Sentence examples for binding copper from inspiring English sources

As β-Syn has been shown to decrease the aggregation of α-Syn [44], it is conceivable that this process might involve prevention of copper binding to α-Syn by either binding copper itself or a physical interaction with α-Syn that inhibits copper binding.

It is certainly likely that a histidine-rich protein could be responsible for detoxification by binding copper [ 53].

Ion binding functions, such as zinc ion binding, copper ion binding, cobalt ion binding and calcium ion binding, were all over-represented (Fig.  5a).

Pyrrolidine dithiocarbamate (PDTC; Fig. 1a) is a synthetic antioxidant and inhibitor of NF-κB that is capable of binding copper [ 55, 56].

With the PAINT process, SOD1 was annotated with three molecular functions: 'SOD activity, zinc ion binding, copper ion binding', four CCs and one process: 'removal of superoxide radicals'.

CopC and CopD are considered a functional unit, with CopC binding copper, possibly for delivery to the copper permease CopD [ 81].

However, protein functions common to both structural and nonstructural proteins such as iron-binding, metal-binding, lipid-binding, copper-binding, transmembrane, outer membrane, channels/pores pore-forming toxins (proteins and peptides) could work as important biomarkers.

S-adenosyl L-homocysteine hydrolase was also shown to bind copper with high affinity and is indeed the major copper binding protein in mouse liver [89,90].

Genes such as chlorophyll-binding and copper ion-binding genes were also suppressed during the initial phase of infestation by aphids.

Molybdenum prevents plasma proteins from binding to copper, and it also increases the amount of copper that is excreted in urine.

After translation by the ribosome, SOD1 binds zinc by a process which has not been characterized; then the binding of copper and concomitant formation of the intramolecular disulfide bond are catalyzed by the copper chaperone for SOD1 (CCS) [88].