메뉴 건너뛰기




Volumn 36, Issue 3, 2003, Pages 215-221

Structural genomics of proteins involved in copper homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; COPPER; COPPER BINDING PROTEIN; COPPER-BINDING PROTEIN; PROTEIN;

EID: 0037349399     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar010120r     Document Type: Article
Times cited : (56)

References (39)
  • 4
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • Rae, T.; Schmidt, P. J.; Pufahl, R. A.; Culotta, V. C.; O'Halloran, T. V. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 1999, 284, 805-808.
    • (1999) Science , vol.284 , pp. 805-808
    • Rae, T.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 6
    • 0030671295 scopus 로고    scopus 로고
    • Delivering copper inside yeast and human cells
    • Valentine, J. S.; Gralla, E. B. Delivering copper inside yeast and human cells. Science 1997, 278, 817-818.
    • (1997) Science , vol.278 , pp. 817-818
    • Valentine, J.S.1    Gralla, E.B.2
  • 7
    • 0037477740 scopus 로고    scopus 로고
    • A delicate balance: Homeostatic control of copper uptake and distribution
    • Pena, M. M. O.; Lee, J.; Thiele, D. J. A delicate balance: homeostatic control of copper uptake and distribution. J. Nutr. 1999, 129, 1251-1260.
    • (1999) J. Nutr. , vol.129 , pp. 1251-1260
    • Pena, M.M.O.1    Lee, J.2    Thiele, D.J.3
  • 8
    • 0034682776 scopus 로고    scopus 로고
    • Metallochaperones: An Intracellular Shuttle Service for Metal Ions
    • O'Halloran, T. V.; Culotta, V. C. Metallochaperones: An Intracellular Shuttle Service for Metal Ions. J. Biol. Chem. 2000, 275, 25057-25060.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25057-25060
    • O'Halloran, T.V.1    Culotta, V.C.2
  • 11
    • 0035923596 scopus 로고    scopus 로고
    • Structural genomics: An approach to the protein folding problem
    • Montelione, G. T. Structural genomics: an approach to the protein folding problem. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 13488-13489.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 13488-13489
    • Montelione, G.T.1
  • 16
    • 0035117191 scopus 로고    scopus 로고
    • Copper delivery by metallochaperone proteins
    • Rosenzweig, A. C. Copper delivery by metallochaperone proteins. Acc. Chem. Res. 2001, 34, 119-128.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 119-128
    • Rosenzweig, A.C.1
  • 17
    • 0034700980 scopus 로고    scopus 로고
    • Crystal structure of the second domain of the human copper chaperone for superoxide dismutase
    • Lamb, A. L.; Wernimont, A. K.; Pufahl, R. A.; O'Halloran, T. V.; Rosenzweig, A. C. Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Biochemistry 2000, 39, 1589-1595.
    • (2000) Biochemistry , vol.39 , pp. 1589-1595
    • Lamb, A.L.1    Wernimont, A.K.2    Pufahl, R.A.3    O'Halloran, T.V.4    Rosenzweig, A.C.5
  • 18
    • 0033813548 scopus 로고    scopus 로고
    • Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins
    • Wernimont, A. K.; Huffman, D. L.; Lamb, A. L.; O'Halloran, T. V.; Rosenzweig, A. C. Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nat. Struct. Biol. 2000, 7, 766-771.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 766-771
    • Wernimont, A.K.1    Huffman, D.L.2    Lamb, A.L.3    O'Halloran, T.V.4    Rosenzweig, A.C.5
  • 19
    • 0034603776 scopus 로고    scopus 로고
    • X-ray crystallographic and analytical ultracentrifugation analyses of truncated and full-length yeast copper chaperones for SOD (LYS7): A dimer-dimer model of LYS7-SOD association and copper delivery
    • Hall, L. T.; Sanchez, R. J.; Holloway, S. P.; Zhu, H.; Stine, J. E.; Lyons, T. J.; Demeler, B.; Schirf, V.; Hansen, J. C.; Nersissian, A. M.; Valentine, J. S.; Hart, P. J. X-ray crystallographic and analytical ultracentrifugation analyses of truncated and full-length yeast copper chaperones for SOD (LYS7): a dimer-dimer model of LYS7-SOD association and copper delivery. Biochemistry 2000, 39, 3611-3623.
    • (2000) Biochemistry , vol.39 , pp. 3611-3623
    • Hall, L.T.1    Sanchez, R.J.2    Holloway, S.P.3    Zhu, H.4    Stine, J.E.5    Lyons, T.J.6    Demeler, B.7    Schirf, V.8    Hansen, J.C.9    Nersissian, A.M.10    Valentine, J.S.11    Hart, P.J.12
  • 20
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • Lamb, A. L.; Torres, A. S.; O'Halloran, T. V.; Rosenzweig, A. C. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat. Struct. Biol. 2001, 8, 751-755.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 751-755
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 21
    • 0031974775 scopus 로고    scopus 로고
    • Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase
    • Gitschier, J.; Moffat, B.; Reilly, D.; Wood, W. I.; Fairbrother, W. J. Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase. Nat. Struct. Biol. 1998, 5, 47-54.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 47-54
    • Gitschier, J.1    Moffat, B.2    Reilly, D.3    Wood, W.I.4    Fairbrother, W.J.5
  • 23
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein - Protein interactions in solution by NMR spectroscopy
    • Zuiderweg, E. R. Mapping protein - protein interactions in solution by NMR spectroscopy. Biochemistry 2002, 41, 1-7.
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.1
  • 24
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G.; Ruben, D. J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 1980, 69, 185-188.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-188
    • Bodenhausen, G.1    Ruben, D.J.2
  • 26
    • 0035852814 scopus 로고    scopus 로고
    • Solution Structure of the Cu(I) and Apo forms of the Yeast Metallochaperone, Atx1
    • Arnesano, F.; Banci, L.; Bertini, I.; Huffman, D. L.; O'Halloran, T. V. Solution Structure of the Cu(I) and Apo forms of the Yeast Metallochaperone, Atx1. Biochemistry 2001, 40, 1528-1539.
    • (2001) Biochemistry , vol.40 , pp. 1528-1539
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Huffman, D.L.4    O'Halloran, T.V.5
  • 27
    • 0035896548 scopus 로고    scopus 로고
    • Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states
    • Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Huffman, D. L.; O'Halloran, T. V. Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states. J. Biol. Chem. 2001, 276, 8415-8426.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8415-8426
    • Banci, L.1    Bertini, I.2    Ciofi-Baffoni, S.3    Huffman, D.L.4    O'Halloran, T.V.5
  • 28
    • 0037418566 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy study of CopZ, a copper chaperone in Bacillus subtilis
    • in press
    • Banci, L.; Bertini, I.; Del Conte, R.; Mangani, S.; Meyer-Klaucke, W. X-ray absorption spectroscopy study of CopZ, a copper chaperone in Bacillus subtilis. Biochemistry 2003, in press.
    • (2003) Biochemistry
    • Banci, L.1    Bertini, I.2    Del Conte, R.3    Mangani, S.4    Meyer-Klaucke, W.5
  • 30
    • 0035798652 scopus 로고    scopus 로고
    • Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase
    • Arnesano, F.; Banci, L.; Bertini, I.; Cantini, F.; Ciofi-Baffoni, S.; Huffman, D. L.; O'Halloran, T. V. Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase. J. Biol. Chem. 2001, 276, 41365-41376.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41365-41376
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Cantini, F.4    Ciofi-Baffoni, S.5    Huffman, D.L.6    O'Halloran, T.V.7
  • 31
    • 0036775946 scopus 로고    scopus 로고
    • Solution structure of CopC: A cupredoxin-like protein involved in copper homeostasis
    • Arnesano, F.; Banci, L.; Bertini, I.; Thompsett, A. Solution structure of CopC: a cupredoxin-like protein involved in copper homeostasis. Structure 2002, 10, 1337-1347.
    • (2002) Structure , vol.10 , pp. 1337-1347
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Thompsett, A.4
  • 32
  • 34
    • 0034923639 scopus 로고    scopus 로고
    • Paramagnetic probes in metalloproteins. Turning limitations into advantages
    • Bertini, I.; Luchinat, C.; Piccioli, M. Paramagnetic Probes in Metalloproteins. Turning Limitations into Advantages. Methods Enzymol. 2001, 339, 314-340.
    • (2001) Methods Enzymol. , vol.339 , pp. 314-340
    • Bertini, I.1    Luchinat, C.2    Piccioli, M.3
  • 36
    • 0035951084 scopus 로고    scopus 로고
    • Copper trafficking: The solution structure of Bacillus subtilis CopZ
    • Banci, L.; Bertini, I.; Del Conte, R.; Markey, J.; Ruiz-Dueñas, F. J. Copper trafficking: the solution structure of Bacillus subtilis CopZ. Biochemistry 2001, 40, 15660-15668.
    • (2001) Biochemistry , vol.40 , pp. 15660-15668
    • Banci, L.1    Bertini, I.2    Del Conte, R.3    Markey, J.4    Ruiz-Dueñas, F.J.5
  • 37
    • 0033955655 scopus 로고    scopus 로고
    • High-resolution solution structure of the protein part of Cu7 metallothionein
    • Bertini, I.; Hartmann, H. J.; Klein, T.; Liu, G.; Luchinat, C.; Weser, U. High-resolution solution structure of the protein part of Cu7 metallothionein. Eur. J. Biochem. 2000, 267, 1008-1018.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1008-1018
    • Bertini, I.1    Hartmann, H.J.2    Klein, T.3    Liu, G.4    Luchinat, C.5    Weser, U.6
  • 38
    • 0033529633 scopus 로고    scopus 로고
    • NMR structure and metal interactions of the CopZ copper chaperone
    • Wimmer, R.; Herrmann, T.; Solioz, M.; Wüthrich, K. NMR structure and metal interactions of the CopZ copper chaperone. J. Biol. Chem. 1999, 274, 22597-22603.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22597-22603
    • Wimmer, R.1    Herrmann, T.2    Solioz, M.3    Wüthrich, K.4
  • 39
    • 0030052073 scopus 로고    scopus 로고
    • 3D solution structure of copper and silver-substituted yeast metallothioneins
    • Peterson, C. W.; Narula, S. S.; Armitage, I. M. 3D solution structure of copper and silver-substituted yeast metallothioneins. FEBS Lett. 1996, 379, 85-93.
    • (1996) FEBS Lett. , vol.379 , pp. 85-93
    • Peterson, C.W.1    Narula, S.S.2    Armitage, I.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.