Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase.
TLDR
Cox17 represents a novel copper chaperone that delivers copper to two proteins, which is specific because no transfer occurs to heterologous proteins, including bovine serum albumin and carbonic anhydrase.About:
This article is published in Journal of Biological Chemistry.The article was published on 2004-08-20 and is currently open access. It has received 276 citations till now. The article focuses on the topics: COX17 & Cytochrome c oxidase.read more
Citations
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Metals in Neurobiology: Probing Their Chemistry and Biology with Molecular Imaging
TL;DR: The brain is a singular organ of unique biological complexity that serves as the command center for cognitive and motor function and has requirements for the highest concentrations of metal ions in the body and the highest per-weight consumption of body oxygen.
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Copper Homeostasis and Neurodegenerative Disorders (Alzheimer's, Prion, and Parkinson's Diseases and Amyotrophic Lateral Sclerosis)
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Mechanisms for copper acquisition, distribution and regulation
TL;DR: Recent advances in the identification and function of cellular and systemic molecules that drive Cu accumulation, distribution and sensing are reviewed.
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Function and Regulation of Human Copper-Transporting ATPases
TL;DR: Current data on the structural organization and functional properties of ATP7A and ATP7B as well as their localization and functions in various tissues are summarized, and the current models of regulated trafficking of human Cu-ATPases are discussed.
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Copper, iron, and zinc ions homeostasis and their role in neurodegenerative disorders (metal uptake, transport, distribution and regulation)
Henryk Kozlowski,Anna Janicka-Klos,Justyna Brasuń,Elena Gaggelli,Daniela Valensin,Gianni Valensin +5 more
TL;DR: In this article, a review of the metal homeostasis for major metal ions (Cu, Fe, and Zn) is presented, and the impact of these metals on some disorders are also discussed.
References
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Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase.
TL;DR: Results indicate that intracellular [Cu]free is limited to less than one free copper ion per cell and suggest that a pool of free copper ions is not used in physiological activation of metalloenzymes.
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Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A
Tomitake Tsukihara,Hiroshi Aoyama,Eiki Yamashita,Takashi Tomizaki,Hiroshi Yamaguchi,Kyoko Shinzawa-Itoh,Ryosuke Nakashima,Rieko Yaono,Shinya Yoshikawa +8 more
TL;DR: The high resolution three-dimensional x-ray structure of the metal sites of bovine heart cytochrome c oxidase is reported, suggesting a dinuclear copper center with an unexpected structure similar to a [2Fe-2S]-type iron-sulfur center.
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Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression
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Metal ion chaperone function of the soluble Cu(I) receptor Atx1.
Robert A. Pufahl,C. P. Singer,Katrina Peariso,Su Ju Lin,Paul J. Schmidt,Christoph J. Fahrni,V. Cizewski Culotta,James E. Penner-Hahn,Thomas V. O'Halloran +8 more
TL;DR: The unusual structure and dynamics of Atx1 suggest a copper exchange function for this protein and related domains in the Menkes and Wilson disease proteins.