*

Institute of Biosciences and Bioresources

National Research Council of Italy

Clemente Capasso

Role: Researcher
Section: Researchers and Technologists
Division: Naples
Tel: (39) 081-6132559-081-6132558
E-mail: clemente.capasso@ibbr.cnr.it


Name: Clemente Capasso

Date and Place of Birth: 22.07.1965, Napoli, Italy

Address: Institute of Biosciences and BioResources, National Research Council, - Via Pietro Castellino 111- 80131, Napoli, Italy,

Tel: ++39 0816132558,

E-mail: clemente.capasso@ibbr.cnr.it

Education and Training

(From 1992-present)

1992 Achieved the master degree in Biology cum laude at University of Naples “Federico II”.

1993-1994 Post-lauream training: University Federico II of Naples, Department of Evolutionary and Comparative Biology. Mentor: Prof. Elio Parisi.-Works on metallothioneins (MTs) in marine and terrestrial organisms

1993-1994 Awarded a C.N.R. fellowship: CNR. Institute of Protein Biochemistry and Enzymology of Naples. Mentor: Prof. Elio Parisi. Continues work on MTs.

1/10/1994-1/12/1994 Visiting Scientist: Biological Station of Roscoff (France, CNR/CNRS cooperation). Works on metal-binding proteins in bacteria.

1995-1996 Awarded a CNR fellowship: University of Genova, Italy. Works on protein crystallization (serine proteinases, superoxide dismutase and hexokinase).

1/10/1996-31/12/2013 Researcher at CNR-Institute of Protein Biochemistry and Enzymology, Naples, Italy. Principal investigator of the scientific project: "Cloning, heterologous expression and structure of proteins and enzymes from Antarctic organisms". Works on multigene family proteins (metallothioneins, aspartic proteinases and carbonic anhydrases).

12/05/1997-09/07/1997 Visiting Scientist: School of Molecular and Medical Biosciences, University College, Cardiff. Works on expression of heterologous proteins (MTs and aspartic proteinases) in E. coli.

2003-2004 Research Associate: University of Southern California Keck School of Medicine, Los Angeles, CA. Works on human 5-lipoxygenase.

1/12/2014-present Researcher at CNR- Institute of Biosciences and Bioresources (IBBR). Principal Principal investigator of the scientific projects: 1) Evolution, adaptation and biodiversity of carbonic anhydrases from Antarctic organisms; 2) Capture of the CO2 from flue gases by using enzymes from moderately thermophilic microorganisms.

Scientific Activities

Clemente Capasso obtained his MSc in biology cum laude at the University of Naples ‘Federico II’ (Italy). His research interest at the Italian National Research Council (CNR; Rome, Italy) from 1992 to date has been the study of the structure/function relationship of both native and recombinant proteins from terrestrial and marine organisms. In particular, he studied metallothioneins and aspartic proteinases in Echinoderms and Antarctic fish. This research activity has allowed him to acquire extensive knowledge of most protein purification procedures as well as kinetic, chemical-physical and structural characterization of enzymes. He also has experience with molecular biology techniques, such as nucleic acids isolation, cloning and expression of recombinant proteins and enzymes in Escherichia coli. Recently, his research activity has been focused on the investigation of enzymes involved in the hydration of CO2 (carbonic anhydrases) in extremophilic microorganisms. The preliminary results of this study are helpful in developing new methodologies for the use of enzymatic systems in biotechnologies. All of these activities have led to more than 75 publications in peer-reviewed journals. He has a long and strong scientific background, developed over 15 years of experience acquired by intense training in Italian and international laboratories. He is the Associate Editor of Journal of Enzyme Inhibition and Medicinal Chemistry, and is on the Editorial Board of the journal Expert Opinion on Therapeutic Patents.

Publications, Books and Articles

1. Vullo D, Kupriyanova EV, Scozzafava A, Capasso C, Supuran CT. Anion inhibition study of the beta-carbonic anhydrase (CahB1) from the cyanobacterium Coleofasciculus chthonoplastes (ex-Microcoleus chthonoplastes). Bioorg Med Chem, 2014;22:1667-1671

2. Vullo D, Flemetakis E, Scozzafava A, Capasso C, Supuran CT. Anion inhibition studies of two alpha-carbonic anhydrases from Lotus japonicus, LjCAA1 and LjCAA2. J Inorg Biochem, 2014;136:67-72

3. Vullo D, Del Prete S, Osman SM, Scozzafava A, Alothman Z, Supuran CT, Capasso C. Anion inhibition study of the beta-class carbonic anhydrase (PgiCAb) from the oral pathogen Porphyromonas gingivalis. Bioorg Med Chem Lett, 2014;24:4402-4406

4. Vullo D, Del Prete S, Osman SM, De Luca V, Scozzafava A, Alothman Z, Supuran CT, Capasso C. Sulfonamide inhibition studies of the delta-carbonic anhydrase from the diatom Thalassiosira weissflogii. Bioorg Med Chem Lett, 2014;24:275-279

5. Vullo D, Del Prete S, Osman SM, De Luca V, Scozzafava A, Alothman Z, Supuran CT, Capasso C. Sulfonamide inhibition studies of the gamma-carbonic anhydrase from the oral pathogen Porphyromonas gingivalis. Bioorg Med Chem Lett, 2014;24:240-244

6. Rodrigues GC, Feijo DF, Bozza MT, Pan P, Vullo D, Parkkila S, Supuran CT, Capasso C, Aguiar AP, Vermelho AB. Design, synthesis, and evaluation of hydroxamic acid derivatives as promising agents for the management of Chagas disease. J Med Chem, 2014;57:298-308

7. Prete SD, Vullo D, Osman SM, Scozzafava A, AlOthman Z, Capasso C, Supuran CT. Sulfonamide inhibition study of the carbonic anhydrases from the bacterial pathogen Porphyromonas gingivalis: the beta-class (PgiCAb) versus the gamma-class (PgiCA) enzymes. Bioorg Med Chem, 2014;22:4537-4543

8. Pisani A, Sabbatini M, Riccio E, Rossano R, Andreucci M, Capasso C, De Luca V, Carginale V, Bizzarri M, Borrelli A, Schiattarella A, Santangelo M, Mancini A. Effect of a recombinant manganese superoxide dismutase on prevention of contrast-induced acute kidney injury. Clin Exp Nephrol, 2014;18:424-431

9. Nishimori I, Vullo D, Minakuchi T, Scozzafava A, Osman SM, AlOthman Z, Capasso C, Supuran CT. Anion inhibition studies of two new beta-carbonic anhydrases from the bacterial pathogen Legionella pneumophila. Bioorg Med Chem Lett, 2014;24:1127-1132

10. Nishimori I, Vullo D, Minakuchi T, Scozzafava A, Capasso C, Supuran CT. Sulfonamide inhibition studies of two beta-carbonic anhydrases from the bacterial pathogen Legionella pneumophila. Bioorg Med Chem, 2014;22:2939-2946

11. Migliardini F, De Luca V, Carginale V, Rossi M, Corbo P, Supuran CT, Capasso C. Biomimetic CO2 capture using a highly thermostable bacterial alpha-carbonic anhydrase immobilized on a polyurethane foam. J Enzyme Inhib Med Chem, 2014;29:146-150

12. Del Prete S, Vullo D, Scozzafava A, Capasso C, Supuran CT. Cloning, characterization and anion inhibition study of the delta-class carbonic anhydrase (TweCA) from the marine diatom Thalassiosira weissflogii. Bioorg Med Chem, 2014;22:531-537

13. Del Prete S, Vullo D, Fisher GM, Andrews KT, Poulsen SA, Capasso C, Supuran CT. Discovery of a new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum-The eta-carbonic anhydrases. Bioorg Med Chem Lett, 2014;24:4389-4396

14. Del Prete S, Vullo D, De Luca V, Supuran CT, Capasso C. Biochemical characterization of the delta-carbonic anhydrase from the marine diatom Thalassiosira weissflogii, TweCA. J Enzyme Inhib Med Chem, 2014;

15. Del Prete S, Vullo D, De Luca V, AlOthman Z, Osman SM, Supuran CT, Capasso C. Biochemical characterization of recombinant beta-carbonic anhydrase (PgiCAb) identified in the genome of the oral pathogenic bacterium Porphyromonas gingivalis. J Enzyme Inhib Med Chem, 2014;1-5

16. Del Prete S, De Luca V, Vullo D, Scozzafava A, Carginale V, Supuran CT, Capasso C. Biochemical characterization of the gamma-carbonic anhydrase from the oral pathogen Porphyromonas gingivalis, PgiCA. J Enzyme Inhib Med Chem, 2014;29:532-537

17. Del Prete S, De Luca V, Scozzafava A, Carginale V, Supuran CT, Capasso C. Biochemical properties of a new alpha-carbonic anhydrase from the human pathogenic bacterium, Vibrio cholerae. J Enzyme Inhib Med Chem, 2014;29:23-27

18. De Luca V, Del Prete S, Supuran CT, Capasso C. Protonography, a new technique for the analysis of carbonic anhydrase activity. J Enzyme Inhib Med Chem, 2014;1-6

19. Ceruso M, Del Prete S, AlOthman Z, Osman SM, Scozzafava A, Capasso C, Supuran CT. Synthesis of sulfonamides with effective inhibitory action against Porphyromonas gingivalis gamma-carbonic anhydrase. Bioorg Med Chem Lett, 2014;24:4006-4010

20. Ceruso M, Del Prete S, Alothman Z, Capasso C, Supuran CT. Sulfonamides with Potent Inhibitory Action and Selectivity against the alpha-Carbonic Anhydrase from Vibrio cholerae. ACS Med Chem Lett, 2014;5:826-830

21. Capasso C, Supuran CT. Sulfa and trimethoprim-like drugs - antimetabolites acting as carbonic anhydrase, dihydropteroate synthase and dihydrofolate reductase inhibitors. J Enzyme Inhib Med Chem, 2014;29:379-387

22. Capasso C, Supuran CT. An overview of the alpha-, beta- and gamma-carbonic anhydrases from Bacteria: can bacterial carbonic anhydrases shed new light on evolution of bacteria? J Enzyme Inhib Med Chem, 2014;

23. Capasso C, Supuran CT. An Overview of the Selectivity and Efficiency of the Bacterial Carbonic Anhydrase Inhibitors. Curr Med Chem, 2014;

24. Bilginer S, Unluer E, Gul HI, Mete E, Isik S, Vullo D, Ozensoy-Guler O, Beyaztas S, Capasso C, Supuran CT. Carbonic anhydrase inhibitors. Phenols incorporating 2- or 3-pyridyl-ethenylcarbonyl and tertiary amine moieties strongly inhibit Saccharomyces cerevisiae beta-carbonic anhydrase. J Enzyme Inhib Med Chem, 2014;29:495-499

25. Alafeefy AM, Ceruso M, Al-Tamimi AM, Del Prete S, Capasso C, Supuran CT. Quinazoline-sulfonamides with potent inhibitory activity against the alpha-carbonic anhydrase from Vibrio cholerae. Bioorg Med Chem, 2014;22:5133-5140

26. Alafeefy AM, Abdel-Aziz HA, Vullo D, Al-Tamimi AM, Awaad AS, Mohamed MA, Capasso C, Supuran CT. Inhibition of human carbonic anhydrase isozymes I, II, IX and XII with a new series of sulfonamides incorporating aroylhydrazone-, [1.2,4]triazolo[3.4-b][1.3,4]thiadiazinyl- or 2-(cyanophenylmethylene)-1.3,4-thiadiazol-3(2H)-yl moieties. J Enzyme Inhib Med Chem, 2014;

27. Alafeefy AM, Abdel-Aziz HA, Vullo D, Al-Tamimi AM, Al-Jaber NA, Capasso C, Supuran CT. Inhibition of carbonic anhydrases from the extremophilic bacteria Sulfurihydrogenibium yellostonense (SspCA) and S. azorense (SazCA) with a new series of sulfonamides incorporating aroylhydrazone-, [1.2,4]triazolo[3.4-b][1.3,4]thiadiazinyl- or 2-(cyanophenylmethylene)-1.3,4-thiadiazol-3(2H)-yl moieties. Bioorg Med Chem, 2014;22:141-147

28. Winum JY, Capasso C. Novel antibody to a carbonic anhydrase: patent evaluation of WO2011138279A1. Expert Opin Ther Pat, 2013;23:757-760

29. Vullo D, Sai Kumar RS, Scozzafava A, Capasso C, Ferry JG, Supuran CT. Anion inhibition studies of a beta-carbonic anhydrase from Clostridium perfringens. Bioorg Med Chem Lett, 2013;23:6706-6710

30. Vullo D, Luca VD, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. The alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 is highly susceptible to inhibition by sulfonamides. Bioorg Med Chem, 2013;21:1534-1538

31. Vullo D, Leewattanapasuk W, Muhlschlegel FA, Mastrolorenzo A, Capasso C, Supuran CT. Carbonic anhydrase inhibitors: inhibition of the beta-class enzyme from the pathogenic yeast Candida glabrata with sulfonamides, sulfamates and sulfamides. Bioorg Med Chem Lett, 2013;23:2647-2652

32. Vullo D, Isik S, Del Prete S, De Luca V, Carginale V, Scozzafava A, Supuran CT, Capasso C. Anion inhibition studies of the alpha-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae. Bioorg Med Chem Lett, 2013;23:1636-1638

33. Vullo D, De Luca V, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. The extremo-alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium azorense is highly inhibited by sulfonamides. Bioorg Med Chem, 2013;21:4521-4525

34. Syrjanen L, Vermelho AB, Rodrigues Ide A, Corte-Real S, Salonen T, Pan P, Vullo D, Parkkila S, Capasso C, Supuran CT. Cloning, characterization, and inhibition studies of a beta-carbonic anhydrase from Leishmania donovani chagasi, the protozoan parasite responsible for leishmaniasis. J Med Chem, 2013;56:7372-7381

35. Russo ME, Olivieri G, Capasso C, De Luca V, Marzocchella A, Salatino P, Rossi M. Kinetic study of a novel thermo-stable alpha-carbonic anhydrase for biomimetic CO2 capture. Enzyme Microb Technol, 2013;53:271-277

36. Pan P, Vermelho AB, Scozzafava A, Parkkila S, Capasso C, Supuran CT. Anion inhibition studies of the alpha-carbonic anhydrase from the protozoan pathogen Trypanosoma cruzi, the causative agent of Chagas disease. Bioorg Med Chem, 2013;21:4472-4476

37. Pan P, Vermelho AB, Capaci Rodrigues G, Scozzafava A, Tolvanen ME, Parkkila S, Capasso C, Supuran CT. Cloning, characterization, and sulfonamide and thiol inhibition studies of an alpha-carbonic anhydrase from Trypanosoma cruzi, the causative agent of Chagas disease. J Med Chem, 2013;56:1761-1771

38. Nishimori I, Vullo D, Minakuchi T, Scozzafava A, Capasso C, Supuran CT. Restoring catalytic activity to the human carbonic anhydrase (CA) related proteins VIII, X and XI affords isoforms with high catalytic efficiency and susceptibility to anion inhibition. Bioorg Med Chem Lett, 2013;23:256-260

39. Monti SM, De Simone G, Dathan NA, Ludwig M, Vullo D, Scozzafava A, Capasso C, Supuran CT. Kinetic and anion inhibition studies of a beta-carbonic anhydrase (FbiCA 1) from the C4 plant Flaveria bidentis. Bioorg Med Chem Lett, 2013;23:1626-1630

40. Luca VD, Vullo D, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. An alpha-carbonic anhydrase from the thermophilic bacterium Sulphurihydrogenibium azorense is the fastest enzyme known for the CO2 hydration reaction. Bioorg Med Chem, 2013;21:1465-1469

41. Guzel-Akdemir O, Akdemir A, Pan P, Vermelho AB, Parkkila S, Scozzafava A, Capasso C, Supuran CT. A class of sulfonamides with strong inhibitory action against the alpha-carbonic anhydrase from Trypanosoma cruzi. J Med Chem, 2013;56:5773-5781

42. Di Fiore A, Capasso C, De Luca V, Monti SM, Carginale V, Supuran CT, Scozzafava A, Pedone C, Rossi M, De Simone G. X-ray structure of the first extremo-alpha-carbonic anhydrase’, a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1. Acta Crystallogr D Biol Crystallogr, 2013;69:1150-1159

43. Del Prete S, Vullo D, De Luca V, Carginale V, Scozzafava A, Supuran CT, Capasso C. A highly catalytically active gamma-carbonic anhydrase from the pathogenic anaerobe Porphyromonas gingivalis and its inhibition profile with anions and small molecules. Bioorg Med Chem Lett, 2013;23:4067-4071

44. Damiano S, Trepiccione F, Ciarcia R, Scanni R, Spagnuolo M, Manco L, Borrelli A, Capasso C, Mancini R, Schiattarella A, Iervolino A, Zacchia E, Bata-Csere A, Florio S, Anastasio P, Pollastro R, Mancini A, Capasso G. A new recombinant MnSOD prevents the cyclosporine A-induced renal impairment. Nephrol Dial Transplant, 2013;28:2066-2072

45. Capasso C, Supuran CT. Anti-infective carbonic anhydrase inhibitors: a patent and literature review. Expert Opin Ther Pat, 2013;23:693-704

46. Alafeefy AM, Isik S, Al-Jaber NA, Vullo D, Abdel-Aziz HA, Ashour AE, Awaad AS, Capasso C, Supuran CT. Carbonic anhydrase inhibitors. Benzenesulfonamides incorporating cyanoacrylamide moieties strongly inhibit Saccharomyces cerevisiae beta-carbonic anhydrase. Bioorg Med Chem Lett, 2013;23:3570-3575

47. Akdemir A, Vullo D, De Luca V, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. The extremo-alpha-carbonic anhydrase (CA) from Sulfurihydrogenibium azorense, the fastest CA known, is highly activated by amino acids and amines. Bioorg Med Chem Lett, 2013;23:1087-1090

48. Akdemir A, Guzel-Akdemir O, Scozzafava A, Capasso C, Supuran CT. Inhibition of tumor-associated human carbonic anhydrase isozymes IX and XII by a new class of substituted-phenylacetamido aromatic sulfonamides. Bioorg Med Chem, 2013;21:5228-5232

49. Vullo D, De Luca V, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. The first activation study of a bacterial carbonic anhydrase (CA). The thermostable alpha-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines. Bioorg Med Chem Lett, 2012;22:6324-6327

50. Vullo D, De Luca V, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. Anion inhibition studies of the fastest carbonic anhydrase (CA) known, the extremo-CA from the bacterium Sulfurihydrogenibium azorense. Bioorg Med Chem Lett, 2012;22:7142-7145

51. Del Prete S, Isik S, Vullo D, De Luca V, Carginale V, Scozzafava A, Supuran CT, Capasso C. DNA cloning, characterization, and inhibition studies of an alpha-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae. J Med Chem, 2012;55:10742-10748

52. De Luca V, Vullo D, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. Anion inhibition studies of an alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1. Bioorg Med Chem Lett, 2012;22:5630-5634

53. Capasso C, De Luca V, Carginale V, Cannio R, Rossi M. Biochemical properties of a novel and highly thermostable bacterial alpha-carbonic anhydrase from Sulfurihydrogenibium yellowstonense YO3AOP1. J Enzyme Inhib Med Chem, 2012;27:892-897

54. Borrelli A, Schiattarella A, Musella A, Mancini R, Capasso C, De Luca V, Carginale V, Sanseverino M, Tornesello AL, Gori E, Pica A, Di Santi A, Basile F, Iacobellis F, Colacurci N, Cobellis L, Mancini A. A molecular carrier to transport and deliver cisplatin into endometrial cancer cells. Chem Biol Drug Des, 2012;80:9-16

55. Stranges S, Galletti F, Farinaro E, D’Elia L, Russo O, Iacone R, Capasso C, Carginale V, De Luca V, Della Valle E, Cappuccio FP, Strazzullo P. Associations of selenium status with cardiometabolic risk factors: an 8-year follow-up analysis of the Olivetti Heart study. Atherosclerosis, 2011;217:274-278

56. Borrelli A, Schiattarella A, Mancini R, Morelli F, Capasso C, De Luca V, Gori E, Mancini A. The leader peptide of a human rec. MnSOD as molecular carrier which delivers high amounts of Cisplatin into tumor cells inducing a fast apoptosis in vitro. Int J Cancer, 2011;128:453-459

57. Venezia A, Barba G, Russo O, Capasso C, De Luca V, Farinaro E, Cappuccio FP, Galletti F, Rossi G, Strazzullo P. Dietary sodium intake in a sample of adult male population in southern Italy: results of the Olivetti Heart Study. Eur J Clin Nutr, 2010;64:518-524

58. Cobucci-Ponzano B, Conte F, Strazzulli A, Capasso C, Fiume I, Pocsfalvi G, Rossi M, Moracci M. The molecular characterization of a novel GH38 alpha-mannosidase from the crenarchaeon Sulfolobus solfataricus revealed its ability in de-mannosylating glycoproteins. Biochimie, 2010;92:1895-1907

59. De Luca V, Maria G, De Mauro G, Catara G, Carginale V, Ruggiero G, Capasso A, Parisi E, Brier S, Engen JR, Capasso C. Aspartic proteinases in Antarctic fish. Mar Genomics, 2009;2:1-10

60. Capasso C, Carginale V, Crescenzi O, Di Maro D, Spadaccini R, Temussi PA, Parisi E. Structural and functional studies of vertebrate metallothioneins: cross-talk between domains in the absence of physical contact. Biochem J, 2005;391:95-103

61. Carginale V, Trinchella F, Capasso C, Scudiero R, Riggio M, Parisi E. Adaptive evolution and functional divergence of pepsin gene family. Gene, 2004;333:81-90

62. Carginale V, Trinchella F, Capasso C, Scudiero R, Parisi E. Gene amplification and cold adaptation of pepsin in Antarctic fish. A possible strategy for food digestion at low temperature. Gene, 2004;336:195-205

63. Capasso C, Carginale V, Scudiero R, Crescenzi O, Spadaccini R, Temussi PA, Parisi E. Phylogenetic divergence of fish and mammalian metallothionein: relationships with structural diversification and organismal temperature. J Mol Evol, 2003;57 Suppl 1:S250-257

64. Capasso C, Carginale V, Crescenzi O, Di Maro D, Parisi E, Spadaccini R, Temussi PA. Solution structure of MT_nc, a novel metallothionein from the Antarctic fish Notothenia coriiceps. Structure, 2003;11:435-443

65. Carginale V, Capasso C, Scudiero R, Parisi E. Identification of cadmium-sensitive genes in the Antarctic fish Chionodraco hamatus by messenger RNA differential display. Gene, 2002;299:117-124

66. Capasso C, Abugo O, Tanfani F, Scire A, Carginale V, Scudiero R, Parisi E, D’Auria S. Stability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse. Proteins, 2002;46:259-267

67. Scudiero R, Carginale V, Capasso C, Riggio M, Filosa S, Parisi E. Structural and functional analysis of metal regulatory elements in the promoter region of genes encoding metallothionein isoforms in the Antarctic fish Chionodraco hamatus (icefish). Gene, 2001;274:199-208

68. D’Auria S, Carginale V, Scudiero R, Crescenzi O, Di Maro D, Temussi PA, Parisi E, Capasso C. Structural characterization and thermal stability of Notothenia coriiceps metallothionein. Biochem J, 2001;354:291-299

69. Llanos J, Capasso C, Parisi E, Prieur D, Jeanthon C. Susceptibility to heavy metals and cadmium accumulation in aerobic and anaerobic thermophilic microorganisms isolated from deep-sea hydrothermal vents. Curr Microbiol, 2000;41:201-205

70. Capasso C, Lees WE, Capasso A, Scudiero R, Carginale V, Kille P, Kay J, Parisi E. Cathepsin D from the liver of the antarctic icefish Chionodraco hamatus exhibits unusual activity and stability at high temperatures1. Biochim Biophys Acta, 1999;1431:64-73

71. Bargelloni L, Scudiero R, Parisi E, Carginale V, Capasso C, Patarnello T. Metallothioneins in antarctic fish: evidence for independent duplication and gene conversion. Mol Biol Evol, 1999;16:885-897

72. Carginale V, Scudiero R, Capasso C, Capasso A, Kille P, di Prisco G, Parisi E. Cadmium-induced differential accumulation of metallothionein isoforms in the Antarctic icefish, which exhibits no basal metallothionein protein but high endogenous mRNA levels. Biochem J, 1998;332 ( Pt 2):475-481

73. Capasso C, Riggio M, Scudiero R, Carginale V, di Prisco G, Kay J, Kille P, Parisi E. Molecular cloning and sequence determination of a novel aspartic proteinase from Antarctic fish. Biochim Biophys Acta, 1998;1387:457-461

74. Scudiero R, Carginale V, Riggio M, Capasso C, Capasso A, Kille P, di Prisco G, Parisi E. Difference in hepatic metallothionein content in Antarctic red-blooded and haemoglobinless fish: undetectable metallothionein levels in haemoglobinless fish is accompanied by accumulation of untranslated metallothionein mRNA. Biochem J, 1997;322 ( Pt 1):207-211

75. Scudiero R, Capasso C, Carginale V, Riggio M, Capasso A, Ciaramella M, Filosa S, Parisi E. PCR amplification and cloning of metallothionein complementary DNAs in temperate and Antarctic sea urchin characterized by a large difference in egg metallothionein content. Cell Mol Life Sci, 1997;53:472-477

76. Pesce A, Capasso C, Battistoni A, Folcarelli S, Rotilio G, Desideri A, Bolognesi M. Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography. J Mol Biol, 1997;274:408-420

77. Capasso C, Rizzi M, Menegatti E, Ascenzi P, Bolognesi M. Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites. J Mol Recognit, 1997;10:26-35

78. Capasso C, Nazzaro F, Marulli F, Capasso A, La Cara F, Parisi E. Identification of a high-molecular-weight cadmium-binding protein in copper-resistant Bacillus acidocaldarius cells. Res Microbiol, 1996;147:287-296

79. Battistoni A, Folcarelli S, Rotilio G, Capasso C, Pesce A, Bolognesi M, Desideri A. Crystallization and preliminary X-ray analysis of the monomeric Cu,Zn superoxide dismutase from Escherichia coli. Protein Sci, 1996;5:2125-2127

80. Scudiero R, Capasso C, Del Vecchio-Blanco F, Savino G, Capasso A, Parente A, Parisi E. Isolation and primary structure determination of a metallothionein from Paracentrotus lividus (Echinodermata, Echinoidea). Comp Biochem Physiol B Biochem Mol Biol, 1995;111:329-336

81. Scudiero R, Capasso C, De Prisco PP, Capasso A, Filosa S, Parisi E. Metal-binding proteins in eggs of various sea urchin species. Cell Biol Int, 1994;18:47-53

 

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