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Role of side chains in collagen triple helix stabilization and partner recognition (293 visite)

Berisio R, De Simone A, Ruggiero A, Improta R, Vitagliano L

J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 131-140.

Tipo di articolo: Journal Article,

Impact factor: 1.807

Impact factor a 5 anni: 1.872


Parole chiave: Collagen, Iminoacids, Molecular Recognition, Protein Stability, Triple Helix, Amino Acid, Imino Acid, Peptide, Receptor, Conference Paper, Molecular Interaction, Molecular Stability, Priority Journal, Protein Family, Protein Function, Protein Motif, Protein Structure, Chemical Structure, Chemistry, Metabolism, Protein Secondary Structure, Protein Tertiary Structure, Review, Models,

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-63449103818&partnerID=40&md5=2937f6856803c162f38cbdece9d543b7

Collagen is a widespread protein family involved in a variety of biological processes. The complexity of collagen and its fibrous nature prevent detailed investigations on the full-length protein. Reductionist approaches conducted by dissecting the protein complexity through the use of model peptides have proved to be quite effective. There are, however, several issues regarding structure-stability relationships, aggregation in higher-order assemblies, and partner recognition that are still extensively investigated. In this review, we discuss the role that side chains play in triple helix stabilization and in partner recognition. On the basis of recent literature data, we show that collagen triple helix stability is the result of the interplay of different factors. As a general trend, interactions established by amino/ imino acid side chains within the triple helix scaffold effectively modulate the intrinsic residue propensity for this common structural motif. The use of peptidemodels has also highlighted the role that side chains play in collagen self-association and in its interactions with receptors. Valuable examples in these fields are illustrated. Finally, future actions required to obtain more detailed information on the structure and the function of this complex protein are also delineated. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.
*** IBB - CNR ***

Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 16, I-80134 Napoli, Italy

Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW Cambridge, United Kingdom
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Persikov, A. V., Ramshaw, J. A. M., Kirkpatrick, A., Brodsky, B., Amino acid propensities for the collagen triple-helix (2000) Biochemistry, 39, pp. 14960-14967

Jenkins, C. L., Raines, R. T., Insights on the conformational stability of collagen (2002) Nat. Prod. Rep, 19, pp. 49-59

Engel, J., B chinger, H., Structure, stability and folding of the collagen triple helix (2005) Top. Curr. Chem, 247, pp. 7-33

B achinger, H., Engel, J., The thermodynamics and kinetics of collagen folding (2005) Protein Folding Handbook, 2, pp. 1059-1111. , Buchner J, Kiefhaber T eds, Wiley-VCH: Weinheim

Kramer, R. Z., Vitagliano, L., Bella, J., Berisio, R., Mazzarella, L., Brodsky, B., Zagari, A., Berman, H. M., X-Ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (1998) J. Mol. Biol, 280, pp. 623-638

Kramer, R. Z., Bella, J., Mayville, P., Brodsky, B., Berman, H. M., Sequence dependent conformational variations of collagen triple-helical structure (1999) Nat. Struct. Biol, 6, pp. 454-457

Kramer, R. Z., Venugopal, M. G., Bella, J., Mayville, P., Brodsky, B., Berman, H. M., Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair (2000) J. Mol. Biol, 301, pp. 1191-1205

Schumacher, M. A., Mizuno, K., B chinger, H. P., The crystal structure of a collagen-like polypeptide with 3 (S) -Hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helix (2006) J. Biol. Chem, 281, pp. 27566-27574

Mooney, S. D., Klein, T. E., Structural models of Osteogenesis imperfecta-associated variants in the col1a1 gene (2002) Mol. Cell Proteomics, 1, pp. 868-875

Park, S., Klein, T. E., Pande, V. S., Folding and misfolding of the collagen triple helix: Markov analysis of molecular dynamics simulations (2007) Biophys. J, 93, pp. 4108-4115

Radmer, R. J., Klein, T. E., Triple helical structure and stabilization of collagen-like molecules with 4 (R) -hydroxyproline in the Xaa position (2006) Biophys. J, 90, pp. 578-588

Mogilner, I. G., Ruderman, G., Grigera, J. R., Collagen stability, hydration and native state (2002) J. Mol. Graph. Model, 21, pp. 209-213

Palfi, V. K., Perczel, A., How stable is a collagen triple helix? An ab initio study on various collagen and -sheet forming sequences (2008) J. Comput. Chem, 29, pp. 1374-1386

Shah, N. K., Ramshaw, J. A., Kirkpatrick, A., Shah, C., Brodsky, B., A host-guest set of triple-helical peptides: Stability of Gly-X-Y triplets containing common nonpolar residues (1996) Biochemistry, 35, pp. 10262-10268

Holmgren, S. K., Taylor, K. M., Bretscher, L. E., Raines, R. T., Code for collagen's stability deciphered (1998) Nature, 392, pp. 666-667

Raines, R. T., Emil Thomas Kaiser award (2005) Protein Sci, 2006 (15), pp. 1219-1225

Renner, C., Sacc, B., Moroder, L., Synthetic heterotrimeric collagen peptides as mimics of cell adhesion sites of the basement membrane (2004) Biopolymers, 76, pp. 34-47

Petsko, G. A., Structural basis of thermostability in hyperthermophilic proteins, or "there's more than one way to skin a cat (2001) Methods Enzymol, 334, pp. 469-478

Privalov, P. L., Stability of proteins. Proteins which do not present a single cooperative system (1982) Adv. Protein Chem, 35, pp. 1-104

Burjanadze, T. V., New analysis of thephylogenetic change of collagen thermostability (2000) Biopolymers, 53, pp. 523-528

Gustavson, K. H., The function of hydroxyproline in collagens (1955) Nature, 175, pp. 70-74

Holmgren, S. K., Bretscher, L. E., Taylor, K. M., Raines, R. T., A hyperstable collagenmimic (1999) Chem. Biol, 6, pp. 63-70

Bretscher, L. E., Jenkins, C. L., Taylor, K. M., DeRider, M. L., Raines, R. T., Conformational stability of collagen relies on a stereoelectronic effect (2001) J. Am. Chem. Soc, 123, pp. 777-778

(4 (S) -fluoroproline-Pro-Gly) 10 forms a triple helix, but (4 (R) -fluoroproline-Pro-Gly) 10 does not (2003) J. Am. Chem. Soc, 125, pp. 9922-9923

Bann, J. G., Bachinger, H. P., Glycosylation/hydroxylation-induced stabilization of the collagen triple helix. 4-trans-hydroxyproline in the Xaa position can stabilize the triple helix (2000) J. Biol. Chem, 275, pp. 24466-24469

Ramachandran, G. N., Bansal, M., Bhatnagar, R. S., A hypothesis on the role of hydroxyproline in stabilizing collagen structure (1973) Biochim. Biophys. Acta, 322, pp. 166-171

Hodges, J. A., Raines, R. T., Stereoelectronic effects on collagen stability: The dichotomy of 4-fluoroproline diastereomers (2003) J. Am. Chem. Soc, 125, pp. 9262-9263

Shoulders, M. D., Hodges, J. A., Raines, R. T., Reciprocity of steric and stereoelectronic effects in the collagen triple helix (2006) J. Am. Chem. Soc, 128, pp. 8112-8113

Cadamuro, S. A., Reichold, R., Kusebauch, U., Musiol, H. J., Renner, C., Tavan, P., Moroder, L., Conformational properties of 4- mercaptoproline and related derivatives (2008) Angew. Chem., Int. Ed. Engl, 47, pp. 2143-2146

Raman, S. S., Parthasarathi, R., Subramanian, V., Ramasami, T., Role of aspartic acid in collagen structure and stability: A molecular dynamics investigation (2006) J. Phys. Chem. B, 110, pp. 20678-20685

Xu, Y., Keene, D. R., Bujnicki, J. M., Hook, M., Lukomski, S., Streptococcal scl1 and scl2 proteins form collagen-like triple helices (2002) J. Biol. Chem, 277, pp. 27312-27318

Ravikumar, K. M., Hwang, W., Region-specific role of water in collagen unwinding and assembly (2008) Proteins, 72, pp. 1320-1332

Sacc, B., Sinner, E. K., Kaiser, J., L bken, C., Eble, J. A., Moroder, L., Binding and docking of synthetic heterotrimeric collagen type IV peptides with 1 1 integrin (2002) ChemBioChem, 3, pp. 904-907

Slatter, D. A., Foley, L. A., Peachey, A. R., Nietlispach, D., Farndale, R. W., Rapid synthesis of a register-specific heterotrimeric type I collagen helix encompassing the integrin 2 1 binding site (2006) J. Mol. Biol, 359, pp. 289-298

Slatter, D. A., Miles, C. A., Bailey, A. J., Asymmetry in the triple helix of collagen-like heterotrimers confirms that external bonds stabilize collagen structure (2003) J. Mol. Biol, 329, pp. 175-183

Kotch, F. W., Raines, R. T., Self-assembly of synthetic collagen triple helices (2006) Proc. Natl. Acad. Sci. U. S. A, 103, pp. 3028-3033

Cejas, M. A., Kinney, W. A., Chen, C., Vinter, J. G., Almond Jr, H. R., Balss, K. M., Maryanoff, C. A., Maryanoff, B. E., Thrombogenic collagen-mimetic peptides: Self-assembly of triple helix-based fibrils driven by hydrophobic interactions (2008) Proc. Natl. Acad. Sci. U. S. A, 105, pp. 8513-8518

Leo, J. C., Elovaara, H., Brodsky, B., Skurnik, M., Goldman, A., The yersinia adhesin yada binds to a collagenous triple-helical conformation but without sequence specificity (2008) Protein Eng. Des. Sel, 21, pp. 475-484

Sacc, B., Fiori, S., Moroder, L., Studies of the local conformational properties of the cell-adhesion domain of collagen type IV in synthetic heterotrimeric peptides (2003) Biochemistry, 42, pp. 3429-3436

Sacc, B., Renner, C., Moroder, L., The chain register in heterotrimeric collagen peptides affects triple helix stability and folding kinetics (2002) J. Mol. Biol, 324, pp. 309-318

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Squeglia F, Ruggiero A, Berisio R
* Collagen degradation in tuberculosis pathogenesis: the biochemical consequences of hosting an undesired guest (27 visite)
Biochem J (ISSN: 1470-8728electronic, 0264-6021linking, 0264-6021print), 2018 Oct 11; 475(19): 3123-3140.
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Mcnitt DH, De Water LV, Marasco D, Berisio R, Lukomski S
* Streptococcal Collagen-like Protein 1 Binds Wound Fibronectin: Implications in Pathogen Targeting (20 visite)
Curr Med Chem (ISSN: 1875-533xelectronic, 0929-8673linking), 2018 Aug 31; N/D: N/D-N/D.
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Roviello GN
* Novel insights into nucleoamino acids: biomolecular recognition and aggregation studies of a thymine-conjugated L-phenyl alanine (81 visite)
Amino Acids (ISSN: 1438-2199electronic, 0939-4451linking), 2018 May 15; DOI10.1007/s00726-01: N/D-N/D.
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Roviello GN, Oliviero G, Di Napoli A, Borbone N, Piccialli G
* Synthesis, self-assembly-behavior and biomolecular recognition properties of thyminyl dipeptides (105 visite)
Arabian Journal Of Chemistry, 2018; inpress: N/D-N/D.
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Lukomski S, Bachert B, Squeglia F, Berisio R
* Collagen-like proteins of pathogenic streptococci (84 visite)
Mol Microbiol (ISSN: 1365-2958electronic, 0950-382xlinking), 2017; 103: 919-930.
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Bachert BA, Choi SJ, Snyder AK, Rio RV, Durney BC, Holland LA, Amemiya K, Welkos SL, Bozue JA, Cote CK, Berisio R, Lukomski S
* A Unique Set of the Burkholderia Collagen-Like Proteins Provides Insight into Pathogenesis, Genome Evolution and Niche Adaptation, and Infection Detection (124 visite)
Plos One (ISSN: 1932-6203electronic, 1932-6203linking), 2015 Sep 10; 10(9): e0137578-e0137578.
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Russo L, Palmieri M, Caso JV, Abrosca GD, Diana D, Malgieri G, Baglivo I, Isernia C, Pedone PV, Fattorusso R
* Towards understanding the molecular recognition process in prokaryotic zinc-finger domain (101 visite)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 1768-3254electronic), 2015; 91: 100-108.
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Balasco N, Pirone L, Smaldone G, Di Gaetano S, Esposito L, Pedone E, Vitagliano L
* Molecular recognition of Cullin3 by KCTDs: Insights from experimental and computational investigations (111 visite)
Biochim Biophys Acta (ISSN: 1570-9639, 0006-3002, 0925-4439), 2014 Jul; 1844(7): 1289-1298.
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Merlino A, Russo Krauss I, Castellano I, Ruocco MR, Capasso A, De Vendittis E, Rossi B, Sica F
* Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability (135 visite)
Biochim Biophys Acta (ISSN: 1570-9639, 0006-3002, 0925-4439), 2014 Mar; 1844(3): 632-640.
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Squeglia F, Bachert B, De Simone A, Lukomski S, Berisio R
* The crystal structure of the streptococcal collagen-like protein 2 globular domain from invasive M3-type group a streptococcus shows significant similarity to immunomodulatory HIV protein gp41 (95 visite)
J Biol Chem Journal Of Biological Chemistry (ISSN: 0021-9258, 1083-351x), 2014 Feb 21; 289(8): 5122-5133.
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Squeglia F, Bachert B, Romanò MF, Lukomski S, Berisio R
* Crystallization and preliminary X-ray crystallographic analysis of the variable domain of Scl2. 3, a streptococcal collagen-like protein from invasive M3-type Streptococcus pyogenes (104 visite)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2013 Sep; 69(9): 1023-1025.
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Roviello GN, Roviello V, Musumeci D, Pedone C
* Synthesis of a novel benzodifuran derivative and its molecular recognition of poly rA RNA (117 visite)
Biol Chem Biological Chemistry (ISSN: 1437-4315, 1431-6730), 2013 Sep; 394(9): 1235-1239.
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Berisio R, Vitagliano L
* Polyproline and triple helix motifs in Host-Pathogen recognition (282 visite)
Curr Protein Pept Sci (ISSN: 1389-2037), 2012 Dec; 13(8): 855-865.
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Ascione G, de Pascale D, De Santi C, Pedone C, Dathan NA, Monti SM
* Native expression and purification of hormone-sensitive lipase from Psychrobacter sp. TA144 enhances protein stability and activity (130 visite)
Biochem Biophys Res Commun (ISSN: 1090-2104, 0006-291x, 1090-2104electronic), 2012 Apr 13; 420(3): 542-546.
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Bonaccorso C, Ciadamidaro A, Sgarlata C, Sciotto D, Arena G, Zito V
* Molecular recognition of organic anions by a water-soluble calix[4]arene: Evidence for enthalpy-entropy compensation (80 visite)
Thermochim Acta (ISSN: 0040-6031), 2012 Feb 20; 530: 107-115.
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Vitagliano L, Berisio R, De Simone A
* Role of hydration in collagen recognition by bacterial adhesins (85 visite)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2011 May 4; 100(9): 2253-2261.
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Benetti F, Pastorino L, Attanasio F, Rizzarelli E, Legname G
* Insights into Prion Protein Stability (103 visite)
Prion (ISSN: 1933-6896), 2010 Jul; 4(3): N/D-N/D.
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Orsi S, De Capua A, Guarnieri D, Marasco D, Netti PA
* Cell recruitment and transfection in gene activated collagen matrix (108 visite)
Biomaterials (ISSN: 0142-9612, 1878-5905electronic, 0142-9612linking), 2010 Jan; 31(3): 570-576.
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Okuyama K, Baechinger HP, Mizuno K, Boudko S, Engel J, Berisio R, Vitagliano L
* Comment on Microfibrillar structure of type i collagen in situ by Orgel et al. (2006), Proc. Natl Acad. Sci. USA, 103, 9001-9005 (100 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2009 Sep; 65(9): 1007-1008.
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Vergara A, Castagnolo D, Carotenuto L, Vitagliano L, Berisio R, Sorrentino G, Gonzalez-ramirez L, Garcia-ruiz J, Zagari A
* Phase behavior and crystallogenesis under counter-diffusion conditions of the collagen-model peptide (Pro-Pro-Gly)10 (95 visite)
J Cryst Growth (ISSN: 0022-0248), 2009 Jan 1; 311(2): 304-309.
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Gioia M, Monaco S, Van Den Steen PE, Sbardella D, Grasso G, Marini S, Overall CM, Opdenakker G, Coletta M
* The Collagen Binding Domain of Gelatinase A Modulates Degradation of Collagen IV by Gelatinase (89 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009; 386(2): 419-434.
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De Simone A, Vitagliano L, Berisio R
* Role of hydration in collagen triple helix stabilization (113 visite)
Biochem Biophys Res Commun (ISSN: 0006-291x), 2008 Jul 18; 372(1): 121-125.
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Improta R, Berisio R, Vitagliano L
* Contribution of dipole-dipole interactions to the stability of the collagen triple helix (87 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2008 May; 17(5): 955-961.
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Berisio R, Granata V, Vitagliano L, Zagari A
* Imino acids and collagen triple helix stability: Characterization of collagen-like polypeptides containing Hyp-Hyp-Gly sequence repeats (128 visite)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2004 Sep 22; 126(37): 11402-11403.
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Berisio R, Granata V, Vitagliano L, Zagari A
* Characterization of Collagen-Like Heterotrimers: Implications for Triple-Helix Stability (113 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 682-688.
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Castagnolo D, Piccolo C, Carotenuto L, Vergara A, Zagari A
* Crystallization of the collagen-like polypeptide (PPG)10 aboard the International Space Station. 3. Analysis of residual acceleration-induced motion (111 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2003; 59(4): 773-776.
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Vergara A, Corvino E, Sorrentino G, Piccolo C, Tortora A, Carotenuto L, Mazzarella L, Zagari A
* Crystallization of the collagen-like polypeptide (PPG)(10) aboard the International Space Station. 1. Video observation (108 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2002 Oct; 58: 1690-1694.
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Berisio R, Vitagliano L, Vergara A, Sorrentino G, Mazzarella L, Zagari A
* Crystallization of the collagen-like polypeptide (PPG)10 aboard the International Space Station. 2. Comparison of crystal quality by X-ray diffraction (111 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2002 Oct; 58(10II): 1695-1699.
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Improta R, Mele F, Crescenzi O, Benzi C, Barone V
* Understanding the role of stereoelectronic effects in determining collagen stability. 2. A quantum mechanical/molecular mechanical study of (Proline-Proline-Glycine)n polypeptides (109 visite)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2002 Jul 3; 124(26): 7857-7865.
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Berisio R, Vitagliano L, Mazzarella L, Zagari A
* Recent progress on collagen triple helix structure, stability and assembly (90 visite)
Protein And Peptide Letters (ISSN: 0929-8665, 1875-5305), 2002 Apr; 9(2): 107-116.
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Berisio R, Vitagliano L, Mazzarella L, Zagari A
* Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3 (92 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2002 Feb; 11(2): 262-270.
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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 (104 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2001 Dec; 10(12): 2627-2632.
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Vitagliano L, Berisio R, Mazzarella L, Zagari A
* Structural bases of collagen stabilization induced by proline hydroxylation (98 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2001 Apr 15; 58(5): 459-464.
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Vitagliano L, Berisio R, Mazzarella L, Zagari A
* Erratum: Structural bases of collagen stabilization induced by proline Hydroxylation (Biopolymers (2001) 58: 5 (459-464)) (124 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2001; 59(6): 465-465.
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Berisio R, Vitagliano L, Sorrentino G, Carotenuto L, Piccolo C, Mazzarella L, Zagari A
Effects of microgravity on the crystal quality of a collagen-like polypeptide (87 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2000 Jan; 56(1): 55-61.
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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 (99 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2000; 56(1): 8-13.
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Kramer RZ, Vitagliano L, Bella J, Berisio R, Mazzarella L, Brodsky B, Zagari A, Berman HM
X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (104 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1998 Jul 24; 280(4): 623-638.
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Campagna T, Grasso G, Rizzarelli E, Vecchio G
L- and D-cysteine derivatives of β-cyclodextrin: Different molecular recognition properties of their copper(II) complexes for amino acids (114 visite)
Inorg Chim Acta (ISSN: 0020-1693), 1998; 275-276: 395-400.
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Bonomo RP, Pedotti S, Vecchio G, Rizzarelli E
Molecular Recognition of Amino Acids by Copper(II) Complexes of 6A, 6X-Diamino-6A, 6 X-dideoxy-β-cyclodextrin (X = B, C, D) (84 visite)
Inorg Chem (ISSN: 0020-1669, 1520-510x, 1520-510xelectronic), 1996 Nov 6; 35(23): 6873-6877.
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