Chromatographic separation of similar post-translationally modified metallothioneins reveals the changing conformations of apo-MT upon cysteine alkylation by high resolution LC-ESI-MS-Reference-Cited by-同舟云学术

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Chromatographic separation of similar post-translationally modified metallothioneins reveals the changing conformations of apo-MT upon cysteine alkylation by high resolution LC-ESI-MS

Published:2018-05 Issue:5-6 Volume:1866 Page:589-601
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Irvine Gordon W.,Stillman Martin J.

Funder

NSERC

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference53 articles.

1. Metallothioneins

2. The “magic numbers” of metallothionein

3. A CADMIUM PROTEIN FROM EQUINE KIDNEY CORTEX

Cited by 4 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. Posttranslational modifications and metal stress tolerance in plants;Biostimulants in Alleviation of Metal Toxicity in Plants;2023

2. Mass spectrometric imaging of cysteine rich proteins in human skin;International Journal of Biological Macromolecules;2019-03

3. Kinetics of competitive Cd2+ binding pathways: the realistic structure of intrinsically disordered, partially metallated metallothioneins;Metallomics;2019-01-31

4. Isolated domains of recombinant human apo-metallothionein 1A are folded at neutral pH: a denaturant and heat-induced unfolding study using ESI-MS;Bioscience Reports;2018-07-18

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