Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS) - Wikidata - awgldk - TriplyDB

Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)

Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)

http://www.wikidata.org/entity/Q36187334

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The Role of Copper Chaperone Atox1 in Coupling Redox Homeostasis to Intracellular Copper Distribution SOD1 misplacing and mitochondrial dysfunction in amyotrophic lateral sclerosis pathogenesis Mechanisms of mutant SOD1 induced mitochondrial toxicity in amyotrophic lateral sclerosis Candida albicans SOD5 represents the prototype of an unprecedented class of Cu-only superoxide dismutases required for pathogen defense A faulty interaction between SOD1 and hCCS in neurodegenerative disease In-cell NMR: an emerging approach for monitoring metal-related events in living cells.Lipid-associated aggregate formation of superoxide dismutase-1 is initiated by membrane-targeting loops.Activation of the cnidarian oxidative stress response by ultraviolet radiation, polycyclic aromatic hydrocarbons and crude oil Atomic-resolution monitoring of protein maturation in live human cells by NMR Superoxide dismutases and superoxide reductases.Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.Acetylation at lysine 71 inactivates superoxide dismutase 1 and sensitizes cancer cells to genotoxic agents.Inhibition of human copper trafficking by a small molecule significantly attenuates cancer cell proliferation Copper chaperones. The concept of conformational control in the metabolism of copper.An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis.Species-specific activation of Cu/Zn SOD by its CCS copper chaperone in the pathogenic yeast Candida albicans.Copper trafficking to the secretory pathway.Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site.Inhibition of Mitochondrial Clearance and Cu/Zn-SOD Activity Enhance 6-Hydroxydopamine-Induced Neuronal Apoptosis.In-cell NMR: a topical review Thiol-based copper handling by the copper chaperone Atox1.Orchestration of dynamic copper navigation - new and missing pieces.Oxygen-dependent activation of Cu,Zn-superoxide dismutase-1.Characterization of proteins by in-cell NMR spectroscopy in cultured mammalian cells.S-acylation of SOD1, CCS, and a stable SOD1-CCS heterodimer in human spinal cords from ALS and non-ALS subjects.Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro.Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants.The influence of protein folding on the copper affinities of trafficking and target sites.Mia40 and MINOS act in parallel with Ccs1 in the biogenesis of mitochondrial Sod1.A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants.Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants.The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase.SOD1:Zn2+ apoenzyme binds CCS:Zn2+:2xCu1+2xSOD1:CCS:Zn2+:2xCu1+ dimer dissociates CCS transfers Cu to SOD1 and oxidizes cysteine residues in SOD1 S95C substitution in CuZn-SOD of Ipomoea carnea: impact on the structure, function and stability.The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation.Human copper chaperone for superoxide dismutase 1 mediates its own oxidation-dependent import into mitochondria.Quantifying the Interaction between Copper-Zinc Superoxide Dismutase (Sod1) and its Copper Chaperone (Ccs1).

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Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)

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Proceedings of the National Academy of Sciences of the United States of America

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Human superoxide dismutase 1 ( ...... pper chaperone for SOD1 (hCCS)

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Chiara Massagni

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Francesca Cantini

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Jeffrey T Rubino

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Kairit Zovo

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Peep Palumaa

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Tatiana Kozyreva

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P2860

The copper chaperone for superoxide dismutase

Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells

Crystal structure of the copper chaperone for superoxide dismutase

Crystal structure of the second domain of the human copper chaperone for superoxide dismutase

Heterodimeric structure of superoxide dismutase in complex with its metallochaperone

The solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerization

Structure and dynamics of copper-free SOD: The protein before binding copper

Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein folding

Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?

A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage.

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34

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230624025

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22869735

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molecular chaperones

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3427097

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