceolin, M., Zweckstetter, M., Interaction of alpha-synuclein with divalent metal ions reveals key differences: A link between structure, binding specificity and fibrillation enhancement (2006) J Am Chem Soc, 128, pp. 9893-9901
Wright, J.A., Brown, D.R., Alpha-synuclein and its role in metal binding: Relevance to Parkinson's disease (2008) J Neurosci Res, 86, pp. 496-503
Jackson, S.E., Ubiquitin: A small protein folding paradigm (2006) Org Biomol Chem, 4, pp. 1845-1853
Milardi, D., Arnesano, F., Grasso, G., Magrì, A., Tabbì, G., Ubiquitin stability and the Lys63-linked polyubiquitination site are compromised on copper binding (2007) Angew Chem Int Ed Engl, 46, pp. 7993-7995
Gaggelli, E., Kozlowski, H., Valensin, D., Valensin, G., Copper homeostasis and neurodegenerative disorders (Alzheimer's, Prion, and Parkinson's diseases and Amyotrophic Lateral Sclerosis) (2006) Chem Rev, 106, pp. 1995-2044
Trovato, A., Chiti, F., Maritan, A., Seno, F., Insight into the structure of amyloid fibrils from the analysis of globular proteins (2006) PLoS Comput Biol, 2, pp. e170
Munishkina, L.A., Phelan, C., Uversky, V.N., Fink, A.L., Conformational behavior and aggregation of alpha-synuclein in organic solvents: Modeling the effects of membranes (2003) Biochemistry, 42, pp. 2720-2730
Chiti, F., Webster, P., Taddei, N., Clark, A., Stefani, M., Designing conditions for in vitro formation of amyloid protofilaments and fibrils (1999) Proc Natl Acad Sci U S A, 96, pp. 3590-3594
Yamaguchi, K., Naiki, H., Goto, Y., Mechanism by which the amyloid-like fibrils of a β2-microglobulin fragment are induced by fluorine-substituted alcohols (2006) J Mol Biol, 363, pp. 279-288
Hawe, A., Sutter, M., Jiskoot, W., Extrinsic fluorescent dyes as tools for protein characterization (2008) Pharm Res, 25, pp. 1487-1499
Hess, S., Lindquist, S.L., Scheibel, T., Alternative assembly pathways of the amyloidogenic yeast prion determinant Sup35-NM (2007) EMBO Rep, 8, pp. 1196-1201
Parag, H.A., Raboy, B., Kulka, R.G., Effect of heat shock on protein degradation in mammalian cells: Involvement of the ubiquitin system (1987) EMBO J, 6, pp. 55-61
Ryu, K.Y., Garza, J.C., Lu, X.Y., Barsh, G.S., Kopito, R.R., Hypothalamic neurodegeneration and adult-onset obesity in mice lacking the Ubb poly-ubiquitin gene (2008) Proc Natl Acad Sci U S A, 105, pp. 4016-4021
Sixt, S.U., Dahlmann, B., Extracellular, circulating proteasomes and ubiquitin - incidence and relevance (2008) Biochim Biophys Acta, 1782, pp. 817-823
Zandomeneghi, G., Krebs, M.R., McCammon, M.G., Fandrich, M., FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils (2004) Protein Sci, 13, pp. 3314-3321
Lowe, R., Pountney, D.L., Jensen, P.H., Gai, W.P., Voelcker, N.H., Calcium(II) selectively induces alpha-synuclein annular oligo via interaction with the C-terminal domain (2004) Protein Sci, 13, pp. 3245-3252
Cole, N.B., Murphy, D.D., Lebowitz, J., Di Noto, L., Levine, R.L., Metal-catalyzed oxidation of alpha-synuclein: Helping to define the relationship between oligomers, protofibrils, and filaments (2005) J Biol Chem, 280, pp. 9678-9690
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (2002) Nature, 416, pp. 507-511
Pellistri, F., Bucciantini, M., Relini, A., Nosi, D., Gliozzi, A., Nonspecific interaction of prefibrillar amyloid aggregates with glutamatergic receptors results in Ca2+ increase in primary neuronal cells (2008) J Biol Chem, 283, pp. 29950-29960
Lashuel, H.A., Membrane permeabilization: A common mechanism in protein-misfolding diseases (2005) Sci Aging Knowledge Environ 2005, pp. e28
Conway, K.A., Lee, S.J., Rochet, J.C., Ding, T.T., Williamson, R.E., Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy (2000) Proc Natl Acad Sci U S A, 97, pp. 571-576
Conway, K.A., Rochet, J.C., Bieganski, R.M., Lansbury Jr, P.T., Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct (2001) Science, 294, pp. 1346-1349
Lashuel, H.A., Hartley, D., Petre, B.M., Walz, T., Lansbury, P.T., Neurodegenerative disease - Amyloid pores from pathogenic mutations (2002) Nature, 418, p. 291
Herrera, F.E., Chesi, A., Paleologou, K.E., Schmid, A., Munoz, A., (2008) Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region, ONE 3, pp. e3394. , PLoS
Bennett, E.J., Bence, N.F., Jayakumar, R., Kopito, R.R., Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation (2005) Mol Cell, 17, pp. 351-365
Lee, J.C., Gray, H.B., Winkler, J.R., Copper(II) binding to alpha-synuclein, the Parkinson's protein (2008) J Am Chem Soc, 130, pp. 6898-6899
Vijay-Kumar, S., Bugg, C.E., Cook, W.J., Structure of ubiquitin refined at 1.8 Å reolution (1987) J Mol Biol, 194, pp. 531-544
Tan, J.M., Wong, E.S., Kirkpatrick, D.S., Pletnikova, O., Ko, H.S., Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases (2008) Hum Mol Genet, 17, pp. 431-439
Maryon, E.B., Molloy, S.A., Zimnicka, A.M., Kaplan, J.H., Copper entry into human cells: Progress and unanswered questions (2007) Biometals, 20, pp. 355-364
Lee, J., Petris, M.J., Thiele, D.J., Characterization of mouse embryonic cells deficient in the Ctr1 high affinity copper transporter. Identification of a Ctr1-independent copper transport system (2002) J Biol Chem, 277, pp. 40253-40259
Moriya, M., Ho, Y.H., Grana, A., Nguyen, L., Alvarez, A., Copper is taken up efficiently from albumin and alpha2-macroglobulin by cultured human cells by more than one mechanism (2008) Am J Physiol Cell Physiol, 295, pp. C708-C721
Pufahl, R.A., Singer, C.P., Peariso, K.L., Lin, S.-J., Schmidt, P.J., Metal ion chaperone function of the soluble Cu(I) receptor Atx1 (1997) Science, 278, pp. 853-856
Xiao, Z., Loughlin, F., George, G.N., Howlett, G.J., Wedd, A.G., C-terminal domain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu(I) ions as a cuprous-thiolate polynuclear cluster: Sub-femtomolar Cu(I) affinity of three proteins involved in copper trafficking (2004) J Am Chem Soc, 126, pp. 3081-3090
Yang, L., McRae, R., Henary, M.M., Patel, R., Lai, B., Imaging of the intracellular topography of copper with a fluorescent sensor and by synchrotron x-ray fluorescence microscopy (2005) Proc Natl Acad Sci U S A, 102, pp. 11179-11184
Chwiej, J., Adamek, D., Szczerbowska-Boruchowska, M., Krygowska-Wajs, A., Bohic, S., Study of Cu chemical state inside single neurons from Parkinson's disease and control substantia nigra using the micro-XANES technique (2008) J Trace Elem Med Biol, 22, pp. 183-188
Rees, E.M., Thiele, D.J., Identification of a vacuole-associated metallo-reductase and its role in Ctr2-mediated intracellular copper mobilization (2007) J Biol Chem, 282, pp. 21629-21638
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Miller, L.M., Wang, Q., Telivala, T.P., Smith, R.J., Lanzirotti, A., Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with beta-amyloid deposits in Alzheimer's disease (2006) J Struct Biol, 155, pp. 30-37
Ide-Ektessabi, A., Rabionet, M., The role of trace metallic elements in neurodegenerative disorders: Quantitative analysis using XRF and XANES spectroscopy (2005) Anal Sci, 21, pp. 885-892
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Gai, W.P., Yuan, H.X., Li, X.Q., Power, J.T., Blumbergs, P.C., In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies (2000) Exp Neurol, 166, pp. 324-333
Sharon, R., Bar-Joseph, I., Frosch, M.P., Walsh, D.M., Hamilton, J.A., The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease (2003) Neuron, 37, pp. 583-595
Quist, A., Doudevski, I., Lin, H., Azimova, R., Ng, D., Amyloid ion channels: A common structural link for protein-misfolding disease (2005) Proc Natl Acad Sci U S A, 102, pp. 10427-10432
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Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2009 Sep 16; 4(9): e7052-e7052.
Export to BibTeX Export to EndNote
Paper type: Abstract, Conference, Research Support, Non-U. S. Gov'T,
Impact factor: 4.351, 5-year impact factor: 4.383
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-75549083286&partnerID=40&md5=accc07268418c75867b98dca8bd31941
Keywords: 2 Oleoyl 1 Palmitoylphosphatidylcholine, Amyloid, Copper, Cupric Ion, Dimer, Oligomer, Ubiquitin, Article, Atomic Force Microscopy, Beta Sheet, Bilayer Membrane, Chelation, Circular Dichroism, Controlled Study, Dielectric Constant, Gel Electrophoresis, Human, Incubation Time, Infrared Spectroscopy, Protein Aggregation, Structure Analysis, Transmission Electron Microscopy, Alzheimer Disease, Cell Membrane, Chelating Agents, Electrochemistry, Molecular Conformation, Proteasome Endopeptidase Complex, Protein Binding, Protein Structure, Secondary, Tertiary, Solvents, Fourier Transform Infrared, Metabolism, Methods,
Affiliations:
*** IBB - CNR ***
Dipartimento Farmaco-Chimico, University of Bari A. Moro, Bari, Italy.
Consorzio Interuniversitario di Ricerca in Chimica dei Metalli nei Sistemi Biologici (CIRCMSB), Bari, Italy
Dipartimento di Chimica, University of Bari A. Moro, Bari, Italy
National Nanotechnology Laboratory of CNR-INFM, IIT Research Unit, University of Salento, Lecce, Italy
Dipartimento di Scienze Chimiche, University of Catania, Catania, Italy
References:
McClellan, A.J., Tam, S., Kaganovich, D., Frydman, J., Protein quality control: Chaperones culling corrupt conformations (2005) Nat Cell Biol, 7, pp. 736-74
Hershko, A., Ciechanover, A., The ubiquitin system (1998) Annu Rev Biochem, 67, pp. 425-479
Pickart, C.M., Fushman, D., Polyubiquitin chains: Polymeric protein signals (2004) Curr Opin Chem Biol, 8, pp. 610-616
Soto, C., Unfolding the role of protein misfolding in neurodegenerative diseases (2003) Nat Rev Neurosci, 4, pp. 49-60
Chiti, F., Dobson, C.M., Protein misfolding, functional amyloid, and human disease (2006) Annu Rev Biochem, 75, pp. 333-366
Brown, D.R., Qin, K., Herms, J.W., Madlung, A., Manson, J., The cellular prion protein binds copper in vivo (1997) Nature, 390, pp. 684-687
Atwood, C.S., Moir, R.D., Huang, X., Scarpa, R.C., Bacarra, N.M., Dramatic aggregation of Alzheimer Ab by Cu(II) is induced by conditions representing physiological acidosis (1998) J Biol Chem, 273, pp. 12817-12826
Paik, S.R., Shin, H.J., Lee, J.H., Chang, C.S., Kim, J., Copper(II)-induced self-oligomerization of alpha-synuclein (1999) Biochem J, 340, pp. 821-828
Morgan, C.J., Gelfand, M., Atreya, C., Miranker, A.D., Kidney dialysis-associated amyloidosis: A molecular role for copper in fiber formation (2001) J Mol Biol, 309, pp. 339-345
Amici, M., Forti, K., Nobili, C., Lupidi, G., Angeletti, M., Effect of neurotoxic metal ions on the proteolytic activities of the 20S proteasome from bovine brain (2002) J Biol Inorg Chem, 7, pp. 750-756
Lowe, J., Blanchard, A., Morrell, K., Lennox, G., Reynolds, L., Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease (1988) J Pathol, 155, pp. 9-15
Ciechanover, A., Brundin, P., The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg (2003) Neuron, 40, pp. 427-446
Ross, C.A., Pickart, C.M., The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases (2004) Trends Cell Biol, 14, pp. 703-711
Lowe, J., Hand, N., Mayer, R.J., Application of ubiquitin immunohistochemistry to the diagnosis of disease (2005) Methods Enzymol, 399, pp. 86-119
Wakabayashi, K., Tanji, K., Mori, F., Takahashi, H., The Lewy body in Parkinson's disease: Molecules implicated in the formation and degradation of alpha-synuclein aggregates (2007) Neuropathology, 27, pp. 494-506
Uversky, V.N., Li, J., Fink, A.L., Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular link between Parkinson's disease and heavy metal exposure (2001) J Biol Chem, 276, pp. 44284-44296
Binolfi, A., Rasia, R.M., Bertoncini, C.W., Ceolin, M., Zweckstetter, M., Interaction of alpha-synuclein with divalent metal ions reveals key differences: A link between structure, binding specificity and fibrillation enhancement (2006) J Am Chem Soc, 128, pp. 9893-9901
Wright, J.A., Brown, D.R., Alpha-synuclein and its role in metal binding: Relevance to Parkinson's disease (2008) J Neurosci Res, 86, pp. 496-503
Jackson, S.E., Ubiquitin: A small protein folding paradigm (2006) Org Biomol Chem, 4, pp. 1845-1853
Milardi, D., Arnesano, F., Grasso, G., Magrì, A., Tabbì, G., Ubiquitin stability and the Lys63-linked polyubiquitination site are compromised on copper binding (2007) Angew Chem Int Ed Engl, 46, pp. 7993-7995
Gaggelli, E., Kozlowski, H., Valensin, D., Valensin, G., Copper homeostasis and neurodegenerative disorders (Alzheimer's, Prion, and Parkinson's diseases and Amyotrophic Lateral Sclerosis) (2006) Chem Rev, 106, pp. 1995-2044
Trovato, A., Chiti, F., Maritan, A., Seno, F., Insight into the structure of amyloid fibrils from the analysis of globular proteins (2006) PLoS Comput Biol, 2, pp. e170
Munishkina, L.A., Phelan, C., Uversky, V.N., Fink, A.L., Conformational behavior and aggregation of alpha-synuclein in organic solvents: Modeling the effects of membranes (2003) Biochemistry, 42, pp. 2720-2730
Chiti, F., Webster, P., Taddei, N., Clark, A., Stefani, M., Designing conditions for in vitro formation of amyloid protofilaments and fibrils (1999) Proc Natl Acad Sci U S A, 96, pp. 3590-3594
Yamaguchi, K., Naiki, H., Goto, Y., Mechanism by which the amyloid-like fibrils of a β2-microglobulin fragment are induced by fluorine-substituted alcohols (2006) J Mol Biol, 363, pp. 279-288
Hawe, A., Sutter, M., Jiskoot, W., Extrinsic fluorescent dyes as tools for protein characterization (2008) Pharm Res, 25, pp. 1487-1499
Hess, S., Lindquist, S.L., Scheibel, T., Alternative assembly pathways of the amyloidogenic yeast prion determinant Sup35-NM (2007) EMBO Rep, 8, pp. 1196-1201
Parag, H.A., Raboy, B., Kulka, R.G., Effect of heat shock on protein degradation in mammalian cells: Involvement of the ubiquitin system (1987) EMBO J, 6, pp. 55-61
Ryu, K.Y., Garza, J.C., Lu, X.Y., Barsh, G.S., Kopito, R.R., Hypothalamic neurodegeneration and adult-onset obesity in mice lacking the Ubb poly-ubiquitin gene (2008) Proc Natl Acad Sci U S A, 105, pp. 4016-4021
Sixt, S.U., Dahlmann, B., Extracellular, circulating proteasomes and ubiquitin - incidence and relevance (2008) Biochim Biophys Acta, 1782, pp. 817-823
Zandomeneghi, G., Krebs, M.R., McCammon, M.G., Fandrich, M., FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils (2004) Protein Sci, 13, pp. 3314-3321
Lowe, R., Pountney, D.L., Jensen, P.H., Gai, W.P., Voelcker, N.H., Calcium(II) selectively induces alpha-synuclein annular oligo via interaction with the C-terminal domain (2004) Protein Sci, 13, pp. 3245-3252
Cole, N.B., Murphy, D.D., Lebowitz, J., Di Noto, L., Levine, R.L., Metal-catalyzed oxidation of alpha-synuclein: Helping to define the relationship between oligomers, protofibrils, and filaments (2005) J Biol Chem, 280, pp. 9678-9690
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (2002) Nature, 416, pp. 507-511
Pellistri, F., Bucciantini, M., Relini, A., Nosi, D., Gliozzi, A., Nonspecific interaction of prefibrillar amyloid aggregates with glutamatergic receptors results in Ca2+ increase in primary neuronal cells (2008) J Biol Chem, 283, pp. 29950-29960
Lashuel, H.A., Membrane permeabilization: A common mechanism in protein-misfolding diseases (2005) Sci Aging Knowledge Environ 2005, pp. e28
Conway, K.A., Lee, S.J., Rochet, J.C., Ding, T.T., Williamson, R.E., Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy (2000) Proc Natl Acad Sci U S A, 97, pp. 571-576
Conway, K.A., Rochet, J.C., Bieganski, R.M., Lansbury Jr, P.T., Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct (2001) Science, 294, pp. 1346-1349
Lashuel, H.A., Hartley, D., Petre, B.M., Walz, T., Lansbury, P.T., Neurodegenerative disease - Amyloid pores from pathogenic mutations (2002) Nature, 418, p. 291
Herrera, F.E., Chesi, A., Paleologou, K.E., Schmid, A., Munoz, A., (2008) Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region, ONE 3, pp. e3394. , PLoS
Bennett, E.J., Bence, N.F., Jayakumar, R., Kopito, R.R., Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation (2005) Mol Cell, 17, pp. 351-365
Lee, J.C., Gray, H.B., Winkler, J.R., Copper(II) binding to alpha-synuclein, the Parkinson's protein (2008) J Am Chem Soc, 130, pp. 6898-6899
Vijay-Kumar, S., Bugg, C.E., Cook, W.J., Structure of ubiquitin refined at 1.8 Å reolution (1987) J Mol Biol, 194, pp. 531-544
Tan, J.M., Wong, E.S., Kirkpatrick, D.S., Pletnikova, O., Ko, H.S., Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases (2008) Hum Mol Genet, 17, pp. 431-439
Maryon, E.B., Molloy, S.A., Zimnicka, A.M., Kaplan, J.H., Copper entry into human cells: Progress and unanswered questions (2007) Biometals, 20, pp. 355-364
Lee, J., Petris, M.J., Thiele, D.J., Characterization of mouse embryonic cells deficient in the Ctr1 high affinity copper transporter. Identification of a Ctr1-independent copper transport system (2002) J Biol Chem, 277, pp. 40253-40259
Moriya, M., Ho, Y.H., Grana, A., Nguyen, L., Alvarez, A., Copper is taken up efficiently from albumin and alpha2-macroglobulin by cultured human cells by more than one mechanism (2008) Am J Physiol Cell Physiol, 295, pp. C708-C721
Pufahl, R.A., Singer, C.P., Peariso, K.L., Lin, S.-J., Schmidt, P.J., Metal ion chaperone function of the soluble Cu(I) receptor Atx1 (1997) Science, 278, pp. 853-856
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Copper-triggered aggregation of ubiquitin
Neurodegenerative disorders share common features comprising aggregation of misfolded proteins, failure of the ubiquitin-proteasome system, and increased levels of metal ions in the brain. Protein aggregates within affected cells often contain ubiquitin, however no report has focused on the aggregation propensity of this protein. Recently it was shown that copper, differently from zinc, nickel, aluminum, or cadmium, compromises ubiquitin stability and binds to the N-terminus with 0.1 micromolar affinity. This paper addresses the role of copper upon ubiquitin aggregation. In water, incubation with Cu(II) leads to formation of spherical particles that can progress from dimers to larger conglomerates. These spherical oligomers are SDS-resistant and are destroyed upon Cu(II) chelation or reduction to Cu(I). In water/trifluoroethanol (80:20, v/v), a mimic of the local decrease in dielectric constant experienced in proximity to a membrane surface, ubiquitin incubation with Cu(II) causes time-dependent changes in circular dichroism and Fourier-transform infrared spectra, indicative of increasing beta-sheet content. Analysis by atomic force and transmission electron microscopy reveals, in the given order, formation of spherical particles consistent with the size of early oligomers detected by gel electrophoresis, clustering of these particles in straight and curved chains, formation of ring structures, growth of trigonal branches from the rings, coalescence of the trigonal branched structures in a network. Notably, none of these ubiquitin aggregates was positive to tests for amyloid and Cu(II) chelation or reduction produced aggregate disassembly. The early formed Cu(II)-stabilized spherical oligomers, when reconstituted in 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) liposomes and in POPC planar bilayers, form annular and pore-like structures, respectively, which are common to several neurodegenerative disorders including Parkinson's, Alzheimer's, amyotrophic lateral sclerosis, and prion diseases, and have been proposed to be the primary toxic species. Susceptibility to aggregation of ubiquitin, as it emerges from the present study, may represent a potential risk factor for disease onset or progression while cells attempt to tag and process toxic substrates.
Neurodegenerative disorders share common features comprising aggregation of misfolded proteins, failure of the ubiquitin-proteasome system, and increased levels of metal ions in the brain. Protein aggregates within affected cells often contain ubiquitin, however no report has focused on the aggregation propensity of this protein. Recently it was shown that copper, differently from zinc, nickel, aluminum, or cadmium, compromises ubiquitin stability and binds to the N-terminus with 0.1 micromolar affinity. This paper addresses the role of copper upon ubiquitin aggregation. In water, incubation with Cu(II) leads to formation of spherical particles that can progress from dimers to larger conglomerates. These spherical oligomers are SDS-resistant and are destroyed upon Cu(II) chelation or reduction to Cu(I). In water/trifluoroethanol (80:20, v/v), a mimic of the local decrease in dielectric constant experienced in proximity to a membrane surface, ubiquitin incubation with Cu(II) causes time-dependent changes in circular dichroism and Fourier-transform infrared spectra, indicative of increasing beta-sheet content. Analysis by atomic force and transmission electron microscopy reveals, in the given order, formation of spherical particles consistent with the size of early oligomers detected by gel electrophoresis, clustering of these particles in straight and curved chains, formation of ring structures, growth of trigonal branches from the rings, coalescence of the trigonal branched structures in a network. Notably, none of these ubiquitin aggregates was positive to tests for amyloid and Cu(II) chelation or reduction produced aggregate disassembly. The early formed Cu(II)-stabilized spherical oligomers, when reconstituted in 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) liposomes and in POPC planar bilayers, form annular and pore-like structures, respectively, which are common to several neurodegenerative disorders including Parkinson's, Alzheimer's, amyotrophic lateral sclerosis, and prion diseases, and have been proposed to be the primary toxic species. Susceptibility to aggregation of ubiquitin, as it emerges from the present study, may represent a potential risk factor for disease onset or progression while cells attempt to tag and process toxic substrates.
Copper-triggered aggregation of ubiquitin
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Copper-triggered aggregation of ubiquitin
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Accardo A, Tesauro D, Mangiapia G, Pedone C, Morelli G
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Ronga L, Palladino P, Tizzano B, Marasco D, Benedetti E, Ragone R, Rossi F
* Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective (454 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Impact Factor: 1.801
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Esposito L, Pedone C, Vitagliano L
* Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation (727 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2006 Sep 1; 103(31): 11533-11538.
Impact Factor: 9.643
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Merlino A, Esposito L, Vitagliano L
* Polyglutamine Repeats And Beta-Helix Structure: Molecular Dynamics Study (504 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Jun 1; 63(4): 918-927.
Impact Factor: 3.73
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Tizzano B, Palladino P, De Capua A, Marasco D, Rossi F, Benedetti E, Pedone C, Ragone R, Ruvo M
* The Human Prion Protein Alpha2 Helix: A Thermodynamic Study Of Its Conformational Preferences (504 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2005 Apr 1; 59(1): 72-79.
Impact Factor: 4.684
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Merlino A, Ceruso MA, Vitagliano L, Mazzarella L
* Open interface and large quaternary structure movements in 3D domain swapped proteins: Insights from molecular dynamics simulations of the C-terminal swapped dimer of ribonuclease (602 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2005 Mar; 88(3): 2003-2012.
Impact Factor: 4.507
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Merlino A, Graziano G, Mazzarella L
* Structural And Dynamic Effects Of Alpha-Helix Deletion In Sso7d: Implications For Protein Thermal Stability (375 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2004 Dec 1; 57(4): 692-701.
Impact Factor: 4.429
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Langella E, Improta R, Barone V
* Checking the pH-induced conformational transition of prion protein by molecular dynamics simulations: Effect of protonation of histidine residues (427 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2004 Dec; 87(6): 3623-3632.
Impact Factor: 4.585
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Merlino A, Vitagliano L, Ceruso MA, Mazzarella L
* Subtle functional collective motions in pancreatic-like ribonucleases: From ribonuclease A to angiogenin (386 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2003 Oct 1; 53(1): 101-110.
Impact Factor: 4.313
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Merlino A, Vitagliano L, Ceruso M, Di Nola A, Mazzarella L
* Global and local motions in ribonuclease A: A molecular dynamics study (411 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2002 Nov 15; 65(4): 274-283.
Impact Factor: 2.372
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Grasso D, Milardi D, La Rosa C, Impellizzeri G, Pappalardo G
* The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: A DSC study (276 views)
Thermochim Acta (ISSN: 0040-6031), 2002 Jul 15; 390(1-2): 73-78.
Impact Factor: 0.974
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* Diphenylalanine Motif Drives Self-Assembling in Hybrid PNA-Peptide Conjugates (15 views)
Chemistry (ISSN: 0947-6539linking, 1521-3765electronic), 2021 Oct 13; 27(57): 14307-14316.
Impact Factor: 5.236
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Gaglione R, Smaldone G, Di Girolamo R, Piccoli R, Pedone E, Arciello A
* Cell milieu significantly affects the fate of AApoAI amyloidogenic variants: predestination or serendipity? (433 views)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 1570-9639print), 2017 Nov 23; 1862(3): 377-384.
Impact Factor: 4.28
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Galdiero S, Falanga A, Morelli G, Galdiero M
* gH625: A milestone in understanding the many roles of membranotropic peptides (524 views)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2015 Jan; 1848(PA): 16-25.
Impact Factor: 5.158
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GrassoG, Satriano C, Milardi D
* A neglected modulator of insulin-degrading enzyme activity and conformation: The pH (406 views)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2015; 203-204: 33-40.
Impact Factor: 2.363
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Tomasello MF, Sinopoli A, Attanasio F, Giuffrida ML, Campagna T, Milardi D, Pappalardo G
* Molecular and cytotoxic properties of hIAPP17-29 and rIAPP17-29 fragments: A comparative study with the respective full-length parent polypeptides (1075 views)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 0223-5234linking), 2014 Jun 23; 81: 442-455.
Impact Factor: 3.447
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Grasso GI, Arena G, Bellia F, Rizzarelli E, Vecchio G
* Copper(II)-chelating homocarnosine glycoconjugate as a new multifunctional compound (560 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2014 Feb; 131: 56-63.
Impact Factor: 3.444
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GrassoG, Magrì A, Bellia F, Pietropaolo A, La Mendola D, Rizzarelli E
* The Copper (ii) And Zinc (ii) Coordination Mode Of Hexxh And Hxxeh Motif In Small Peptides: The Role Of Carboxylate Location And Hydrogen Bonding Network (526 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2014 Jan; 130(1): 92-102.
Impact Factor: 3.444
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Bellia F, Oliveri V, Rizzarelli E, Vecchio G
* New derivative of carnosine for nanoparticle assemblies (458 views)
Eur J Med Chem (ISSN: 1768-3254, 0223-5234, 1768-3254electronic), 2013 Dec; 70: 225-232.
Impact Factor: 3.432
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Pica A, Merlino A, Buell AK, Knowles TJ, Pizzo E, D'Alessio G, Sica F, Mazzarella L
* Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase (876 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2013 Oct; 69: 2116-2123.
Impact Factor: 7.232
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Galdiero S, Falanga A, Cantisani M, Vitiello M, Morelli G, Galdiero M
* Peptide-Lipid Interactions: Experiments and Applications (1013 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2013 Sep; 14(9): 18758-18789.
Impact Factor: 2.339
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Attanasio F, Bonaccorso C, Bellia F, Cataldo S, Fortuna CG, Musumarra G, Pignataro B, Rizzarelli E
* (E)-2-Cyano-3-(5 Alpha-Piperidin-1-Yl-2, 2 Alpha-Bithien-5-Yl)acrylic Acid: A Fluorescent Probe For Detecting Prefibrillar Oligomers (449 views)
European Journal Of Organic Chemistry (ISSN: 1434-193x), 2013 Jun; (18): 3635-3639.
Impact Factor: 3.154
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De Simonea A, Stanzione F, Marasco D, Vitagliano L, Esposito L
* The Intrinsic Stability Of The Human Prion Beta-Sheet Region Investigated By Molecular Dynamics (608 views)
Journal Of Biomolecular Structure & Dynamics, 2013 May 1; 31(5): 441-452.
Impact Factor: 2.983
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Galdiero S, Falanga A, Tarallo R, Russo L, Galdiero E, Cantisani M, Morelli G, Galdiero M
* Peptide inhibitors against herpes simplex virus infections (888 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2013 Mar; 19(3): 148-158.
Impact Factor: 1.862
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Sciacca MFM, Milardi D, Messina GML, Marletta G, Brender JR, Ramamoorthy A, La Rosa C
* Cations as switches of amyloid-mediated membrane disruption mechanisms: Calcium and IAPP (604 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2013 Jan 8; 104(1): 173-184.
Impact Factor: 3.832
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Causa F, Della Moglie R, Iaccino E, Mimmi S, Marasco D, Scognamiglio PL, Battista E, Palmieri C, Cosenza C, Sanguigno L, Quinto I, Scala G, Netti PA
* Evolutionary screening and adsorption behavior of engineered M13 bacteriophage and derived dodecapeptide for selective decoration of gold interfaces (412 views)
J Colloid Interface Sci (ISSN: 0021-9797, 1095-7103electronic, 0021-9797linking), 2013 Jan 1; 389(1): 220-229.
Impact Factor: 1.646
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Pannuzzo M, Milardi D, Raudino A, Karttunen M, La Rosa C
* Analytical model and multiscale simulations of Aβ peptide aggregation in lipid membranes: Towards a unifying description of conformational transitions, oligomerization and membrane damage (728 views)
Phys Chem Chem Phys (ISSN: 1463-9076, 1463-3907, 1463-9084electronic), 2013; 15(23): 8940-8951.
Impact Factor: 4.198
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Attanasio F, De Bona P, Cataldo S, Sciacca MFM, Milardi D, Pignataro B, Pappalardo G
* Copper(II) and zinc(II) dependent effects on A beta 42 aggregation: a CD, Th-T and SFM study (456 views)
New J Chem (ISSN: 1144-0546), 2013; 37(4): 1206-1215.
Impact Factor: 3.159
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Pannuzzo M, Raudino A, Milardi D, La Rosa C, Karttunen M
* α-Helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes (741 views)
Sci Rep (ISSN: 2045-2322, 2045-2322electronic, 2045-2322linking), 2013; 3: N/D-N/D.
Impact Factor: 5.078
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Roviello GN, Mottola A, Musumeci D, Bucci EM, Pedone C
* Synthesis and aggregation properties of a novel enzymatically resistant nucleoamino acid (423 views)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2012 Oct; 43(4): 1465-1470.
Impact Factor: 3.914
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Stanzione F, De Simone A, Esposito L, Vitagliano L
* Dynamical Properties of Steric Zipper Polymorphs Formed by a IAPP-Derived Peptide (461 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2012 Sep; 19(8): 846-851.
Impact Factor: 1.994
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Jószai V, Turi I, Kállay C, Pappalardo G, Di Natale G, Rizzarelli E, Sóvágó I
* Mixed metal copper(II)-nickel(II) and copper(II)-zinc(II) complexes of multihistidine peptide fragments of human prion protein (481 views)
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2012 Jul; 112: 17-24.
Impact Factor: 3.197
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Castellano I, Merlino A
* γ-glutamyltranspeptidases: Sequence, structure, biochemical properties, and biotechnological applications (422 views)
Cell Mol Life Sci (ISSN: 1420-682x), 2012; 69(20): 3381-3394.
Impact Factor: 5.615
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D'Errico G, Ercole C, Lista M, Pizzo E, Falanga A, Galdiero S, Spadaccini R, Picone D
* Enforcing the positive charge of N-termini enhances membrane interaction and antitumor activity of bovine seminal ribonuclease (478 views)
Bba-Gen Subjects (ISSN: 0005-2736, 0006-3002, 0925-4439), 2011 Dec; 1808(12): 3007-3015.
Impact Factor: 3.99
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Accardo A, Morisco A, Gianolio E, Tesauro D, Mangiapia G, Radulescu A, Brandt A, Morelli G
* Nanoparticles containing octreotide peptides and gadolinium complexes for MRI applications (504 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2011 Feb; 17(2): 154-162.
Impact Factor: 1.799
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Milardi D, Sciacca MFM, Pappalardo M, Grasso DM, La Rosa C
* The Role Of Aromatic Side-Chains In Amyloid Growth And Membrane Interaction Of The Islet Amyloid Polypeptide Fragment Lanflvh (457 views)
Eur Biophys J, 2011 Jan; 40(1): 1-12.
Impact Factor: 3.832
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Pedone E, Limauro D, D'Ambrosio K, De Simone G, Bartolucci S
* Multiple catalytically active thioredoxin folds: a winning strategy for many functions (725 views)
Cell Mol Life Sci Cellular And Molecular Life Sciences (ISSN: 1420-682x), 2010 Nov; 67(22): 3797-3814.
Impact Factor: 7.047
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Turi I, Kállay C, Szikszai D, Pappalardo G, Di Natale G, De Bona P, Rizzarelli E, Sóvágó I
* Nickel(II) complexes of the multihistidine peptide fragments of human prion protein (480 views)
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2010 Sep; 104(8): 885-891.
Impact Factor: 3.317
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Satriano C, Messina GM, Marino C, Aiello I, Conte E, La Mendola D, Distefano DA, D'Alessandro F, Pappalardo G, Impellizzeri G
* Surface immobilization of fibronectin-derived PHSRN peptide on functionalized polymer films - Effects on fibroblast spreading (534 views)
J Colloid Interface Sci (ISSN: 1095-7103electronic, 0021-9797linking), 2010 Jan 15; 341(2): 232-239.
Impact Factor: 3.068
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Vitagliano L, Stanzione F, De Simone A, Esposito L
* Dynamics and Stability of Amyloid-Like Steric Zipper Assemblies with Hydrophobic Dry Interfaces (549 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1161-1171.
Impact Factor: 2.605
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Palladino P, Ronga L, Benedetti E, Rossi F, Ragone R
* Peptide Fragment Approach to Prion Misfolding: The Alpha-2 Domain (401 views)
Int J Pept Res Ther (ISSN: 1573-3149, 0929-5666), 2009 Sep; 15(3): 165-176.
Impact Factor: 0.869
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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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De Bona P, Giuffrida ML, Caraci F, Copani A, Pignataro B, Attanasio F, Cataldo S, Pappalardo G, Rizzarelli E
* Design And Synthesis Of New Trehalose-Conjugated Pentapeptides As Inhibitors Of Abeta (1-42) Fibrillogenesis And Toxicity (688 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 220-228.
Impact Factor: 1.807
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Morisco A, Accardo A, Gianolio E, Tesauro D, Benedetti E, Morelli G
* Micelles derivatized with octreotide as potential target-selective contrast agents in MRI (417 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 242-250.
Impact Factor: 1.807
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Ruggiero A, Tizzano B, Pedone E, Pedone C, Wilmanns M, Berisio R
* Crystal Structure of the Resuscitation-Promoting Factor (Delta DUF)RpfB from M. tuberculosis (571 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009 Jan 9; 385(1): 153-162.
Impact Factor: 3.871
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Vitagliano L, Esposito L, Pedone C, De Simone A
* Stability of single sheet GNNQQNY aggregates analyzed by replica exchange molecular dynamics: antiparallel versus parallel association (626 views)
Biochem Biophys Res Commun (ISSN: 1090-2104, 0006-291x, 1090-2104electronic), 2008 Dec 26; 377(4): 1036-1041.
Impact Factor: 2.648
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La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
* Prion proteins leading to neurodegeneration (420 views)
Current Alzheimer Research (ISSN: 1567-2050), 2008 Dec; 5(6): 579-590.
Impact Factor: 4.132
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Di Natale G, Damante CA, Nagy Z, Osz K, Pappalardo G, Rizzarelli E, Sóvágó I
* Copper(II) binding to two novel histidine-containing model hexapeptides: evidence for a metal ion driven turn conformation (423 views)
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2008 Nov; 102(11): 2012-2019.
Impact Factor: 3.133
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Ronga L, Palladino P, Saviano G, Tancredi T, Benedetti E, Ragone R, Rossi F
* Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein α2-helical 180-195 segment and comparison with full-length α2-helix-derived peptides (411 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2008; 14(10): 1096-1102.
Impact Factor: 1.654
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Vaccaro M, Accardo A, D'Errico G, Schillen K, Radulescu A, Tesauro D, Morelli G, Paduano L
* Peptides and gd complexes containing colloidal assemblies as tumor-specific contrast agents in MRI: Physicochemical characterization (399 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2007 Sep; 93(5): 1736-1746.
Impact Factor: 4.627
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Amorini AM, Bellia F, Di Pietro V, Giardina B, La Mendola D, Lazzarino G, Sortino S, Tavazzi B, Rizzarelli E, Vecchio G
* Synthesis And Antioxidant Activity Of New Homocarnosine Beta-Cyclodextrin Conjugates (370 views)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 1768-3254electronic), 2007 Jul; 42(7): 910-920.
Impact Factor: 2.301
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Giuffrida ML, Grasso G, Ruvo M, Pedone C, Saporito A, Marasco D, Pignataro B, Cascio C, Copani A, Rizzarelli E
* Abeta(25-35) And Its C- And/Or N-Blocked Derivatives: Copper Driven Structural Features And Neurotoxicity (613 views)
Journal Of Neuroscience Research (ISSN: 0360-4012), 2007 Feb 15; 85(3): 623-633.
Impact Factor: 3.268
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Ronga L, Langella E, Palladino P, Marasco D, Tizzano B, Saviano M, Pedone C, Improta R, Ruvo M
* Does Tetracycline Bind Helix 2 Of Prion? An Integrated Spectroscopical And Computational Study Of The Interaction Between The Antibiotic And Alpha Helix 2 Human Prion Protein Fragments (512 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Feb 15; 66(3): 707-715.
Impact Factor: 3.354
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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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Ronga L, Palladino P, Costantini S, Facchiano A, Ruvo M, Benedetti E, Ragone R, Rossi F
* Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides (553 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2007 Feb; 8(1): 83-90.
Impact Factor: 3.259
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Arena G, Deretzis I, Forte G, Giannazzo F, La Magna A, Lombardo G, Raineri V, Sgarlata C, Spoto G
* Electron transport properties of calix[4]arene based systems in a metal-molecule-metal junction (334 views)
New J Chem (ISSN: 1144-0546), 2007; 31(5): 756-761.
Impact Factor: 2.651
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Accardo A, Tesauro D, Mangiapia G, Pedone C, Morelli G
* Nanostructures by self-assembling peptide amphiphile as potential selective drug carriers (429 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2007; 88(2): 115-121.
Impact Factor: 2.389
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Crisma M, Saviano M, Moretto A, Broxterman QB, Kaptein B, Toniolo C
* Peptide α/310-helix dimorphism in the crystal state (299 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2007; 129(50): 15471-15473.
Impact Factor: 7.885
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Ronga L, Palladino P, Tizzano B, Marasco D, Benedetti E, Ragone R, Rossi F
* Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective (454 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Impact Factor: 1.801
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Esposito L, Pedone C, Vitagliano L
* Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation (727 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2006 Sep 1; 103(31): 11533-11538.
Impact Factor: 9.643
View Export to BibTeX Export to EndNote
Merlino A, Esposito L, Vitagliano L
* Polyglutamine Repeats And Beta-Helix Structure: Molecular Dynamics Study (504 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Jun 1; 63(4): 918-927.
Impact Factor: 3.73
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Tizzano B, Palladino P, De Capua A, Marasco D, Rossi F, Benedetti E, Pedone C, Ragone R, Ruvo M
* The Human Prion Protein Alpha2 Helix: A Thermodynamic Study Of Its Conformational Preferences (504 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2005 Apr 1; 59(1): 72-79.
Impact Factor: 4.684
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Merlino A, Ceruso MA, Vitagliano L, Mazzarella L
* Open interface and large quaternary structure movements in 3D domain swapped proteins: Insights from molecular dynamics simulations of the C-terminal swapped dimer of ribonuclease (602 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2005 Mar; 88(3): 2003-2012.
Impact Factor: 4.507
View Export to BibTeX Export to EndNote
Merlino A, Graziano G, Mazzarella L
* Structural And Dynamic Effects Of Alpha-Helix Deletion In Sso7d: Implications For Protein Thermal Stability (375 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2004 Dec 1; 57(4): 692-701.
Impact Factor: 4.429
View Export to BibTeX Export to EndNote
Langella E, Improta R, Barone V
* Checking the pH-induced conformational transition of prion protein by molecular dynamics simulations: Effect of protonation of histidine residues (427 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2004 Dec; 87(6): 3623-3632.
Impact Factor: 4.585
View Export to BibTeX Export to EndNote
Merlino A, Vitagliano L, Ceruso MA, Mazzarella L
* Subtle functional collective motions in pancreatic-like ribonucleases: From ribonuclease A to angiogenin (386 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2003 Oct 1; 53(1): 101-110.
Impact Factor: 4.313
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Merlino A, Vitagliano L, Ceruso M, Di Nola A, Mazzarella L
* Global and local motions in ribonuclease A: A molecular dynamics study (411 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2002 Nov 15; 65(4): 274-283.
Impact Factor: 2.372
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Grasso D, Milardi D, La Rosa C, Impellizzeri G, Pappalardo G
* The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: A DSC study (276 views)
Thermochim Acta (ISSN: 0040-6031), 2002 Jul 15; 390(1-2): 73-78.
Impact Factor: 0.974
View Export to BibTeX Export to EndNote
57 Records (56 excluding Abstracts).
Total impact factor: 204.032 (198.954 excluding Abstracts).
Total 5 year impact factor: 207.522 (202.444 excluding Abstracts).
Total impact factor: 204.032 (198.954 excluding Abstracts).
Total 5 year impact factor: 207.522 (202.444 excluding Abstracts).
533 views. Last view on Monday 06 March 2023, 19:18:30
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