Multiple catalytically active thioredoxin folds: a winning strategy for many functions (1226 views)
Cell Mol Life Sci Cellular And Molecular Life Sciences (ISSN: 1420-682x), 2010 Nov; 67(22): 3797-3814.
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Paper type: Journal Article,
Impact factor: 7.047, 5-year impact factor: 6.609
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-78149469953&partnerID=40&md5=9969db18476e473c709ff98ea4b658b0
Keywords: Disulfide Bond, Hybrid Peroxiredoxin, Protein Disulfide Isomerase, Protein Disulfide Oxidoreductase, Redox Sites, Trx Fold, Hybrid Protein, Protein Erp57, Thioredoxin, Unclassified Drug, Alpha Helix, Beta Sheet, Catalysis, Dimerization, Enzyme Activity, Enzyme Analysis, Enzyme Structure, Molecular Evolution, Nonhuman, Nucleotide Sequence, Oxidation Reduction State, Protein Analysis, Protein Domain, Protein Folding, Protein Function, Protein Interaction, Protein Structure, Review, Thermophilic Bacterium, Amino Acid Sequence, Animals, Archaea, Archaeal Proteins, Bacterial Proteins, Catalytic Domain, Models, Molecular Sequence Data, Protein Disulfide-Isomerases, Sequence Alignment, Eukaryota,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, Naples 80134, Italy
Dipartimento di Biologia Strutturale e Funzionale, Università Degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, Naples 80126, Italy
References:
Not available.
Cell Mol Life Sci Cellular And Molecular Life Sciences (ISSN: 1420-682x), 2010 Nov; 67(22): 3797-3814.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 7.047, 5-year impact factor: 6.609
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-78149469953&partnerID=40&md5=9969db18476e473c709ff98ea4b658b0
Keywords: Disulfide Bond, Hybrid Peroxiredoxin, Protein Disulfide Isomerase, Protein Disulfide Oxidoreductase, Redox Sites, Trx Fold, Hybrid Protein, Protein Erp57, Thioredoxin, Unclassified Drug, Alpha Helix, Beta Sheet, Catalysis, Dimerization, Enzyme Activity, Enzyme Analysis, Enzyme Structure, Molecular Evolution, Nonhuman, Nucleotide Sequence, Oxidation Reduction State, Protein Analysis, Protein Domain, Protein Folding, Protein Function, Protein Interaction, Protein Structure, Review, Thermophilic Bacterium, Amino Acid Sequence, Animals, Archaea, Archaeal Proteins, Bacterial Proteins, Catalytic Domain, Models, Molecular Sequence Data, Protein Disulfide-Isomerases, Sequence Alignment, Eukaryota,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, Naples 80134, Italy
Dipartimento di Biologia Strutturale e Funzionale, Università Degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, Naples 80126, Italy
References:
Not available.
Multiple catalytically active thioredoxin folds: a winning strategy for many functions
The Thioredoxin (Trx) fold is a versatile protein scaffold consisting of a four-stranded β-sheet surrounded by three α-helices. Various insertions are possible on this structural theme originating different proteins, which show a variety of functions and specificities. During evolution, the assembly of different Trx fold domains has been used many times to build new multi-domain proteins able to perform a large number of catalytic functions. To clarify the interaction mode of the different Trx domains within a multi-domain structure and how their combination can affect catalytic performances, in this review, we report on a structural and functional analysis of the most representative proteins containing more than one catalytically active Trx domain: the eukaryotic protein disulfide isomerases (PDIs), the thermophilic protein disulfide oxidoreductases (PDOs) and the hybrid peroxiredoxins (Prxs). © 2010 Springer Basel AG.
The Thioredoxin (Trx) fold is a versatile protein scaffold consisting of a four-stranded β-sheet surrounded by three α-helices. Various insertions are possible on this structural theme originating different proteins, which show a variety of functions and specificities. During evolution, the assembly of different Trx fold domains has been used many times to build new multi-domain proteins able to perform a large number of catalytic functions. To clarify the interaction mode of the different Trx domains within a multi-domain structure and how their combination can affect catalytic performances, in this review, we report on a structural and functional analysis of the most representative proteins containing more than one catalytically active Trx domain: the eukaryotic protein disulfide isomerases (PDIs), the thermophilic protein disulfide oxidoreductases (PDOs) and the hybrid peroxiredoxins (Prxs). © 2010 Springer Basel AG.
Multiple catalytically active thioredoxin folds: a winning strategy for many functions
| ▼ Structural characterization of proteins and enzymes isolated from organisms living under unusual conditions |
Multiple catalytically active thioredoxin folds: a winning strategy for many functions
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Impact Factor: 2.596
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Hilvo M, Baranauskiene L, Salzano AM, Scaloni A, Matulis D, Innocenti A, Scozzafava A, Monti SM, Di Fiore A, De Simone G, Lindfors M, Janis J, Valjakka J, Pastorekova S, Pastorek J, Kulomaa MS, Nordlund HR, Supuran CT, Parkkila S
* Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymes (1124 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 10; 283(41): 27799-27809.
Impact Factor: 5.52
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Dalla Serra M, Cirioni O, Vitale RM, Renzone G, Coraiola M, Giacometti A, Potrich C, Baroni E, Guella G, Sanseverino M, De Luca S, Scalise G, Amodeo P, Scaloni A
* Structural features of distinctin affecting peptide biological and biochemical properties (994 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 29; 47(30): 7888-7899.
Impact Factor: 3.379
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Pedone E, Limauro D, Bartolucci S
* The machinery for oxidative protein folding in thermophiles (664 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2008 Jan; 10(1): 157-169.
Impact Factor: 6.19
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Pedone E, Limauro D, D'Alterio R, Rossi M, Bartolucci S
* Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (648 views)
Febs Journal (ISSN: 1742-464x), 2006 Dec; 273(23): 5407-5420.
Impact Factor: 3.033
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De Simone A, Berisio R, Zagari A, Vitagliano L
* Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation (931 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 740-747.
Impact Factor: 1.801
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Calvanese L, Saporito A, Marasco D, D'Auria G, Minchiotti G, Pedone C, Paolillo L, Falcigno L, Ruvo M
* Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala (1020 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Nov 30; 49(24): 7054-7062.
Impact Factor: 5.115
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D'Ambrosio K, Pedone E, Langella E, De Simone G, Rossi M, Pedone C, Bartolucci S
* A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: Structure, function and electrostatics (983 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Sep 29; 362(4): 743-752.
Impact Factor: 4.89
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De Simone G, Vitale RM, Di Fiore A, Pedone C, Scozzafava A, Montero JL, Winum JY, Supuran CT
* Carbonic anhydrase inhibitors: Hypoxia-activatable sulfonamides incorporating disulfide bonds that target the tumor-associated isoform IX (872 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Sep 7; 49(18): 5544-5551.
Impact Factor: 5.115
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Pedone E, D'Ambrosio K, De Simone G, Rossi M, Pedone C, Bartolucci S
* Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus (793 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Feb 10; 356(1): 155-164.
Impact Factor: 4.89
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Pedone E, Saviano M, Bartolucci S, Rossi M, Ausili A, Scire A, Bertoli E, Tanfani F
* Temperature-, SDS-, and pH-induced conformational changes in protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: A dynamic simulation and fourier transform infrared spectroscopic study (835 views)
J Proteome Res (ISSN: 1535-3893), 2005 Nov; 4(6): 1972-1980.
Impact Factor: 6.901
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Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F
* The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants (984 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 May 6; 280(18): 17953-17960.
Impact Factor: 5.854
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Picone D, Di Fiore A, Ercole C, Franzese M, Sica F, Tomaselli S, Mazzarella L
* The role of the hinge loop in domain swapping - The special case of bovine seminal ribonuclease (861 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Apr 8; 280(14): 13771-13778.
Impact Factor: 5.854
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Esposito L, De Simone A, Zagari A, Vitagliano L
* Correlation Between Omega And Psi Dihedral Angles In Protein Structures (1531 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2005 Apr 1; 347(3): 483-487.
Impact Factor: 5.229
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D'Ambrosio K, De Simone G, Pedone E, Rossi M, Bartolucci S, Pedone C
* Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1 (612 views)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2005 Mar 1; 61(3): 335-336.
Impact Factor: 0.568
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D'Ambrosio K, De Simone G, Pedone E, Rossi M, Bartolucci S, Pedone C
* Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aquifex aeolicus (585 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2004 Nov; 60(11): 2076-2077.
Impact Factor: 1.693
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Sica F, Di Fiore A, Merlino A, Mazzarella L
* Structure and stability of the non-covalent swapped dimer of bovine seminal ribonuclease - An enzyme tailored to evade ribonuclease protein inhibitor (859 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2004 Sep 27; 279(35): 36753-36760.
Impact Factor: 6.355
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Pedone E, Ren B, Ladenstein R, Rossi M, Bartolucci S
* Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase (716 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 Sep; 271(16): 3437-3448.
Impact Factor: 3.26
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Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L
* Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer (594 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 689-695.
Impact Factor: 2.863
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Sica F, Di Fiore A, Zagari A, Mazzarella L
* The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative (532 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2003 Sep 1; 52(2): 263-271.
Impact Factor: 4.313
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Orru S, Vitagliano L, Esposito L, Mazzarella L, Marino G, Ruoppolo M
Effect of deamidation on folding of ribonuclease (997 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2000 Dec; 9(12): 2577-2582.
Impact Factor: 3.869
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38 Records (37 excluding Abstracts).
Total impact factor: 153.67 (149.712 excluding Abstracts).
Total 5 year impact factor: 154.543 (149.163 excluding Abstracts).
Total impact factor: 153.67 (149.712 excluding Abstracts).
Total 5 year impact factor: 154.543 (149.163 excluding Abstracts).
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