Published in J Biol Chem on October 03, 2000
Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS. EMBO J (2004) 2.55
Activation of superoxide dismutases: putting the metal to the pedal. Biochim Biophys Acta (2006) 2.33
Affinity gradients drive copper to cellular destinations. Nature (2010) 1.82
Dietary Cu stabilizes brain superoxide dismutase 1 activity and reduces amyloid Abeta production in APP23 transgenic mice. Proc Natl Acad Sci U S A (2003) 1.46
Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase. Proc Natl Acad Sci U S A (2004) 1.45
Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis. Antioxid Redox Signal (2006) 1.36
Copper chaperones: personal escorts for metal ions. J Bioenerg Biomembr (2002) 1.19
Structure and dynamics of copper-free SOD: The protein before binding copper. Protein Sci (2002) 1.04
Neuronal gene expression in non-demented individuals with intermediate Alzheimer's Disease neuropathology. Neurobiol Aging (2008) 1.00
Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS). Proc Natl Acad Sci U S A (2012) 0.94
Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system. Mol Biol Cell (2011) 0.90
Global structural motions from the strain of a single hydrogen bond. Proc Natl Acad Sci U S A (2013) 0.87
Copper at the Fungal Pathogen-Host Axis. J Biol Chem (2015) 0.83
Selenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase. Biochemistry (2008) 0.80
Inhibition of human copper trafficking by a small molecule significantly attenuates cancer cell proliferation. Nat Chem (2015) 0.80
Divalent-metal-dependent nucleolytic activity of Cu, Zn superoxide dismutase. J Biol Inorg Chem (2006) 0.76
Copper trafficking in biology: an NMR approach. HFSP J (2009) 0.76
Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper-ion entry site. J Biol Chem (2017) 0.75
Susceptibility of Mutant SOD1 to Form a Destabilized Monomer Predicts Cellular Aggregation and Toxicity but Not In vitro Aggregation Propensity. Front Neurosci (2016) 0.75
Oxidative folding in the mitochondrial intermembrane space in human health and disease. Int J Mol Sci (2013) 0.75
Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science (1999) 6.86
Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science (2001) 6.81
Metal ion chaperone function of the soluble Cu(I) receptor Atx1. Science (1997) 4.55
The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J Biol Chem (2001) 2.78
Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat Struct Biol (2001) 2.67
Identification of a copper-responsive two-component system on the chromosome of Escherichia coli K-12. J Bacteriol (2000) 2.63
Function, structure, and mechanism of intracellular copper trafficking proteins. Annu Rev Biochem (2001) 2.33
Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nat Struct Biol (2000) 2.26
A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport. J Biol Chem (1997) 2.18
DNA-bend modulation in a repressor-to-activator switching mechanism. Nature (1995) 1.97
Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal MerR homologue, cueR. J Biol Chem (2000) 1.95
Allosteric underwinding of DNA is a critical step in positive control of transcription by Hg-MerR. Nature (1992) 1.76
The ferric uptake regulation (Fur) repressor is a zinc metalloprotein. Biochemistry (1999) 1.65
DNA distortion mechanism for transcriptional activation by ZntR, a Zn(II)-responsive MerR homologue in Escherichia coli. J Biol Chem (1999) 1.64
DNA distortion accompanies transcriptional activation by the metal-responsive gene-regulatory protein MerR. Biochemistry (1990) 1.57
Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution. Structure (1999) 1.50
Ultrasensitivity and heavy-metal selectivity of the allosterically modulated MerR transcription complex. Proc Natl Acad Sci U S A (1990) 1.45
Multiple protein domains contribute to the action of the copper chaperone for superoxide dismutase. J Biol Chem (1999) 1.41
Structure and chemistry of the copper chaperone proteins. Curr Opin Chem Biol (2000) 1.39
Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2. J Biol Chem (2000) 1.36
Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1. Biochemistry (2001) 1.30
Iron metabolism in eukaryotes: Mars and Venus at it again. Science (1996) 1.27
Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase. J Biol Chem (2001) 1.22
Metallothionein is part of a zinc-scavenging mechanism for cell survival under conditions of extreme zinc deprivation. J Biol Chem (1999) 1.21
Crystal structure of the copper chaperone for superoxide dismutase. Nat Struct Biol (1999) 1.19
Extreme zinc-binding thermodynamics of the metal sensor/regulator protein, ZntR. J Am Chem Soc (2001) 1.18
Overproduction, purification, and characterization of chlorocatechol dioxygenase, a non-heme iron dioxygenase with broad substrate tolerance. Biochemistry (1991) 1.17
Structure-function analyses of the ATX1 metallochaperone. J Biol Chem (1999) 1.16
Characterization of the metal receptor sites in Escherichia coli Zur, an ultrasensitive zinc(II) metalloregulatory protein. Biochemistry (2001) 1.15
Mercury-199 NMR of the metal receptor site in MerR and its protein-DNA complex. Science (1995) 1.14
Heterodimer formation between superoxide dismutase and its copper chaperone. Biochemistry (2000) 1.09
Construction and characterization of a mercury-independent MerR activator (MerRAC): transcriptional activation in the absence of Hg(II) is accompanied by DNA distortion. EMBO J (1993) 1.08
The chemical cell biology of zinc: structure and intracellular fluorescence of a zinc-quinolinesulfonamide complex. J Biol Inorg Chem (1999) 1.07
Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states. J Biol Chem (2000) 0.95
Metalloregulatory proteins and molecular mechanisms of heavy metal signal transduction. Adv Inorg Biochem (1990) 0.94
Imaging and elemental mapping of biological specimens with a dual-EDS dedicated scanning transmission electron microscope. Ultramicroscopy (2013) 0.93
Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Biochemistry (2000) 0.93
Copper stabilizes a heterodimer of the yCCS metallochaperone and its target superoxide dismutase. J Biol Chem (2001) 0.91
Biochemical and spectroscopic probes of mercury(II) coordination environments in proteins. Methods Enzymol (1993) 0.83
Metal-responsive gene regulation and the zinc metalloregulatory model. Met Ions Biol Syst (1996) 0.82
Mercury-responsive gene regulation and mercury-199 as a probe of protein structure. Met Ions Biol Syst (1997) 0.79
Effects of nutrient substrates on immune function. Nutrition (1992) 0.76
Evidence for retention of biological activity of a non-heme iron enzyme adsorbed on a silver colloid: a surface-enhanced resonance Raman scattering study. Biochemistry (1993) 0.75
[Thyrotoxic periodic paralysis. Report of a case]. Arq Neuropsiquiatr (1979) 0.75