Determination of amino acid pairs sensitive to variants in human copper-transporting ATPase 2

Biochemical and Biophysical Research Communications

Volumn 319, Issue 1, 2004, Pages 27-31

  Wu, Guang ^a   Yan, Shaomin ^a  

^a DreamSciTech Consulting   (China)

Author keywords

Amino acid; ATPase; Genetic Stability; Modeling; Protein; Wilson disease

Indexed keywords

ADENOSINE TRIPHOSPHATASE; AMINO ACID; COPPER; COPPER EXPORTING ADENOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; ARTICLE; MISSENSE MUTATION; PRIORITY JOURNAL; PROBABILITY;

ADENOSINE TRIPHOSPHATASES; AMINO ACIDS; CATION TRANSPORT PROTEINS; COMPUTATIONAL BIOLOGY; HUMANS; MODELS, STATISTICAL; MUTATION; MUTATION, MISSENSE; VARIATION (GENETICS);

EID: 2442707531     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.04.143     Document Type: Article

References (19)

1. Linder M.C. Biochemistry of copper. Frieden E. Biochemistry of the Elements. 1991;Plenum, New York
2. Orth M., Schapira A.H.V. Mitochondria and degenerative disorders. Am. J. Med. Genet. 106:2001;27-36
3. Mercer J.F.B. The molecular basis of copper-transport diseases. Trends Mol. Med. 7:2001;64-69
4. Yamaguchi Y., Heiny M.E., Gitlin J.D. Isolation and characterisation of a human liver cDNA as a candidate gene for Wilson disease. Biochem. Biophys. Res. Commun. 197:1993;271-277
5. Murata Y., Yamakawa E., Iizuka T., Kodama H., Abe T., Seki Y., Kodama M. Failure of copper incorporation into ceruloplasmin in the Golgi apparatus of LEC rat hepatocytes. Biochem. Biophys. Res. Commun. 209:1995;349-355
6. Danks D.M. Copper deficiency in humans. Annu. Rev. Nutr. 8:1988;235-257
7. Strausak D., Mercer J.F.B., Dieter H.H., Stremmel W., Multhaup G. Copper in disorders with neurological symptoms: Alzheimer's, Menkes, and Wilson diseases. Brain Res. Bull. 55:2001;175-185
8. Loudianos G., Gitlin J.D. Wilson's disease. Semin. Liver Dis. 20:2000;353-364
9. Rideout W.M., Coetzee G.A., Olumi A.F., Jones P.A. 5-Methylcytosine as an endogenous mutagen in human LL receptor and p53 genes. Science. 249:1990;1288-1290
10. PROSITE: a dictionary of protein sites and patterns user manual. Available from 〈http://www.expasy.ch/prosite/〉
11. Montesano R., Hainaut P., Wild C.P. Hepatocellular carcinoma: from gene to public health. J. Natl. Cancer Inst. 89:1997;1844-1851
12. Hainaut P., Pfeifer G.P. Patterns of p53 G. → T transversions in lung cancers reflect the primary mutagenic signature of DNA-damage by tobacco smoke Carcinogenesis. 22:2001;367-374
13. Ory K., Legros Y., Auguin C., Soussi T. Analysis of the most representative tumour-derived p53 mutants reveals that changes in protein conformation are not correlated with loss of transactivation or inhibition of cell proliferation. EMBO J. 13:1994;3496-3504
14. Forrester K., Lupold S.E., Ott V.L., Chay C.H., Band V., Wang X.W., Harris C.C. Effects of p53 mutants on wild-type p53-mediated transactivation are cell type dependent. Oncogene. 10:1995;2103-2111
15. Aas T., Borresen A.L., Geisler S., Smith-Sorensen B., Johnsen H., Varhaug J.E., Akslen L.A., Lonning P.E. Specific p53 mutations are associated with de novo resistance to doxorubicin in breast cancer patients. Nat. Med. 2:1996;811-814
16. Bairoch A., Apweiler R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 2000. Nucleic Acids Res. 28:2000;45-48
17. Wu G., Yan S.M. Randomness in the primary structure of protein: methods and implications. Mol. Biol. Today. 3:2002;55-69
18. Wu G., Yan S.M. Prediction of presence and absence of two- and three-amino-acid sequence of human monoamine oxidase B from its amino acid composition according to the random mechanism. Biomol. Eng. 18:2001;23-27
19. Feller W. third ed. An Introduction to Probability Theory and its Applications. vol. I:1968;Wiley, New York