Crossref
journal-article
Elsevier BV
Current Opinion in Chemical Biology (78)
References
50
Referenced
174
10.1002/anie.199600431
/ Angew Chem Int Ed Engl / Copper – a ‘modern’ bioelement by Kaim (1996)10.1126/science.278.5339.853
/ Science / Metal ion chaperone function of the soluble Cu(I) receptor, Atx1 by Pufahl (1997)10.1074/jbc.272.38.23469
/ J Biol Chem / The copper chaperone for superoxide dismutase by Culotta (1997)10.1126/science.284.5415.805
/ Science / Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase by Rae (1999)10.1016/S0014-5793(99)00091-5
/ FEBS Lett / The Enterococcus hirae copper chaperone CopZ delivers copper(I) to the CopY repressor by Cobine (1999)10.1074/jbc.271.24.14504
/ J Biol Chem / Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase by Glerum (1996)10.1074/jbc.272.52.33191
/ J Biol Chem / Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle by Beers (1997)10.1021/bi980418y
/ Biochemistry / Characterization of the copper chaperone Cox17 of Saccharomyces cerevisiae by Srinivasan (1998)10.1104/pp.117.4.1227
/ Plant Physiol / Identification of a functional homolog of the yeast copper homeostasis gene Atx1 from Arabidopsis by Himelblau (1998){'key': '10.1016/S1367-5931(99)00066-6_BIB10', 'first-page': '3259', 'article-title': 'Expression of copper trafficking genes in the mouse brain', 'volume': '9', 'author': 'Nishihara', 'year': '1998', 'journal-title': 'Molec Neurosci'}
/ Molec Neurosci / Expression of copper trafficking genes in the mouse brain by Nishihara (1998)10.1006/bbrc.1999.1678
/ Biochem Biophys Res Commun / Molecular cloning of rat ATX1 homologue protein by Hiromura (1999)10.1006/geno.1999.5983
/ Genomics / The copper chaperone atox1 in canine copper toxicosis in bedlington terriers by Nanji (1999)10.1074/jbc.272.14.9221
/ J Biol Chem / Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis by Klomp (1997)10.1016/S0306-4522(99)00175-X
/ Neuroscience / Expression profile of the copper homeostasis gene, rAtox1, in the rat brain by Naeve (1999)10.1016/0168-9525(94)90172-4
/ Trends Genet / Wilson disease and Menkes disease: new handles on heavy-metal transport by Bull (1994)10.1073/pnas.92.9.3784
/ Proc Natl Acad Sci USA / The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity by Lin (1995)10.1074/jbc.274.21.15041
/ J Biol Chem / Structure-function analyses of the ATX1 metallochaperone by Portnoy (1999)10.1074/jbc.275.1.580
/ J Biol Chem / The copper transport protein Atox1 promotes neuronal survival by Kelner (2000)10.1074/jbc.272.14.9215
/ J Biol Chem / >A role for the Saccharomyces cervisiae ATXI gene in copper trafficking and iron transport by Lin (1997)10.1016/0092-8674(94)90346-8
/ Cell / The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake by Askwith (1994)10.1074/jbc.274.40.28497
/ J Biol Chem / Characterization of the interactions between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone HAH1p by Larin (1999)10.1073/pnas.96.23.13363
/ Proc Natl Acad Sci USA / Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis by Hamza (1999)10.1038/nsb0198-8
/ Nat Struct Biol / Living with metal ions by McRee (1998)10.1021/bi9631632
/ Biochemistry / Structures of the reduced and mercury-bound forms of MerP, the periplasmic proteinfrom the bacterial mercury detoxification system by Steele (1997)10.1016/S0969-2126(99)80082-3
/ Structure / Crystal structure of the Atx1 metallochaperone protein at 1.02 Å resolution by Rosenzweig (1999)10.1074/jbc.274.32.22597
/ J Biol Chem / NMR structure and metal interactions of the CopZ copper chaperone by Wimmer (1999)10.1038/nsb0198-47
/ Nat Struct Biol / Solution structure of the fourth metal binding domain from the Menkes copper-transporting ATPase by Gitschier (1998)10.1038/11489
/ Nat Struct Biol / Crystal structure of the copper chaperone for superoxide dismutase by Lamb (1999)10.1021/ja982990i
/ J Am Chem Soc / The Menkes disease protein binds copper via novel 2-coordinate Cu(I)-cysteinates in the N-terminal domain by Ralle (1998)10.1074/jbc.270.9.4349
/ J Biol Chem / Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae by Odermatt (1995)10.1006/bbrc.1999.0807
/ Biochem Biophys Res Commun / Effects of promoter mutations on the in vivo regulation of the cop operon of Enterococcus hirae by copper(I) and copper(II) by Wunderli-Ye (1999)10.1074/jbc.272.14.8932
/ J Biol Chem / CopY is a copper-inducible repressor of the Enterococcus hirae copper ATPases by Strausak (1997)10.1046/j.1432-1327.1998.2510716.x
/ Eur J Biochem / The Saccharomyces cerevisiae LYS7 gene is involved in oxidative stress protection by Gamonet (1998)10.1074/jbc.273.37.23625
/ J Biol Chem / The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase by Casareno (1998)10.1046/j.1471-4159.1999.0720422.x
/ J Neurochem / The copper chaperone CCS is abundant in neurons and astrocytes in human and rodent brain by Rothstein (1999){'key': '10.1016/S1367-5931(99)00066-6_BIB36', 'first-page': '219', 'article-title': 'Familial amyotrophic lateral sclerosis', 'volume': '49', 'author': 'Siddique', 'year': '1997', 'journal-title': 'J Neural Transm'}
/ J Neural Transm / Familial amyotrophic lateral sclerosis by Siddique (1997)10.1016/S0959-4388(98)80123-2
/ Curr Opin Neurobiol / The genetic and molecular mechanisms of motor neuron disease by Wong (1998)10.1126/science.284.5415.748
/ Science / Free copper ions in the cell? by Lippard (1999)10.1074/jbc.274.34.23719
/ J Biol Chem / Multiple protein domains contribute to the action of the copper chaperone for superoxide dismutase by Schmidt (1999)10.1038/11464
/ Nat Struct Biol / Helping copper find a home by Poulos (1999)10.1021/bi992822i
/ Biochemistry / Crystal structure of the second domain of the human copper chaperone for superoxide dismutase by Lamb (2000)10.1074/jbc.274.52.36952
/ J Biol Chem / A gain of superoxide dismutase activity obtained with CCS, the copper metallochaperone for SOD1 by Schmidt (1999)10.1016/S0969-2126(99)80117-8
/ Structure / A model for the incorporation of metal from the copper chaperone CCS into Cu,Zn superoxide dismutase by Falconi (1999)10.1021/bi982435t
/ Biochemistry / Identification of metal-binding residues in the Klebsiella aerogenes urease nickel metallochaperone, UreE by Colpas (1999)10.1073/pnas.96.22.12339
/ Proc Natl Acad Sci USA / Purification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assembly by Nguyen (1999)10.1006/jmbi.1999.3294
/ J Mol Biol / Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assembly by Garland (1999)10.1074/jbc.274.22.15869
/ J Biol Chem / Incorporation of molybdenum into the iron-molybdenum cofactor of nitrogenase by Allen (1999)10.1074/jbc.273.47.31138
/ J Biol Chem / Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly by Strain (1998)10.1073/pnas.97.2.599
/ Proc Natl Acad Sci USA / NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein by Yuvaniyama (2000)10.1074/jbc.273.30.19243
/ J Biol Chem / Roles of copper ligands in the activation and secretion of Streptomyces tyrosinase by Tsai (1998)
Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 5:55 a.m.) |
Deposited | 6 years, 4 months ago (April 28, 2019, 3:51 p.m.) |
Indexed | 1 month, 1 week ago (July 22, 2025, 6:46 a.m.) |
Issued | 25 years, 5 months ago (April 1, 2000) |
Published | 25 years, 5 months ago (April 1, 2000) |
Published Print | 25 years, 5 months ago (April 1, 2000) |
@article{Rosenzweig_2000, title={Structure and chemistry of the copper chaperone proteins}, volume={4}, ISSN={1367-5931}, url={http://dx.doi.org/10.1016/s1367-5931(99)00066-6}, DOI={10.1016/s1367-5931(99)00066-6}, number={2}, journal={Current Opinion in Chemical Biology}, publisher={Elsevier BV}, author={Rosenzweig, A}, year={2000}, month=apr, pages={140–147} }