A structurally driven analysis of thiol reactivity in mammalian albumins

Biopolymers

Volumn 95, Issue 4, 2011, Pages 278-285

  Spiga, Ottavia ^a   Summa, Domenico ^a   Cirri, Simone ^a   Bernini, Andrea ^a   Venditti, Vincenzo ^b   De Chiara, Matteo ^a   Priora, Raffaella ^a   Frosali, Simona ^a   Margaritis, Antonios ^a   Di Giuseppe, Danila ^a   Di Simplicio, Paolo ^a   Niccolai, Neri ^a  

^a UNIVERSITY OF SIENA   (Italy)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

atom depth analysis; homology modeling; MD simulations; protein structure and function; thiolation rate

Indexed keywords

DEPTH ANALYSIS; HOMOLOGY MODELING; MD SIMULATIONS; PROTEIN STRUCTURES; THIOLATION;

AMINO ACIDS; ATOMS; HYDROGEN BONDS; MAMMALS; MOLECULAR DYNAMICS; PROTEINS; REACTION RATES; REDOX REACTIONS; SULFUR;

STRUCTURAL ANALYSIS;

5,5' DITHIOBIS(2 NITROBENZOIC ACID); ALBUMIN; AMINO ACID; BOVINE SERUM ALBUMIN; DISULFIDE; SULFUR; THIOL;

ANIMAL EXPERIMENT; ARTICLE; ATOM; CHEMOREACTIVITY; CONTROLLED STUDY; CORRELATION ANALYSIS; DONOR; HUMAN; HYDROGEN BOND; MAMMAL; MOLECULAR DYNAMICS; MOLECULAR EVOLUTION; NONHUMAN; PORCINE ADENOVIRUS; PROTEIN STRUCTURE; RAT; SIMULATION; STRUCTURAL GENOMICS;

ALBUMINS; AMINO ACID SEQUENCE; ANIMALS; CATTLE; DISULFIDES; DITHIONITROBENZOIC ACID; HUMANS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RATS; SEQUENCE ALIGNMENT; SULFHYDRYL COMPOUNDS;

BOVINAE; MAMMALIA; RATTUS; SUS;

EID: 79551523391     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.21577     Document Type: Article

References (37)

1. Hankins, J., J Infus Nurs 2006, 29, 260-265.
2. Baker, M. E., J Endocrinol 2002, 175, 121-127.
3. Mansoor, M. A., Svardal, A. M., Schneede, J., Ueland, P. M., Clin Chem 1992, 38, 1316-1321.
4. Okazaki, T., Okudaira, N., Ishii, N., Yotsuyanagi, H., Nagai, T., Tokudome, S., Fujioka, T., Takahashi, S., Zoolog Sci 2008, 25, 172-177.
5. Lewis, S. D., Misra, D. C., Shafer, J. A., Biochemistry 1980, 19, 6129-6137.
6. Narazaki, R., Hamada, M., Harada, K., Otagiri, M., Pharm Res 1996, 13, 1317-1321.
7. Pedersen, A. O., Jacobsen, J., Eur J Biochem 1980, 106, 291-295.
8. Peters, T. J., All About Albumin: Biochemistry, Genetics, and Medical Applications; Academic Press: San Diego, 1996.
9. Levi, V., Gonzalez Flecha, F. L., Biochim Biophys Acta 2002, 1599, 141-148.
10. Pirisino, R., Di Simplicio, P., Ignesti, G., Bianchi, G., Barbera, P., Pharmacol Res Commun 1988, 20, 545-552.
11. Stewart, A. J., Blindauer, C. A., Berezenko, S., Sleep, D., Tooth, D., Sadler, P. J., FEBS J 2005, 272, 353-362.
12. Gryzunov, Y. A., Arroyo, A., Vigne, J. L., Zhao, Q., Tyurin, V. A., Hubel, C. A., Gandley, R. E., Vladimirov, Y. A., Taylor, R. N., Kagan, V. E., Arch Biochem Biophys 2003, 413, 53-66.
13. Summa, D., Spiga, O., Bernini, A., Venditti, V., Priora, R., Frosali, S., Margaritis, A., Di Giuseppe, D., Niccolai, N., Di Simplicio, P., Proteins 2007, 69, 369-378.
14. Priora, R., Coppo, L., Margaritis, A., Di Giuseppe, D., Frosali, S., Summa, D., Heo, J., Di Simplicio, P., Toxicol Appl Pharmacol 2010, 242, 333-343.
15. Sengupta, S., Chen, H., Togawa, T., DiBello, P. M., Majors, A. K., Budy, B., Ketterer, M. E., Jacobsen, D. W., J Biol Chem 2001, 276, 30111-30117.
16. Ellman, C. L., Arch Biochem Biophys 1959, 82, 70-77.
17. Townsend, J. P., Lopez-Giraldez, F., Friedman, R., J Mol Evol 2008, 67, 437-447.
18. Felsenstein, J., Cladistics 1989, 5, 164-166.
19. Valdar, W. S., Proteins 2002, 48, 227-241.
20. Baker, D., Sali, A., Science 2001, 294, 93-96.
21. Sugio, S., Kashima, A., Mochizuki, S., Noda, M., Kobayashi, K., Protein Eng 1999, 12, 439-446.
22. Gilbert, H. F., Methods Enzymol 1995, 251, 8-28.
23. Sessions, R. B., Gibbs, N., Dempsey, C. E., Biophys J 1998, 74, 138-152.
24. Dastidar, S. G., Mukhopadhyay, C., Phys Rev E 2003, 68, 021921.
25. Varrazzo, D., Bernini, A., Spiga, O., Ciutti, A., Chiellini, S., Venditti, V., Bracci, L., Niccolai, N., Bioinformatics 2005, 21, 2856-2860.
26. Ogasawara, Y., Namai, T., Togawa, T., Ishii, K., Biochem Biophys Res Commun 2006, 340, 353-358.
27. Ueno, Y., Mio, M., Sato, C., Mio, K., J Electron Microsc (Tokyo) 2007, 56, 103-110.
28. Sadler, P. J., Tucker, A., Eur J Biochem 1993, 212, 811-817.
29. Thompson, J. D., Higgins, D. G., Gibson, T. J., Nucleic Acids Res 1994, 22, 4673-4680.
30. Guex, N., Peitsch, M. C., Electrophoresis 1997, 18, 2714-2723.
31. Canutescu, A. A., Shelenkov, A. A., Dunbrack, R. L., Jr., Protein Sci 2003, 12, 2001-2014.
32. Van Der Spoel, D., Lindahl, E., Hess, B., Groenhof, G., Mark, A. E., Berendsen, H. J., J Comput Chem 2005, 26, 1701-1718.
33. Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R., Thornton, J. M., J Biomol NMR 1996, 8, 477-486.
34. Wiederstein, M., Sippl, M. J., Nucleic Acids Res 2007, 35, W407-W410.
35. Castrignano, T., De Meo, P. D., Cozzetto, D., Talamo, I. G., Tramontano, A,. Nucleic Acids Res 2006, 34, D306-309.
36. Daura, X., Gademann, K., Jaun, B., Seebach, D., van Gunsteren, W. F., Mark, A. E., Angew Chem Int Ed 1999, 38, 236-240.
37. Koradi, R., Billeter, M., Wuthrich, K., J Mol Graph 1996, 14, 51-55, 29-32.