Kinetic Analysis of Arsenic−Metalation of Human Metallothionein: Significance of the Two-Domain Structure-Reference-Cited by-同舟云学术

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Kinetic Analysis of Arsenic−Metalation of Human Metallothionein: Significance of the Two-Domain Structure

Published:2008-11-19 Issue:50 Volume:130 Page:17016-17028
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Ngu Thanh T.¹,Easton Alexandria¹,Stillman Martin J.¹

Affiliation:

1. Department of Chemistry, The University of Western Ontario, London, Ontario, Canada, N6A 5B7

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja8060326

Reference78 articles.

1. Arsenic Binding to Human Metallothionein

Cited by 65 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. ESI–MS analysis of Cu(I) binding to apo and Zn7 human metallothionein 1A, 2, and 3 identifies the formation of a similar series of metallated species with no individual isoform optimization for Cu(I);Metallomics;2024-03-19

2. Supermetalation of Cd-MT3 beyond the two-domain model;Journal of Inorganic Biochemistry;2023-12

3. Xenobiotic Bi³⁺ Coordination by Cysteine-Rich Metallothionein-3 Reveals a Cooperatively Formed Thiolate-Sharing Bi₂S₅ Cluster;Inorganic Chemistry;2023-08-03

4. Arsenic binding to human metallothionein-3;Chemical Science;2023

5. An ion mobility-mass spectrometry study of copper-metallothionein-2A: binding sites and stabilities of Cu-MT and mixed metal Cu–Ag and Cu–Cd complexes;The Analyst;2023

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