Идентификация молекулярной формы церулоплазмина, локализованной в митохондриях крысы

Список литературы

1. Abe Y. Shodai Т., Muto Т. Mihara К., Torii Н&bdquo- Nishikawa S., Endo Т., Kohda D. Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20 // Cell. 100: 551−560. 2000-
2. Adman E.T. and Murphy M.E.P. Copper nitrite reductase // Handbook of Metalloproteins. 2: 1381−1390.2001:
3. Adman E.T. Godden J.W. and Turley S. The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2 bound and with type II copper depleted // J. Biol. Chem. 270: 27 458−27 474. 1995-
4. Ahting U. Thun С. Hegerl R. Турке D" Nargang F.E., Neupert W" Nussberger S. The TOM core complex: the general protein import pore of the outer membrane of mitochondria // J. Cell. Biol., 147: 959−968. 1999-
5. Alexandre G. and Zhulin l.B. Laccases are widespreadin bacteria // Trends Biotechnol. 18: 41², 2000-
6. Altschul S.F. Madden T.L. Schaffer A.A. Zhang J. Zhang Z, Miller W. Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs // Nucleic Acids Res. 25: 3389−3402. 1997:
7. Askwith C. Eide D. Van Ho A. Bernard P. S., Li L, Davis-Kaplan S. Sipe D.M. and Kaplan J. The Fet3p gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake // Cell, 76: 403−410, 1994:
8. Askwith C. Kaplan J. Iron and copper transport in yeast and its relevance to human disease. //Trends Biochem Sci., 23(4): 135−138. 1998-
9. Bannai H. Tamada К. Maruyama O., Nakai K. Miyano. S. Extensive feature detection of N-terminal protein sorting signals // Bioinformatics, 18 (2): 298−305,2002-
10. Barnes G. Frieden E. Ceruloplasmin receptors of erytrocytes // Biochem. Biophys. Res. Commun. 125: 157−162, 1984-
11. Bauer M.F., Sirrenberg С., Neupert W. Brunner M. Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria //Cell, 87: 33−41, 1996-
12. Bielli P. Calabrese L. Structure to function relatioships in ceruloplasmin: a «moonlighting» protein // CMLS, Cell. Mol. Life Sci., 59: 1413 1427, 2002-
13. Blumenthal T. Trans-splicing and polycistronic transcription in Caenorbabditis elegans I/ Trends Genet., 11(4): 132−136, 1995-
14. Blumenthal T. Trans-splicing and polycistronic transcription in Caenorhabditis elegans//TIG, 11: 132−136, 1995-
15. Bolliger L, Junne Т., Schatz G. Lithgow T. Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria // EMBO J., 14: 6318−6326,1995-
16. Borjigin J., Payne A.S. Deng J., Li X. Wang M.M. Ovodenko В., Gitlin J.D. Snyder S.H. A novel pineal night-specific ATPase encoded by the Wilson disease gene //The Journal of Neuroscience, 19(3): 1018−1026. 1999-
17. Brennicke A., March/elder A. Binder S. RNA editing // FEMS Microbiology Reviews 23: 297−316, 1999-
18. Brix J., Dietmeier K. Pfanner N. Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70 // J. Biol. Chem., 272: 20 730−20 735, 1997-
19. Brix J., Ziegler G.A., Dietmeier K., Schneider-Mergener J. Schulz G.E., Pfanner N. The mitochondrial import receptor Tom70: identification of a 25kDa core domain with a specific binding site for preproteins // J. Mol. Biol., 303:479−488, 2000-
20. Calabrese L, Muski G. Molecular properties of ceruloplasmin from different species. //In: Multi-copper oxidases, Academic Press, N.-Y., 307−354, 1997-
21. Cartharius K., Freeh K., Grote K., Klocke В., Haltmeier M, Klingenhoff A., Frisch M., Bayerlein M., Werner T. Matlnspector and beyond: promoter analysis based on transcription factor binding sites // Bioinformatics, 21 (13): 2933−2942, 2005-
22. Ceciliani F. Giordano A., Spagnola V. The systemic reaction during inflamentation: the acute phase proteins // Protein and Peptide letters, 9: 211−223,2002-
23. Claros M.G. Vincens P. Computational method to predict mitochondrially imported proteins and their targeting sequences // Eur. J. Biochem. 241: 779 786, 1996-
24. Claus H. Laccases and their occurrence in prokaryotes // Arch. Microbiol., 179: 145−150, 2003-
25. Claus H. Laccases: structure, reactions, distribution // Micron, 35: 93−96, 2004-
26. Cooper C.E. Nitric oxide and cytochrome oxidase: substrate, inhibitor or effector? //TIBS, 27: 33−39, 2002-
27. Cousin R.J. Absorption, transport, and hepatic metabolism of copper and tine: special reference to metallothionein and ceruloplasmin // Physiol.Rev., 65 (2): 238−309, 1985-
28. Craig E.A., Voisine C., Schilke B. Mitochondrial iron metabolism in the yeast Saccharomyces cerevisiae II Biol. Chem., 380: 1167−1173,1999-
29. Daimon M., Yamatani K., Igarashi M, Fukase N. Kawanami Т., Kato Т., Sasaki H. Fine structure of human ceruloplasmin gene // Biochem. Biophys. Res. Commun., 208: 1028−1035,1995-
30. Danzeisen К. Ponnambalam S. Lea R.G. Page K. Gambling L. McArdle H.J. The effect of ceruloplasmin on iron release from placental (BeWo) cells- evidence for an endogenous Cu oxidase // Placenta. 21: 805−812. 2000-
31. Dekker P.J., Ryan M.T. Brix J. Muller H" Honlinger A. Pfanner N. Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex // Mol. Cell Biol. 18: 6515−6524, 1998-
32. Donley S.A. Ilagan B.J. Rim H. Linder M.C. Copper transport to mammary gland and milk during lactation in rats // Am. J. Physiol. Endocrinol. Metab. 283: E667-E675,2002-
33. Ellis M.J. Dodd F.E. Sawers G. Eady R.R. and Hasnain S.S. Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu // J. Mol. Biol., 328: 429 438, 2003-
34. Emanuelsso .0. Nielsen H. Brunak S. von Heijne G. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence // J. Mol. Biol. 300: 1005−1016. 2000-
35. Emtage J.L.T., Jensen R.E. MAS6 encodes an essential inner membrane component of the yeast mitochondrial protein import pathway // J. Cell Biol., 122: 1003−1012, 1993-
36. Endo Т., Kohda D. Functions of outer membrane receptors in mitochondrial protein import// Biochim. Biophys. Acta, 1592: 3−14, 2002-
37. Felsenstein J. PHYLIP (Phylogeny Inference Package) version З. баЗ // Department of Genome Sciences, University of Washington, Seattle, 2002-
38. Fleming R.E. Gitlin J.D. Primary structure of rat ceruloplasmin and analisis of tissue specific gene expression during development // J.Biol.Chem., 265 (13):7701−7709, 1990-
39. Fortna R.R., Watson H. A, Nyquist S.E. Glycosyl phosphatidylinositol-anchored ceruloplasmin is expressed by rat Sertoli cells and is concentrated in detergent-insoluble membrane fractions // Biol. Reprod. 61 (4): 1042−9, 1999-
40. Francis C.A. and Tebo B.M. Enzymatic manganese (II) oxidation by metabolically dormant spores of diverse Bacillus species // Appl. Environ. Microbiol., 68: 874−880, 2002-
41. Fransson L-A. Glypicans // The International Journal of Biochemistry & Cell Biology, 35: 125−129, 2003-
42. Frantz C, Ebel C., Paulus F., Imbaut P. Characterization of trans-splicing in Euglenoids //Curr. Genet., 37: 349−355, 2000-
43. Frazer D.M., Vulpe C., McKie A.T., Wilkins S.J. Trinder D., Cleghom G.J., Anderson G.J. Cloning and gastrointestinal expression of rat hephaestin: relationship to other iron transport proteins // Am. J. Physiol., 284 (4): 9, 2001-
44. Frieden E. Ceruloplasmin: a multi-functional metalloprotein of vertebrate plasma. In: Biological roles of copper // Excepta Medica, 93−124, 1980-
45. Funfschilling {/., Rospert S. Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria // Mol. Biol. Cell, 10: 3289−3299, 1999-
46. Gaitskhoki V.S., L’vov V.M. Monakhov N.K. Puchkova L.V., Schwartzman A.L. Frolova LJu., Skobeleva N.A., Zagorski W., Neifakh S.A. Intracellular distribution of rat-liver polyribosomes synthesizing coeruloplasmin // Eur J Biochem. 115(1): 39−44, 1981:
47. Gaitskhoki V.S. L’vov V.M. Puchkova LV. Schwartzman A.L. Neifakh S.A. Highly purified ceruloplasmin messenger RNA from rat liver. Physico-chemical and functional characteristics // Mol. Cell Biochem., 35(3): 171 182.1981:
48. Gibbs J.S. Malide D. Hornung F. Bennik J.R. Yewdell J. W. The enfluenza A virus PB1-F2 protein targets the inner mitochondrial membrane via a predicted basic amphipathic helix that disrupts mitochondrial function // J. Virol., 77: 7214−7224. 2003:
49. Gitlin J.D. Aceruloplasminemia // Pediatr Res., Sep., 44(3): 271 276, 1998:
50. Gitlin J.D. Transcriptional regulation of ceruloplasmin gene expression during inflammation // J. Biol. Chem., 263: 6281−6287, 1988:
51. Gott J.M. Expanding genome capacity via RNA editing // Comptes Rendus Biologies Molecular biology and genetics, 326: 901−908, 2003:
52. Gutteridge J.M.C. Halliwell B. Free radicals and antioxidants in the year 2000: a historical look to the future // Ann. New York Acad. Sci. 899: 136 147, 2000:
53. Harris E.D. Cellular copper transport and metabolism //Annu. Rev. Nutr. 2000. V. 20. P. 291-
54. Harris Z.L. Takahashi Y., Miyajima H., Serizawa M. MacGillivray /?. Gitlin J.D. Aceruloplaminemia: molecular characterization of this disoder of iron metabolism// Proc. Natl. Acad. Sci. USA, 92: 2539−2543.1995-
55. Harvey L.J., Dainty J.R., Hollands W.J.Bull V.J., Beattie J.H., Venelinov T. L, Hoogewerff J.A., Davies I.M., Fainveather-Tait S.J. Use of mathematical modeling to study copper metabolism in humans // Am. J. Clin. Nutr. 81: 807−813,2005-
56. Hellman N.E. Kono S. Miyajima N. Gitlin J.D. Biochemical analysis of a missense mutation in aceruloplasminemia // J. Biol. Chem., 277: 1375−1380, 2002-
57. Holmberg C.G. On the presence of a laccase-like enzyme in serum and its relation to the copper in serum // Acta. Physiol. Scand., 8- 227−229, 1944-
58. Holmberg C.G. Laurell C.B. Investigations in serum copper II // Acta.Chem.Scand. 2: 550−556. 1948-
59. Hortnagel K. Prokisch H. Meitinger T. An isoform of hPANK2. deficient in pantothenate kinase-associated neurodegeneration. localizes to mitochondria // Human Molecular Genetics, 12(3): 321−327,2003-
60. Horton T.L. Landweber LF. Rewriting the information in DNA: RNA editing in kinetoplastids and myxomycetes // Current Opinion in Microbiology, 5: 620−626. 2002-
61. Horwich A.L. Kalousek F. Mellman /. Rosenberg LE. A leader peptide is sufficient to direct mitochondrial import of a chimeric protein // EMBO J., 4: 1129−1135,1985-
62. Huffman D. L, O’Halloran T.V. Function, structure, and mechanism of intracellular copper trafficking proteins // Annu. Rev. Biochem. 70: 677 701.2001:
63. Hunter, W.M. Greenwood. F.C. Standardization of the chloramin-T method of protein iodination // Nature, 194: 495−496, 1962-
64. Hurley L.S., Keen C.L. Lonnerdal B.O. Copper in fetal and neonatal development // Hunt Ciba Foundation Symp. 227−245.1980-
65. Hurt E.C. Pesold-Hurt В. Schatz G. The cleavable prepiece of an imported mitochondrial protein is sufficien to direct cytosolic dihydrofolate reductase into the mitochondrial matrix // FEBS Lett., 178: 306−310, 1984-
66. Jalkanen S. Salmi M. Cell surface monoamine oxidases: enzymes in search of a function // EMBO J., 20: 3893−3901. 2001:
67. Janger J. L, Shimizu. Gitlin J.D. Tissue-specific synthesis of the ceruloplasmin by mamary glands of the rat //Biochem. J. 280 (3): 671−677, 1977:
68. Jeffery C.J. Moonlighting proteins // TiBS. 8−11. 1999:
69. Jeong Y. S., David S. GPI-anchored Ceruloplasmin is required for iron efflux from cells in the central nervous system // J. Biol. Chem., 278:. 2 714 427 148,2003-
70. Juan S.H. Guo J.H. Aust S.D. Loading of iron into recombinant rat liver ferritin heteropolymers by ceruloplasmin // Arch. Biochem. Biophys., 341(2): 280−286. 1997:
71. Kang P.J. Ostermann J. Shilling J., Neupert W. Craig E.A. Pfanner N. Requirement for Hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins//Nature, 348: 137−143, 1990-
72. Karlin K.D. Metalloenzymes. structural motif, and inorganic models // Science. 261: 701−707, 1993-
73. Kerscher O. Sepuri N.B., Jensen R.E. Timl8p is a new component of the Tim54p-Tim22p translocon in the mitochondrial inner membrane // Mol. Biol. Cell, 11: 103−116,2000-
74. Klomp L.W., Farhangrazi Z.S., Dugan LL, Culotta V. Gitlin J.D. Ceruloplasmin gene expression in the murine central nervous system // J. Clin. Invest. 98: 207−215, 1996-
75. Knox C., Sass E., Neupert W. Pines. O. Import into mitochondria, folding and retrograde movement of fumarase in yeast // J. Biol. Chem., 273: 25 587−25 593. 1998-
76. Komiya Т. Rospert S. Koehler C. Looser R. Schatz G. Mihara K. Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesis II EMBO J., 17- 3886−3898. 1998-
77. Koschinsky M.L. Funk W.D., Van Oost B.A. MacGillivray R.T. Complete cDNA seguence of human preceruloplasmin //Proc. Natl. Acad. Sci. USA, 83:5086−5090. 1986-
78. Kunapuli S.P. Singh H. Singh P. Kumar A. Ceruloplasmin gene expression in human cancer cells // Life Sci. 40: 2225−2228.1987:
79. Kunkele К.P., Heins S., Dembowski M., Nargang F.E., Benz R-, Thieffry M., Walz J., Lill R., Nussberger S., Neupert IV. The preprotein translocation channel of the outer membrane of mitochondria // Cell, 93: 1009−1019, 1998-
80. La Fontaine S., Quinn J.M., Nakamoto S.S., Page M.D., Gohre V., Moseley J.L., Kropat J. and Merchant S. Copper-Dependent Iron Assimilation Pathway in the Model Photosynthetic Eukaryote Chlamydomonas reinhardtii II Eukaryotic cell, 1(5): 736−757, 2002-
81. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 // Nature, 227: 680−685, 1970-
82. Lange H. Kispal G., Lill R. Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria // J. Biol. Chem., 274: 18 989−18 996, 1999-
83. Lee C.M. Sedman J. Neupert W. Stuart R.A. The DNA helicase. Hmilp, is transported into mitochondria by a C-terminal cleavable targeting signal И J. Biol. Chem., 274: 20 937−20 942, 1999-
84. Leuenberger D., Bally N.A., Schatz G. Koehler C.M. Different import pathways through the mitochondrial intermembrane space for inner membrane proteins // EMBO J., 18: 4816−4822, 1999-
85. Levi S., Corsi В., Bosisio M., Invernizz г., Volz A., Sanford D., Arosio P., Drysdale J. A human mitochondrial ferritin encoded by an intronless gene // JBIC, 270(27): 24 437−24 440, 2001-
86. Lill R. Kispal G. Maturation of cellular Fe-S proteins: an essential function of mitochondria // TIBS, 25: 352−356,2000-
87. Linder M.C. Copper and genomic stability in mammals // Mutation Res. V. 475(1): 141,2001-
88. Lockhart P.J., Mercer J.F.B. Cloning and expression analysis of the sheep ceruloplasmin cDNA // Gene, 236: 251−257, 1999-
89. Lohret T.A., Jensen R.E., Kinnally K. W. Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel // MCC. J. Cell Biol. 137: 377−386. 1997-
90. Lowry O.H., Rosebrough N.Y., Fair A.L. Randall R.I. Protein measurement with the Folin phenol reagent // J. Biol. Chem., 193: 265. 1951.
91. Lutsenko S. Cooper M.J. Localization of the Wilson’s disease protein product to mitochondria // Proc Natl Acad Sci USA- 95(11): 6004−6009. 1998:
92. L’vovskaia E.I. Gavriliuk T.A., Mokhova S.V. In vitro effect of BITO preparation, ceruloplasmin. transferrin, and essentiale on the intensity of lipid peroxidation during thermal injury // Vopr. Med. Khim., 42(2): 125−7, 1996-
93. Maltais D. Desroches D. Aouffen M. Mateescu M.A. Wang R. Paquin J. The blue copper ceruloplasmin induces aggregation of newly differentiated neurons: a potential modulator of nervous system organization // Neuroscience, 121: 73−82, 2003-
94. Martin J. Mahlke K. Pfanner N. Role of an energized inner membrane in mitochondrial protein import: Av|/ drives the movement of presequenees // J. Biol. Chem., 266: 18 051−18 057,1991:
95. Mason K.E. A conspectus of research on copper metabolism and requirements of man.//J.Nutr., 109(11): 1979−2066. 1979-
96. Mazumder В. Seshadri V. Fox P.L. Translational control by the 3'-UTR: the ends specify the means // TRENDS in Biochemical Sciences. 28(2), 9198.2003-
97. McArdle H.J. Danks D.M. Secretion of copper 64 into breast milk following intravenous injection in a human subject // J. Trace Elements Exp. Med. 4: 81−84, 1991-
98. McArdle H.J. Danzeisen R. Fosset C. Gambling L The role of the placenta in iron status and fetal outcome // BioMetal. 16: 161−167, 2003:
99. Ш. Menkes J.H. Alter M., Steigleder G., Wekley D.R., Sung J.H. A sex-linked recessive disoder with retardation of growth, pecular hair and focal cerebral and cerebellar degeneration // Pediatrics, 29: 764−779. 1962-
100. Mertz W. Trace elements // Science. 211: 315−319. 1985-
101. Messerschmidt A. Ascorbate oxidase // Handbook of Metalloproteins. 2: 1345−1358.2001:
102. Messerschmidt A. Huber R. The blue oxidases, ascorbate oxidase, Iaccase and ceruloplasmin. Modelling and structural relationships // Eur. J. Biochem. 187: 341−352,1990-
103. Mitchell P.J. Tjian R. Transcriptional regulation in mammalian cells by sequence-specific DNA binding proteins // Science, 245: 371−378, 1989-
104. Mittal В. Doroudchi M.M. Jeong S.Y. Patel. B.N. David S. Expression of a membrane-bound form of the ferroxidase ceruloplasmin by leptomeningeal cells // GLIA. 41: 337−346,2003-
105. Miyajima H. Takahashi Y. Kono S. Aceruloplasminemia. an inherited disorder of iron metabolism // BioMetals Kluwer Academic Publishers. Printed in the Netherlands, 16: 205−213. 2003.
106. Mukhopadyay C.K., Attien Z.K., Fox P. L Role of ceruloplasmin in cellular iron uptake // Science. 279: 714−717.1998-
107. Musci G. Fraterrigo T.Z.L., Calabrese L. McMillin D.R. On the lability and functional significance of the type I copper pool in ceruloplasmin // JBIC, 4: 441−446. 1999-
108. Muski G., DiMarco S. Bonaccorsi di Patti M.C., Calabrese L Interaction of nitric oxide with ceruloplasmin lacking an EPR-detectable type 2 copper // Biochemistry, 30: 9866−9872, 1991:
109. Nakamura K, Kawabata T. Yura K. Go N. Novel types of two-domain multi-copper oxidases: possible missing links in the evolution // FEBS Lett., 553(3): 239−244, 2003-
110. Nakamura K, Go N. Function and molecular evolution of multicopper blue proteins // Cell. Mol. Life Sci., Epub ahead of print. 2005-
111. Nakamura K. Kawabata Т., Yura K. and Go N. Novel types of two-domain multi-copper oxidases: possible missing links in the evolution // FEBS Lett., 553: 239−244,2003-
112. Neifakh S.A. Monakhov N.K. Shaposhnikov A.M. Zubzhitski Yu.N. Localization og ceruloplasmin biosynthesis in human and monkey liver // Experientia, 25: 337−344,1969.
113. Nersissian A.M. and Shipp E.L. Blue copper-binding domains // Adv. Prot. Chem., 60: 271−340, 2002−125.0'Halloran T.V. Transition metals in control of gene expression // Science, 261: 715−724, 1993-
114. Okamoto N. Wada S. Oga Т. Kawabata Y. Baba Y. Habu D. Takeda Z. Wada Y. Hereditary ceruloplasmin deficiency with hemosiderosis // Hum. Genet., 97 (6):755−8, 1996-
115. Olivares M., Uauy R. Copper as an essential nutrient // Am. J. Clin. Nutr., 63(5): 7915−7965, 1996-
116. Omoto E" Tavassoli M. Purification and partial characterization of ceruloplasmin receptors from rat liver endothelium // Arch. Biochem. Biophys. 282 (1): 34−8,1990:
117. Orrenius S., Zhivotovsky В. Nicotera P. Regulation of cell death: the calcium-apoptosis link. Nature Reviews. //Molecular Cell Biology, 4: 552 565, 2003-
118. Owen C.A. Wilson’s disease: the etiology, clinical aspects and treatment of inhereted copper to toxicosis // N.N.: Noges publications, pp. 539. 1981-
119. Patel B.N. David S. A novel glycosylphosphatidylinositol-anchored form of ceruloplasmin is expressed by mammalian astrocytes // J. Biol. Chem., 272: 20 185−20 190,1997:
120. Patel B.N. Dunn R.J., David S. Alternative RNA splicing generates a glycosylphosphatidylinositol-anchored form of ceruloplasmin in mammalian brain //J. Biol. Chem., 275: 4305−4310. 2000-
121. Patel B.N. Dunn R.J., Jeong S.Y. Zhu Q. Julien J.-P., David S. Ceruloplasmin regulates iron levels in the CNS and prevents free radical injury // J. Neuroscience. 22: 6578−6586. 2002-
122. Репа M. O. Jaekwon. Thiele D.J. A Delicate Balance: Homeostatic Control of Copper Uptake and Distribution // J. Nutr., 129: 1251−1260,1999:
123. Pfanner N, Geissler A. Versatility of the mitochondrial protein import machinery // Nat. Rev. Mol. Cell. Biol., 2(5): 339−349,2001-
124. Platonova N.A., Vasin A.V., Klotchenko S.A., Tsymbalenko N.V., Puchkova LV. The revelation of expressing region in the processed ceruloplasmin gene in human genome by biocomputational and biochemical methods // Biophys Cheat., 115(2−3): 247−25, 2005-
125. Ponka P. Cellular iron metabolism // Kidney International, 55: 2−11, 1999-
126. Pyle A.M. Ribozymes: a distinct class of metalloenzymes. // Science, 261: 709−714, 1993-
127. Ul.Rae T.D., Schmidt P.J., Pufahl R.A. et al. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase // Science, 284: 805−808, 1999
128. Raju K.S., Alessandri G., Ziche M., Gullano P.M. Ceruloplasmin, copper ions, and angiogenesis //J. Natl. Cancer Inst., 69: 1183- 1188, 1982-
129. Reid G.A., Schatz G. Import of proteins into mitochondria: extramitochondrial pools and post-translational import of mitochondrial protein precursors in vivo И J. Biol. Chem., 257: 13 062−13 067, 1982-
130. Reilly C.A., Aust S.D. Iron loading into ferritin by an intracellular ferroxidase//Arch. Biochem. Biophys., 1, 359(l):69−76, 1998-
131. Rock С.О., Calder R.B. Karim M.A., Jackowski S. Pantothenate kinase regulation of the intracellular concentration of coenzyme // A. J. Biol. Chem., 275: 1377−1383,2000-
132. Ryan T.P. Grover T.A., Aust S.D. Rat ceruloplasmin: resistance to proteolysis and kinetic comparison with human ceruloplasmin // Arch. Biochem. Biophys. 293: 1−8, 1992-
133. Ryden L. Ceruloplasmin is a single peptide chain // Eur. J. Biochem., 26: 380−386.1972-
134. Ryden L.G. and Hunt L.T. Evolution of protein complexity: the blue copper-containing oxidases and related proteins // J. Mol. Evol., 36: 41−66, 1993-
135. Salzer J. Lovejoy L, Under M.C., Rosen C. Ran-2, a glial lineage marker, is a GPI-anchored form of ceruloplasmin // J. Neurosci. Res., 54: 147 157, 1998-
136. Sato M. Gitlin J.D. Mechanisms of copper incorporation during the biosynthesis of human ceruloplasmin // J. Biol. Chem., 266 (8): 5128−5134, 1991:
137. Schapira A.H.V. Mitochondrial disorders // Biochim. Biophys. Acta. 1410: 99−102, 1999-
138. Scheffler I.E. Mitochondria // John Wiley & Sons NY. pp384. 1999-
139. Schwartsman A. L, Gaitskhoki V.S., L’vov V.M., Nosikov V.V., Braga E.M. Frolova L.Y., Skobleva N.A., Kisselev L.L., Neifakh S.A. Complex molecular structure of the gene coding for rat ceruloplasmin // Gene, 11: 1−10, 1980-
140. Seeburg P.H., Hartner J. Regulation of ion channel/neurotransmitter receptor function by RNA editing // Current Opinion in Neurobiology, 13: 279−283,2003-
141. Shim H., Leah Harris Z. Genetic Defects in Copper Metabolism // J. Nutr. 133: 1527−1531,2003-
142. Sirrenberg С. Bauer M.F. Guiard В., Neupert W. Brunner M. Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22 //Nature, 384: 582−585, 1996-
143. Skinner M.K. Griswold M.D. Sertoli cells synthesize and secrete a ceruloplasmin-like protein // Biol. Reprod. 28: 1225−1229, 1983-
144. Skulachev V.P. Cytochrome с in the apoptotic and antioxidant cascades // FEBS Letters, 423: 275−280, 1998:
145. Sollner Т. Rassow J., Wiedmann M. Schlossmann J. Keil P., Neupert W., Pfanner N. Mapping of the protein import machinery in the mitochondrial outer membrane by crosslinking of translocation intermediates // Nature, 355: 84−87,1992-
146. Solomon E.I. Sundaram U.M. and Machonkin Т.Е. Multicopper oxidases and oxygenases // Chem. Rev., 96: 2563−2606, 1996-
147. Stan Т. Ahting U., Dembowski M. Kunkele K.P. Nussberger S. Neupert W., Rapaport D. Recognition of preproteins by the isolated TOM complex of mitochondria // EMBO J., 19: 4895−4902, 2000-
148. Stevens M.D., DiSilvestro R.A., Harris E.D. Specific receptor for ceruloplasmin in membrane fragments from aortic and heart tissues // Biochemistry, 23: 261−266, 1984:
149. Stoj C. and Kosman D.J. Cuprous oxidase activity of yeast Fet3p and human ceruloplasmin: implication for function // FEBS Lett., 554: 422−426, 2003-
150. Strobel G. Zollner A., Angermayr M. Bandlow W. Competition of spontaneous protein folding and mitochondrial import causes dual subcellular location of major adenylate kinase // Molecular Biology of the Cell, 13: 1439−1448,2002-
151. Suzuki Т., Endo К., I to M. Tsujibo H., Miyamoto K. and Inamori Y. A thermostable laccase from Streptomyces lavendulae REN-7: purification, characterization, nucleotide sequence, and expression // Biosci. Biotechnol. Biochem., 67: 2167−2175,2003-
152. Takahashi N. Ortel T.L. Putnam F.W. Single-chain structure of human ceruloplasmin: the complete amino acid sequence of the whole molecule // Proc. Natl. Acad. Sci. USA. 81: 390−394. 1984-
153. Tavassoli M. Kishimoto Т. Kataoka M. Liver endothelium mediates the hepatocyte’s uptake of ceruloplasmin //J Cell Biol. 102 (4): 1298, 1986-
154. Thompson J.D., Higgin. D.G. Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice // Nucleic Acids Res., 22:4673−4680. 1994-
155. Torres J. Wilson M.T. The reactions of copper proteins with nitric oxide // Biochim. Biophys. Acta. 1411: 310−322. 1999-
156. Turner Z, Horn N. Menkes disease- Recent advances and new insights into copper metabolism И Anhals of Medicine, 28: 121−129. 1996-
157. Vasin A.V. Platonova N.A. Mistchenko B.S. Tcymbalenko N.V. Puchkova L V. The application of computer methods for finding the role of the CP-like copper containing proteins in ferrous ion metabolism // SPIE Proceedings, 4707 (7): 323−332, 2002-
158. Verbina LA., Puchkova L.V. Gaitskhoki VS. Neifakh S.A. Isolation and partial characterization of molecular forms of ceruloplasmin from human bile // FEBS Letters. 298: 105−108, 1992-
159. Кои А.К., Thomas Т. Gruss P. Efficiency assessment of the gene trap approach. // Develop. Dynamics, 212: 171−180, 1998-
160. Vulpe C.D., Kuo Y.M., Murphy T.L. Cowley L, Askwith С. Libina N. Gitschier J., Anderson G.J. Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse // Nat. Genet., 21(2): 195−9, 1999-
161. Waasbergen L.G. van, Hildebrand M. and Tebo B.M. Identification and characterization of a gene cluster involved in manganese oxidation by spores of the marine Bacillus sp. strain SG-1 //J. Bacteriol., 178: 3517−3530, 1996-
162. Wang H., Koschinsky M. Hamerton J.L. Localization of processed gene for human ceruloplasmin to chromosome region 8q21.13-q23.1 by in situ hybridization // Cytogenet. Cell Genet., 47: 230−231, 1988-
163. Wienhues U., Becker K., Schleyer M. Guiard В., Tropschug M., Horwich A.L., Pfanner N. Neupert W. Protein folding causes an arrest of preprotein translocation into mitochondria in vivo // J. Cell Biol., 115: 1601−1609, 1991-
164. Wingender, E. Chen, X., Hehl, R" Karas, H" Liebich, /., Matys, V., Meinhardt, Т., Prufi, M" Reuter, /., F. Schacherer. TRANSFAC: an integrated system for gene expression regulation // Nucleic Acids Res. 28: 316−319,2000-
165. Wittung-Stafshede P. Role of cofactors in protein folding // Accounts of Chemical Research, 35: 201−208, 2002-
166. Wooten L, Shulze R.A. Lancey R.W. et al. Ceruloplasmin is found in milk and amniotic fluid and may have a nutritional role // J. Nutr. Biochem. 7(3): 632−639. 1996-
167. Xu F. Berka R.M., Wahleithner J.A., Nelson B.A. Shuster J.R., Brown S.H. Site-directed mutations in fungal laccase: effect on redox potential, activity and pH profile // Biochem. J., 334: 63−70,1998-
168. Yang F. Freidrichs W.E. Cupples R.L., Bonifacio M.J. Sanford J. A., Horton W.A., Bowman B.H. Human ceruloplasmin. Tissue-specific expression of transcripts produced by alternative splicing //J. Biol. Chem. 265(18) — 10 780−10 785.1990-
169. Zaitsev V.N., Zaitseva I., Papiz M. Lindley P.F. An X-ray crystallographic study of the binding sites of the azide inhibitor and organic substrates ti ceruloplasmin //J. Biol. Inorg. Chem. 4: 579−587,1999
170. Василец ИМ. Церулоплазмины. их молекулярная структура и биологические функции//Успехи биол. химии. 14: 172−201, 1973.
171. Васильев В.Б., Шавловский М. М., Нейфах С. А., Прозоровский В. А. Внутримолекулярная гомология церулоплазмина // Биоорг. химия 5: 1045−1052,1979-
172. Васин А. В. Платонова Н.А., Клотченко С. А. Цымбаленко Н.В., Пучкова Л. В. Экспрессия псевдогена церулоплазмина в культивируемых клетках человека // Доклады РАН 397: 827−831. 2004
173. Васин А. В. Платонова Н.А., Повалихин Р. Г., Клотченко С.А, Самсонов С. А., Цымбаленко Н. В., Пучкова JJ.B. Митохондриальный церулоплазмин млекопитающих // Молекуляр. Биология 39: 48−60, 2005-
174. Гайцхоки B.C. Воронина О. В. Денежкина В.В. Плисс М. Г. Пучкова Л.В. Шварцман А. Л. Неифах С.А. Экспрессия гена церулоплазмина в различных органах крысы // Биохимия. 55 (5): 927−937, 1990:
175. Гюлиханданова Н.Е. Изучение регуляции экспрессии гена церулоплазмина в клетках молочной железы // Авт. Кан. Дис. СПб. ГУ НИИЭМ РАМН. 2004.
176. Калинин В.Л. Транскрипция и регуляции экспрессии генов. // Изд. СПбГТУ. Санкт-Петербург, 2001-
177. КарасХ. КельА.Э. Кель О. В. Колчанов Н.А. Вингендер Э. Интеграция знаний по транскрипционной регуляции генов эукариот на основе объединения баз данных TRANSFAC, TRRD и COMPEL // Мол. Биология. 31(4): 637−646, 1997:
178. Кольман Я. Рем К.-Г. Наглядная биохимия // Мир, 2000-
179. Кочетов Г. А. Практическое руководство по энзимологии // М., Высшая Школа. 1980-
180. Маниатис Т. и др. Методы генетической инженерии. Молекулярное клонирование: Пер. с англ. Маниатис Т., Фрич Э., Сэмбрук Дж. // М.: Мир, 1984-
181. Нейфах С.А., Васильев В. Б. Шавловский М.М. Строение, каталитические свойства и эволюция церулоплазмина и других голубых белков // Успехи биол. химии. 23: 102−124. 1988-
182. Платонова Н.А., Жигулева Э. А., Цымбаленко Н. В. Мищенко Б.С. Васин А. В. Живулько Т.В., Пучкова JI.B. Возрастные особенности биосинтеза и распределения церулоплазмина в организме крыс // Онтогенез, 35(3): 171−182,2004:
183. Пучкова JI.В. Алейникова Т. Д., Вербина И. А., Захарова Е. Т., Плисс М. Г., Гайцхоки B.C. Биосинтез двух молекулярных форм церулоплазмина в печени крысы и их полярная секреция в кровоток и в желчь // Биохимия 58 (12): 1893−1900, 1993-
184. Пучкова Л.В., Алейникова Т. Д., Цымбаленко Н. В. и др. Биосинтез и секреция церулоплазмина клетками молочной железы в период лактации // Биохимия. 59: 341−348. 19 946-
185. Пучкова JI.B., Вербина И. А., Гайцхоки B.C., Нейфах С. А. Взаимодействие молекулярных форм церулоплазмина со специфическим рецептором мембран эритроцитов здоровых людей и больных гепатолентикулярной дегенерацией // Биохимия. 56 (12): 2261−2269,1991а
186. Пучкова JI.B. Вербина И. А., Денежкина В. В. Шавловский М.М., Гайцхоки B.C., Нейфах С. А. Некоторые свойства рецептора церулоплазмина. выделенного из мембран эритроцитов человека // Биохимия. 55 (12): 2182−2189. 1990-
187. Пучкова Л.В., Платонова Н. А. Механизм, обеспечивающий гомеостаз меди у эукариотов, и его связь с транспортом железа // Успехи современной биологии, 123 (1): 41−58, 2003-
188. Пучкова Л.В., Сасина Л. К., Алейникова Т. Д., Гайцхоки B.C. Внутриклеточный церулоплазминоподобный белок млекопитающих // Бюл. эксперим. биол. и мед., 1: 83−85, 1994-
189. Саминский Е.М. Трансляция генетического кода на рибосомах // Изд. СПбГТУ, Санкт-Петербург. 2000-
190. Сасина Л.К., Цъшбаленко Н. В. Платонова Н.А., Пучкова Л. В., Воронина О. В., Гюлиханданова Н. Е., Гайцхоки B.C. Выделение и частичная характеристика клона кДНК рецептора церулоплазмина человека // Бюлл. эксп. биол. и мед., 129 (5): 578,2000-
191. Сингер М. Берг П. Гены и геномы // М., Мир, 1998.