Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites-Reference-Cited by-同舟云学术

Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites

Published:2018 Issue:7 Volume:10 Page:1003-1015
ISSN:1756-5901
Container-title:Metallomics
language:en
Short-container-title:Metallomics

Author:

Vujačić Nikezić Ana V.¹²³⁴^ORCID,Janjić Goran V.⁵²³⁴^ORCID,Bondžić Aleksandra M.¹²³⁴^ORCID,Zarić Božidarka L.¹²³⁴^ORCID,Vasić-Anićijević Dragana D.¹²³⁴^ORCID,Momić Tatjana G.¹²³⁴^ORCID,Vasić Vesna M.¹²³⁴^ORCID

Affiliation:

1. Vinča Institute of Nuclear Sciences

2. University of Belgrade

3. Belgrade

4. Serbia

5. Institute of Chemistry, Metallurgy and Technology

Abstract

Inhibition of Na/K-ATPase by selected Au(iii) and Pt(ii) complexes is induced by binding these complexes between the M2 and M4 helices at the intracellular side of pump.

Funder

Ministarstvo Prosvete, Nauke i Tehnološkog Razvoja

Publisher

Oxford University Press (OUP)

Subject

Metals and Alloys,Biochemistry,Biomaterials,Biophysics,Chemistry (miscellaneous)

Link

http://pubs.rsc.org/en/content/articlepdf/2018/MT/C8MT00111A

Reference63 articles.

1. Structure and Mechanism of Na,K-ATPase: Functional Sites and Their Interactions

2. Na+/K+-ATPase as a signal transducer

3. Isoforms of the Na,K-ATPase: Family members in search of function

4. Biochemistry of Na,K-ATPase

5. Isozymes of the Na-K-ATPase: heterogeneity in structure, diversity in function

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