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A new RNase sheds light on the RNase/angiogenin subfamily from zebrafish (108 visite)

Pizzo E, Merlino A, Turano M, Russo Krauss I, Coscia F, Zanfardino A, Varcamonti M, Furia A, Giancola C, Mazzarella L, Sica F, D'Alessio G

Biochem J (ISSN: 1470-8728electronic, 0264-6021linking, 0264-6021print), 2011 Jan 15; 433(2): 345-355.

Tipo di articolo: Journal Article, Research Support, Non-U. S. Gov'T,

Impact factor: 4.897

Impact factor a 5 anni: 4.693


Parole chiave: Angiogenin, Bactericidal Activity, Rnase, Vertebrate, Zebrafish (zf) (danio Rerio), Enzyme, Ribonuclease, Unclassified Drug, Article, Biological Activity, Controlled Study, Drug Structure, Human, Nonhuman, Priority Journal, Thermodynamics, Zebra Fish, Amino Acid Sequence, Animals, Cells, Cultured, Gene Expression Regulation, Developmental, Enzymologic, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Pancreatic, Sequence Alignment, Pancreatic Chemistry, Genetics, Metabolism, Ribonucleases Chemistry, Embryology, Genetics Metabolism, Pancreatic Chemistry Genetics Metabolism, Ribonucleases Chemistry Genetics Metabolism, Zebrafish Embryology Genetics Metabolism,

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-78651266853&partnerID=40&md5=30a61a9b637299df0873584fb2dc55dc

Recently, extracellular RNases of the RNase A superfamily, with the characteristic CKxxNTF sequence signature, have been identified in fish. This has led to the recognition that these RNases are present in the whole vertebrate subphylum. In fact, they comprise the only enzyme family unique to vertebrates. Four RNases from zebrafish (Danio rerio) have been previously reported and have a very low RNase activity; some of these are endowed, like human angiogenin, with powerful angiogenic and bactericidal activities. In the present paper, we report the three-dimensional structure, the thermodynamic behaviour and the biological properties of a novel zebrafish RNase, ZF-RNase-5. The investigation of its structural and functional properties, extended to all other subfamily members, provides an inclusive description of the whole zebrafish RNase subfamily. The Authors Journal compilation 2011 Biochemical Society
*** IBB - CNR ***

Dipartimento di Biologia Strutturale e Funzionale, Università di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, I-80126 Naples, Italy

Dipartimento di Chimica, Università di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, I-80126 Naples, Italy

Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale Delle Ricerche (CNR), Via Mezzocannone 16, I-80134 Naples, Italy
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Covassin, L. D., Siekmann, A. F., Kacergis, M. C., Laver, E., Moore, J. C., Villefranc, J. A., Weinstein, B. M., Lawson, N. D., A genetic screen for vascular mutants in zebrafish reveals dynamic roles for Vegf/Plcg1 signaling during artery development (2009) Dev. Biol., 329, pp. 212-226

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Monti, D. M., Yu, W., Pizzo, E., Shima, K., Hu, M. G., Di Malta, C., Piccoli, R., Hu, G. F., Characterization of the angiogenic activity of zebrafish ribonucleases (2009) FEBS J., 276, pp. 4077-4090

Rosenberg, H. F., Recombinant human eosinophil cationic protein ribonuclease activity is not essential for cytotoxicity (1995) J. Biol. Chem., 270, pp. 7876-7881

Kelemen, B. R., Klink, T. A., Behlke, M. A., Eubanks, S. R., Leland, P. A., Raines, R. T., Hypersensitive substrate for ribonucleases (1999) Nucleic Acids Res., 27, pp. 3696-3701

Venyaminov, S. Y., Yang, J. T., Determination of protein secondary structure (1996) Circular Dichroism and the Conformational Analysis of Biomolecules, pp. 69-107. , Fasman, G. D., ed., Plenum Press, New York

McCoy, A. J., Grosse-Kunstleve, R. W., Storoni, L. C., Read, R. J., Likelihood-enhanced fast translation functions (2005) Acta Crystallogr. D Biol. Crystallogr., 61, pp. 458-464

Acharya, K. R., Shapiro, R., Riordan, J. F., Vallee, B. L., Crystal structure of bovine angiogenin at 1. 5- resolution (1995) Proc. Natl. Acad. Sci U. S. A., 92, pp. 2949-2953

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Jones, T. A., Zou, J. Y., Cowan, S. W., Kjedgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. D Biol. Crystallogr., 56, pp. 714-721

Laskowski, R. A., MacArthur, M. W., Moss, M. D., Thornton, J. M., PROCHECK: A program to check the stereochemical quality of protein structure (1993) J. Appl. Crystallogr., 26, pp. 283-291

Hooft, R. W., Vriend, G., Sander, C., Abola, E. E., Errors in protein structures (1996) Nature, 381, p. 272

Sippl, M. J., Recognition of errors in three-dimensional structures of proteins (1993) Proteins, 17, pp. 355-362

Sippl, M. J., Knowledge-based potentials for proteins (1995) Curr. Opin. Struct. Biol., 5, pp. 229-235

Holloway, D. E., Chavali, G. B., Hares, M. C., Subramanian, V., Acharya, K. R., Structure of murine angiogenin: Features of the substrate- and cell-binding regions and prospects for inhibitor-binding studies (2005) Acta Crystallogr. D Biol. Crystallogr., 61, pp. 1568-1578

Leonidas, D. D., Chavali, G. B., Jardine, A. M., Li, S., Shapiro, R., Acharya, K. R., Binding of phosphate and pyrophosphate ions at the active site of human angiogenin as revealed by X-ray crystallography (2001) Protein Sci., 10, pp. 1669-1676

Leland, P. A., Staniszewski, K. E., Park, C., Kelemen, B. R., Raines, R. T., The ribonucleolytic activity of angiogenin (2002) Biochemistry, 41, pp. 1343-1350

Schultz, L. W., Quirk, D. J., Raines, R. T., His. Asp catalytic dyad of ribonuclease A: Structure and function of the wild-type, D121N, and D121A enzymes (1998) Biochemistry, 37, pp. 8886-8898

Huang, Y. C., Lin, Y. M., Chang, T. W., Wu, S. J., Lee, Y. S., Chang, M. D., Chen, C., Liao, Y. D., The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity (2007) J. Biol. Chem., 282, pp. 4626-4633

Nitto, T., Dyer, K. D., Czapiga, M., Rosenberg, H. F., Evolution and function of leukocyte RNase a ribonucleases of the avian species, Gallus gallus (2006) J. Biol. Chem., 281, pp. 25622-25634

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* Structure and stability of the non-covalent swapped dimer of bovine seminal ribonuclease - An enzyme tailored to evade ribonuclease protein inhibitor (101 visite)
Sica F, Di Fiore A, Merlino A, Mazzarella L
J Biol Chem Journal Of Biological Chemistry (ISSN: 0021-9258, 1083-351x), 2004 Sep 27; 279(35): 36753-36760.
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* Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer (86 visite)
Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 689-695.
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* Dynamic properties of the N-terminal swapped dimer of ribonuclease (92 visite)
Merlino A, Vitagliano L, Ceruso MA, Mazzarella L
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2004 Apr; 86(4): 2383-2391.
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* Crystal Structure Of The Dimeric Un-Swapped Form Of Bovine Seminal Ribonuclease (106 visite)
Berisio R, Sica F, De Lorenzo C, Di Fiore A, Piccoli R, Zagari A, Mazzarella L
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2003 Nov 6; 554(1-2): 105-110.
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* Subtle functional collective motions in pancreatic-like ribonucleases: From ribonuclease A to angiogenin (87 visite)
Merlino A, Vitagliano L, Ceruso MA, Mazzarella L
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2003 Oct 1; 53(1): 101-110.
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* The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative (95 visite)
Sica F, Di Fiore A, Zagari A, Mazzarella L
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2003 Sep 1; 52(2): 263-271.
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* Antineoplastic ribonucleases selectively kill thyroid carcinoma cells via caspase-mediated induction of apoptosis (99 visite)
Spalletti-cernia D, Sorrentino R, Di Gaetano S, Arciello A, Garbi C, Piccoli R, D'Alessio G, Vecchio G, Laccetti P, Santoro M
Journal Of Clinical Endocrinology & Metabolism (ISSN: 0021-972x), 2003 Jun; 88(6): 2900-2907.
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* Global and local motions in ribonuclease A: A molecular dynamics study (87 visite)
Merlino A, Vitagliano L, Ceruso M, Di Nola A, Mazzarella L
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2002 Nov 15; 65(4): 274-283.
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* Reversible substrate-induced domain motions in ribonuclease (70 visite)
Vitagliano L, Merlino A, Zagari A, Mazzarella L
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2002 Jan 1; 46(1): 97-104.
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* Atomic resolution structures of ribonuclease A at six pH values (101 visite)
Berisio R, Sica F, Lamzin VS, Wilson KS, Zagari A, Mazzarella L
Acta Crystallogr Sect D Biol Crystallogr Acta Crystallographica Section D Biological Crystallography (ISSN: 0907-4449), 2002; 58(3): 441-450.
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Effect of deamidation on folding of ribonuclease (65 visite)
Orru S, Vitagliano L, Esposito L, Mazzarella L, Marino G, Ruoppolo M
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2000 Dec; 9(12): 2577-2582.
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Productive and nonproductive binding to ribonuclease A: X-ray structure of two complexes with uridylyl(2 ', 5 ')guanosine (103 visite)
Vitagliano L, Merlino A, Zagari A, Mazzarella L
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2000 Jun; 9(6): 1217-1225.
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The ultrahigh resolution crystal structure of ribonuclease A containing an isoaspartyl residue: Hydration and sterochemical analysis (136 visite)
Esposito L, Vitagliano L, Sica F, Sorrentino G, Zagari A, Mazzarella L
J Mol Biol Journal Of Molecular Biology (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2000 Mar 31; 297(3): 713-732.
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Reversible domain motions induced by substrate binding in ribonuclease (62 visite)
ZagariA, Berisio R, Merlino A, Sica F, Vitagliano L, Mazzarella L
Acta Crystallographica Section A, 2000; 56: 263-263.
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A potential allosteric subsite generated by domain swapping in bovine seminal ribonuclease (90 visite)
Vitagliano L, Adinolfi S, Sica F, Merlino A, Zagari A, Mazzarella L
J Mol Biol Journal Of Molecular Biology (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1999 Oct 29; 293(3): 569-577.
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Crystallization of multiple forms of bovine seminal ribonuclease in the liganded and unliganded state (86 visite)
Sica F, Adinolfi S, Berisio R, De Lorenzo C, Mazzarella L, Piccoli R, Vitagliano L, Zagari A
J Cryst Growth (ISSN: 0022-0248), 1999; 196(2-4): 305-312.
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Binding of a substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2 ', 5 ')adenosine (87 visite)
Vitagliano L, Adinolfi S, Riccio A, Sica F, Zagari A, Mazzarella L
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 1998 Sep; 7(8): 1691-1699.
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Cosolute effect on crystallization of two dinucleotide complexes of bovine seminal ribonuclease from concentrated salt solutions (83 visite)
Sica F, Adinolfi S, Vitagliano L, Zagari A, Capasso S, Mazzarella L
J Cryst Growth (ISSN: 0022-0248), 1996; 168(1-4): 192-197.
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Deamidation in proteins: The crystal structure of bovine pancreatic ribonuclease with an isoaspartyl residue at position 67 (83 visite)
Capasso S, Di Donato A, Esposito L, Sica F, Sorrentino G, Vitagliano L, Zagari A, Mazzarella L
J Mol Biol Journal Of Molecular Biology (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1996; 257(3): 492-496.
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Phylogenetic evolution of intermediate filament associated proteins in ependymal cells of several adult poikilotherm vertebrates (95 visite)
Lauro GM, Fonti R, Margotta V
Journal Fur Hirnforschung (ISSN: 0021-8359), 1991; 32(2): 257-261.
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40 Records (39 escludendo Abstract e Conferenze).
Impact factor totale: 149.432 (147.102 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 141.418 (139.088 escludendo Abstract e Conferenze).

Interrogazione bibliografica effettuata: (([btitle] "Angiogenin" OR [btitle] "Bactericidal Activity" OR [btitle] "Vertebrate" OR [btitle] "Zebrafish (zf) (danio Rerio)" OR [btitle] "Ribonuclease") AND NOT [id] = 8839)







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