Supplemental material
Journal of Enzyme Inhibition and Medicinal Chemistry
Volume 33, 2018 - Issue 1
Research Paper
Identification of cisplatin-binding sites on the large cytoplasmic loop of the Na+/K+-ATPase
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Martin KubalaDepartment of Biophysics, Faculty of Science, Centre of Region Haná for Biotechnological and Agricultural Research, Palacký University, Olomouc, Czech Republic; Correspondence[email protected]
http://orcid.org/0000-0002-3555-0016View further author information
http://orcid.org/0000-0002-3555-0016View further author informationRelated Research Data
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The hydrogen bonds between Arg423 and Glu472 and other key residues, Asp443, Ser477, and Pro489, are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na(+)/K(+)-ATPase.
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The functional role of beta subunits in oligomeric P-type ATPases.
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Repair capacity for platinum-DNA adducts determines the severity of cisplatin-induced peripheral neuropathy
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Changes in electrostatic surface potential of Na+/K+-ATPase cytoplasmic headpiece induced by cytoplasmic ligand(s) binding.
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Crystal Structure of Na+, K+-ATPase in the Na+-Bound State
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American Association for the Advancement of Science (AAAS)
"Oxygen Sensing" by Na,K-ATPase: These Miraculous Thiols
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Catalytic Activity of an Isolated Domain of Na,K-ATPase Expressed in Escherichia coli
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Na(+)/K(+)-ATPase inhibition by cisplatin and consequences for cisplatin nephrotoxicity.
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ATP and magnesium drive conformational changes of the Na+/K+-ATPase cytoplasmic headpiece.
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S-glutathionylation of the Na,K-ATPase catalytic α subunit is a determinant of the enzyme redox sensitivity.
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Structure, Recognition, and Processing of Cisplatin-DNA Adducts.
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Metals in Medicine
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Molecular dynamics with coupling to an external bath.
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