How do bacterial cells ensure that metalloproteins get the correct metal?
KJ Waldron, NJ Robinson - Nature Reviews Microbiology, 2009 - nature.com
Protein metal-coordination sites are richly varied and exquisitely attuned to their inorganic
partners, yet many metalloproteins still select the wrong metals when presented with …
partners, yet many metalloproteins still select the wrong metals when presented with …
Copper in diseases and treatments, and copper‐based anticancer strategies
Copper is found in all living organisms and is a crucial trace element in redox chemistry,
growth and development. It is important for the function of several enzymes and proteins …
growth and development. It is important for the function of several enzymes and proteins …
Metal ions and amyloid fiber formation in neurodegenerative diseases. Copper, zinc and iron in Alzheimer's, Parkinson's and prion diseases
JH Viles - Coordination Chemistry Reviews, 2012 - Elsevier
There are a group of diseases associated with protein misfolding and accumulation into
amyloid fibers. Many of these diseases have a major impact on human health, in particular …
amyloid fibers. Many of these diseases have a major impact on human health, in particular …
Fluorescent gold clusters as nanosensors for copper ions in live cells
This paper reports the use of fluorescent gold nanoclusters synthesized using bovine serum
albumin (Au–BSA) for the sensing of copper ions in live cells. The fluorescence of the …
albumin (Au–BSA) for the sensing of copper ions in live cells. The fluorescence of the …
Substoichiometric levels of Cu2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-β from Alzheimer disease
A role for Cu 2+ ions in Alzheimer disease is often disputed, as it is believed that Cu 2+ ions
only promote nontoxic amorphous aggregates of amyloid-β (Aβ). In contrast with currently …
only promote nontoxic amorphous aggregates of amyloid-β (Aβ). In contrast with currently …
Copper (II) binding to α-synuclein, the Parkinson's protein
Variations in tryptophan fluorescence intensities confirm that copper (II) interacts with α-
synuclein, a protein implicated in Parkinson's disease. Trp4 fluorescence decay kinetics …
synuclein, a protein implicated in Parkinson's disease. Trp4 fluorescence decay kinetics …
Copper (II) binding to amyloid-β fibrils of Alzheimer's disease reveals a picomolar affinity: stoichiometry and coordination geometry are independent of Aβ oligomeric …
Cu2+ ions are found concentrated within senile plaques of Alzheimer's disease patients
directly bound to amyloid-β peptide (Aβ) and are linked to the neurotoxicity and self …
directly bound to amyloid-β peptide (Aβ) and are linked to the neurotoxicity and self …
Site-specific interactions of Cu (II) with α and β-synuclein: Bridging the molecular gap between metal binding and aggregation
The aggregation of α-synuclein (AS) is a critical step in the etiology of Parkinson's disease
(PD) and other neurodegenerative synucleinopathies. Protein− metal interactions play a …
(PD) and other neurodegenerative synucleinopathies. Protein− metal interactions play a …
Bioinorganic chemistry of copper coordination to alpha-synuclein: Relevance to Parkinson's disease
Alpha-synuclein (AS) aggregation is associated with neurodegeneration in Parkinson's
disease (PD). At the same time, alterations in metal ion homeostasis may play a pivotal role …
disease (PD). At the same time, alterations in metal ion homeostasis may play a pivotal role …
[HTML][HTML] The cellular prion protein traps Alzheimer's Aβ in an oligomeric form and disassembles amyloid fibers
There is now strong evidence to show that the presence of the cellular prion protein (PrP C)
mediates amyloid-β (Aβ) neurotoxicity in Alzheimer's disease (AD). Here, we probe the …
mediates amyloid-β (Aβ) neurotoxicity in Alzheimer's disease (AD). Here, we probe the …