A distinct Cu4-thiolate cluster of human metallothionein-3 is located in the N-terminal domain-Reference-Cited by-同舟云学术

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A distinct Cu4-thiolate cluster of human metallothionein-3 is located in the N-terminal domain

Published:2002-02-07 Issue:6 Volume:7 Page:611-616
ISSN:0949-8257
Container-title:JBIC Journal of Biological Inorganic Chemistry
language:en
Short-container-title:J Biol Inorg Chem

Author:

Roschitzki Bernd,Vašák Milan

Publisher

Springer Science and Business Media LLC

Subject

Inorganic Chemistry,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s00775-002-0339-1.pdf

Cited by 49 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Structural Characterization of Cu(I)/Zn(II)-metallothionein-3 by Ion Mobility Mass Spectrometry and Top-Down Mass Spectrometry;Analytical Chemistry;2023-07-13

2. Metallothionein‐3: ⁶³Cu(I) binds to human ⁶⁸Zn₇‐βα MT3 with no preference for Cu₄‐β cluster formation;The FEBS Journal;2023-05-19

3. Metallothionein-3 attenuates the effect of Cu2+ ions on actin filaments;Journal of Inorganic Biochemistry;2023-05

4. Metallothionein-3 attenuates the effect of Cu²⁺ ions on actin filaments;2022-09-24

5. Evidence for a Long-Lived, Cu-Coupled and Oxygen-Inert Disulfide Radical Anion in the Assembly of Metallothionein-3 Cu(I)₄-Thiolate Cluster;Journal of the American Chemical Society;2022-01-05

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