Evolutionary implications of metal binding features in different species' prion protein: an inorganic point of view (456 views)
Biomolecules (ISSN: 2218-273x), 2014 May 23; 4(2): 546-565.
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*** IBB - CNR ***
Department of Pharmacy, University of Pisa, Via Bonanno Pisano 6, Pisa 56126, Italy. lamendola@farm.unipi.it.
Institute of Biostructures and Bioimages, National Council of Research (CNR), Viale A. Doria 6, Catania 95125, Italy. erizzarelli@unict.it.
References:
Not available.
Biomolecules (ISSN: 2218-273x), 2014 May 23; 4(2): 546-565.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.095, 5-year impact factor: 2.638
Url: Not available.
Keywords: Not available.
Affiliations:
*** IBB - CNR ***
Department of Pharmacy, University of Pisa, Via Bonanno Pisano 6, Pisa 56126, Italy. lamendola@farm.unipi.it.
Institute of Biostructures and Bioimages, National Council of Research (CNR), Viale A. Doria 6, Catania 95125, Italy. erizzarelli@unict.it.
References:
Not available.
Evolutionary implications of metal binding features in different species' prion protein: an inorganic point of view
Prion disorders are a group of fatal neurodegenerative conditions of mammals. The key molecular event in the pathogenesis of such diseases is the conformational conversion of prion protein, PrPC, into a misfolded form rich in beta-sheet structure, PrPSc, but the detailed mechanistic aspects of prion protein conversion remain enigmatic. There is uncertainty on the precise physiological function of PrPC in healthy individuals. Several evidences support the notion of its role in copper homeostasis. PrPC binds Cu2+ mainly through a domain composed by four to five repeats of eight amino acids. In addition to mammals, PrP homologues have also been identified in birds, reptiles, amphibians and fish. The globular domain of protein is retained in the different species, suggesting that the protein carries out an essential common function. However, the comparison of amino acid sequences indicates that prion protein has evolved differently in each vertebrate class. The primary sequences are strongly conserved in each group, but these exhibit a low similarity with those of mammals. The N-terminal domain of different prions shows tandem amino acid repeats with an increasing amount of histidine residues going from amphibians to mammals. The difference in the sequence affects the number of copper binding sites, the affinity and the coordination environment of metal ions, suggesting that the involvement of prion in metal homeostasis may be a specific characteristic of mammalian prion protein. In this review, we describe the similarities and the differences in the metal binding of different species' prion protein, as revealed by studies carried out on the entire protein and related peptide fragments.
Prion disorders are a group of fatal neurodegenerative conditions of mammals. The key molecular event in the pathogenesis of such diseases is the conformational conversion of prion protein, PrPC, into a misfolded form rich in beta-sheet structure, PrPSc, but the detailed mechanistic aspects of prion protein conversion remain enigmatic. There is uncertainty on the precise physiological function of PrPC in healthy individuals. Several evidences support the notion of its role in copper homeostasis. PrPC binds Cu2+ mainly through a domain composed by four to five repeats of eight amino acids. In addition to mammals, PrP homologues have also been identified in birds, reptiles, amphibians and fish. The globular domain of protein is retained in the different species, suggesting that the protein carries out an essential common function. However, the comparison of amino acid sequences indicates that prion protein has evolved differently in each vertebrate class. The primary sequences are strongly conserved in each group, but these exhibit a low similarity with those of mammals. The N-terminal domain of different prions shows tandem amino acid repeats with an increasing amount of histidine residues going from amphibians to mammals. The difference in the sequence affects the number of copper binding sites, the affinity and the coordination environment of metal ions, suggesting that the involvement of prion in metal homeostasis may be a specific characteristic of mammalian prion protein. In this review, we describe the similarities and the differences in the metal binding of different species' prion protein, as revealed by studies carried out on the entire protein and related peptide fragments.
Evolutionary implications of metal binding features in different species' prion protein: an inorganic point of view
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Evolutionary implications of metal binding features in different species' prion protein: an inorganic point of view
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* Evolutionary screening and adsorption behavior of engineered M13 bacteriophage and derived dodecapeptide for selective decoration of gold interfaces (614 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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Damante CA, Ösz K, Nagy Z, Grasso G, Pappalardo G, Rizzarelli E, Sóvágó I
* Zn2+'s ability to alter the distribution of Cu2+ among the available binding sites of A beta(1-16)-polyethylenglycol-ylated peptide: Implications in Alzheimer's disease (740 views)
Inorg Chem (ISSN: 0020-1669, 1520-510x, 1520-510xelectronic), 2011 Jun 20; 50(12): 5342-5350.
Impact Factor: 4.601
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Pirone L, Correale S, De Paola I, Zaccaro L, De Simone G, Vitagliano L, Pedone E, Di Gaetano S
* Design, synthesis and characterization of a peptide able to bind proteins of the KCTD family: implications for KCTD - cullin 3 recognition (572 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2011 May; 17(5): 373-376.
Impact Factor: 1.799
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Grasso G, Pietropaolo A, Spoto G, Pappalardo G, Tundo GR, Ciaccio C, Coletta M, Rizzarelli E
* Copper(I) and Copper(II) Inhibit A beta Peptides Proteolysis by Insulin-Degrading Enzyme Differently: Implications for Metallostasis Alteration in Alzheimer's Disease (728 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Feb 25; 17(9): 2752-2762.
Impact Factor: 5.925
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Varriale S, Merlino A, Coscia MR, Mazzarella L, Oreste U
* An evolutionary conserved motif is responsible for Immunoglobulin heavy chain packing in the B cell membrane (693 views)
Molecular Phylogenetics And Evolution (ISSN: 1055-7903), 2010 Dec; 57(3): 1238-1244.
Impact Factor: 3.889
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Coppola D, Giordano D, Vergara A, Mazzarella L, Di Prisco G, Verde C, Russo R
* The hemoglobins of sub-Antarctic fishes of the suborder Notothenioidei (981 views)
Polar Science (ISSN: 1873-9652), 2010 Sep; 4(2): 295-308.
Impact Factor: 31.477
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Kelly SE, Di Benedetto A, Greco A, Howard CM, Sollars VE, Primerano DA, Valluri JV, Claudio PP
* Rapid Selection and Proliferation of CD133(+) Cells from Cancer Cell Lines: Chemotherapeutic Implications (667 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2010 Apr 8; 5(4): N/D-N/D.
Impact Factor: 4.411
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Esposito C, Carullo C, Pedone E, Graziano G, Del Vecchio P, Berisio R
* Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: Implications for bacterial agglutination (670 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 0014-5793linking), 2010 Mar 19; 584(6): 1091-1096.
Impact Factor: 3.601
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Attanasio F, Cataldo S, Fisichella S, Nicoletti S, Nicoletti VG, Pignataro B, Savarino A, Rizzarelli E
* Protective effects of L- and D-carnosine on alpha-crystallin amyloid fibril formation: implications for cataract disease (584 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2009 Jul 14; 48(27): 6522-6531.
Impact Factor: 3.226
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Arpaia P, Clemente F, Manna C, Montenero G
* Automatic modeling based on cultural programming for osseointegration diagnosis (431 views)
Vols 1 3i2mtc (ISSN: 1091-5281), 2009; N/D: 1278-1283.
Impact Factor: 0
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Verde C, Vergara A, Mazzarella L, Di Prisco G
* The Hemoglobins of Fishes Living at Polar Latitudes - Current Knowledge on Structural Adaptations in a Changing Environment (539 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2008 Dec; 9(6): 578-590.
Impact Factor: 3.011
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Sciacca MFM, Pappalardo M, Milardi D, Grasso DM, La Rosa C
* Calcium-Activated Membrane Interaction Of The Islet Amyloid Polypeptide: Implications In The Pathogenesis Of Type Ii Diabetes Mellitus (1326 views)
Arch Biochem Biophys, 2008 Sep 15; 65(1-2): 291-298.
Impact Factor: 3.043
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Doti N, Marasco D, Sabatella M, Monti SM, Dathan N, Viparelli F, Cassese A, Miele C, Pedone C, Ruvo M
* An analysis of deletion mutants of the PLD1 D4 domain defines short regions within the PLD1 interacting with PED/PEA15: implications for the development of peptides-specific antagonist (553 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2008 Sep; 14(8): N/D-N/D.
Impact Factor: 1.654
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Verde C, Vergara A, Giordano D, Mazzarella L, Di Prisco G
* The Root effect - a structural and evolutionary perspective (338 views)
Antarctic Science (ISSN: 0954-1020), 2007 Jun; 19(2): 271-278.
Impact Factor: 1.265
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Di Pietro C, Piro S, Tabbì G, Ragusa M, Di Pietro V, Zimmitti V, Cuda F, Anello M, Consoli U, Salinaro ET, Caruso M, Vancheri C, Crimi N, Sabini MG, Cirrone GA, Raffaele L, Privitera G, Pulvirenti A, Giugno R, Ferro A, Cuttone G, Lo Nigro S, Purrello R, Purrello F, Purrello M
* Cellular and molecular effects of protons: Apoptosis induction and potential implications for cancer therapy (739 views)
Apoptosis (ISSN: 1360-8185), 2006 Jan; 11(1): 57-66.
Impact Factor: 3.421
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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 (574 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2004 Dec 1; 57(4): 692-701.
Impact Factor: 4.429
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Leone M, Di Lello P, Ohlenschläger O, Pedone E, Bartolucci S, Rossi M, Di Blasio B, Pedone C, Saviano M, Isernia C, Fattorusso R
* Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: A molecular analysis of its reduced thermal stability (1285 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2004 May 25; 43(20): 6043-6058.
Impact Factor: 4.008
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Berisio R, Granata V, Vitagliano L, Zagari A
* Characterization of Collagen-Like Heterotrimers: Implications for Triple-Helix Stability (1205 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 682-688.
Impact Factor: 2.863
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Piscione F, De Luca G, Perrone-filardi P, Prastaro M, Pace L, Galasso G, Marrazzo G, Salvatore M, Chiariello M
* Relationship between contractile reserve, TI-201 uptake, and collateral angiographic circulation in collateral-dependent myocardium: Implications regarding the evaluation of myocardial viability (817 views)
J Nucl Cardiol (ISSN: 1071-3581, 1532-6551, 1532-6551electronic), 2003 Jan; 10(1): 17-27.
Impact Factor: 1.629
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Vitagliano L, Berisio R, Mastrangelo A, Mazzarella L, Zagari A
* Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability (1571 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2001 Dec; 10(12): 2627-2632.
Impact Factor: 3.472
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Menchise V, Corbier C, Didierjean C, Saviano M, Benedetti E, Jacquot JP, Aubry A
* Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism (1045 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2001 Oct 1; 359(1): 65-75.
Impact Factor: 4.326
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Petretta M, Acampa W, Cuocolo A
* Myocardial viability assessment in regions of left ventricular dysfunction. Part I: Radionuclide imaging and clinical implications (504 views)
Nuclear Medicine Communications (ISSN: 0143-3636, 1473-5628), 2001 Jun; 22(6): 607-611.
Impact Factor: 1.19
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Berisio R, Vitagliano L, Mazzarella L, Zagari A
Crystal Structure Of A Collagen-Like Polypeptide With Repeating Sequence Pro-Hyp-Gly At 1. 4 Ang Resolution: Implications For Collagen Hydration (652 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2000; 56(1): 8-13.
Impact Factor: 2.405
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Reynolds JC, Del Vecchio S, Sakahara H, Lora ME, Carrasquillo JA, Neumann RD, Larson SM
ANTI-MURINE ANTIBODY RESPONSE TO MOUSE MONOCLONAL ANTIBODIES CLINICAL FINDINGS AND IMPLICATIONS (1111 views)
Nucl Med Biol (ISSN: 0969-8051, 0883-2897), 1989; 16(2): 121-125.
Impact Factor: 1.042
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40 Records (38 excluding Abstracts).
Total impact factor: 163.824 (157.759 excluding Abstracts).
Total 5 year impact factor: 159.399 (153.007 excluding Abstracts).
Total impact factor: 163.824 (157.759 excluding Abstracts).
Total 5 year impact factor: 159.399 (153.007 excluding Abstracts).
456 views. Last view on Saturday 11 January 2025, 10:36:19
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