Properties of recombinant extracellular N-terminal domain of human high-affinity copper transporter 1 (hNdCTR1) and its interactions with Cu(<scp>ii</scp>) and Ag(<scp>i</scp>) ions-Reference-Cited by-同舟云学术

Properties of recombinant extracellular N-terminal domain of human high-affinity copper transporter 1 (hNdCTR1) and its interactions with Cu(ii) and Ag(i) ions

Published:2023 Issue:11 Volume:52 Page:3403-3419
ISSN:1477-9226
Container-title:Dalton Transactions
language:en
Short-container-title:Dalton Trans.

Author:

Orlov Iurii A.¹,Sankova Tatiana P.²,Skvortsov Alexey N.²³,Klotchenko Sergey A.⁴,Sakhenberg Elena I.⁵,Mekhova Aleksandra A.¹²,Kiseleva Irina V.⁶,Ilyechova Ekaterina Yu.¹²⁷^ORCID,Puchkova Ludmila V.¹²⁷^ORCID

Affiliation:

1. Research centre of advanced functional materials and laser communication systems, ADTS Institute, ITMO, University, 197101 St. Petersburg, Russia

2. Institute of Biomedical Systems and Biotechnology, Peter the Great St. Petersburg Polytechnic University, 195251 St. Petersburg, Russia

3. Laboratory of The Molecular Biology of Stem Cells, Institute of Cytology, RAS, 194064 St. Petersburg, Russia

4. Laboratory for the Development of Molecular Diagnostic Systems, Smorodintsev Research Institute of Influenza, 197376 St. Petersburg, Russia

5. Laboratory of cell protection mechanisms, Institute of Cytology, RAS, 194064 St. Petersburg, Russia

6. Department of Virology, Institute of Experimental Medicine, 197376 St. Petersburg, Russia

7. Department of Molecular Genetics, Institute of Experimental Medicine, 197376 St. Petersburg, Russia

Abstract

Recombinant fusion protein GB1-NdCTR1 containing N-terminal domain of human copper transporter CTR1 specifically and reversibly binds copper and silver, bacteria that synthesize the GB1-NdCTR1 become resistant to silver ions.

Funder

Russian Science Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2023/DT/D2DT04060C

Reference112 articles.

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