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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, 2018-08, Vol.38 (4)

2018

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Residue Modification and Mass Spectrometry for the Investigation of Structural and Metalation Properties of Metallothionein and Cysteine-Rich Proteins

International journal of molecular sciences, 2017-04, Vol.18 (5), p.913

2017

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Selective cysteine modification of metal‐free human metallothionein 1a and its isolated domain fragments: Solution structural properties revealed via ESI‐MS

Protein science, 2017-05, Vol.26 (5), p.960-971

2017

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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

Biochimica et biophysica acta. Proteins and proteomics, 2018-05, Vol.1866 (5-6), p.589-601

2018

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Stepwise copper(i) binding to metallothionein: a mixed cooperative and non-cooperative mechanism for all 20 copper ions

Metallomics, 2017-05, Vol.9 (5), p.447

2017

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Cadmium binding mechanisms of isolated domains of human MT isoform 1a: Non-cooperative terminal sites and cooperative cluster sites

Journal of inorganic biochemistry, 2016-05, Vol.158, p.115-121

2016

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Defining the metal binding pathways of human metallothionein 1a: balancing zinc availability and cadmium seclusion

Metallomics, 2016-01, Vol.8 (1), p.71-81

2016

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Topographical analysis of As-induced folding of α-MT1a

Biochemical and biophysical research communications, 2013-11, Vol.441 (1), p.208-213

2013

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Cysteine accessibility during As3+ metalation of the α- and β-domains of recombinant human MT1a

Biochemical and biophysical research communications, 2013-04, Vol.433 (4), p.477-483

2013

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Formation of oxidative and non‐oxidative dimers in metallothioneins: Implications for charge‐state analysis for structural determination

Rapid communications in mass spectrometry, 2017-12, Vol.31 (24), p.2118-2124

2017

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Domain Selection in Metallothionein 1A: Affinity-Controlled Mechanisms of Zinc Binding and Cadmium Exchange

Biochemistry (Easton), 2015-08, Vol.54 (32), p.5006-5016

2015

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Isolated domains of recombinant human apo-metallothionein 1A are folded at neutral pH: a denaturant and heat-induced unfolding study using ESI-MS

Residue Modification and Mass Spectrometry for the Investigation of Structural and Metalation Properties of Metallothionein and Cysteine-Rich Proteins

Selective cysteine modification of metal‐free human metallothionein 1a and its isolated domain fragments: Solution structural properties revealed via ESI‐MS

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

Stepwise copper(i) binding to metallothionein: a mixed cooperative and non-cooperative mechanism for all 20 copper ions

Cadmium binding mechanisms of isolated domains of human MT isoform 1a: Non-cooperative terminal sites and cooperative cluster sites

Defining the metal binding pathways of human metallothionein 1a: balancing zinc availability and cadmium seclusion

Topographical analysis of As-induced folding of α-MT1a

Cysteine accessibility during As3+ metalation of the α- and β-domains of recombinant human MT1a

Formation of oxidative and non‐oxidative dimers in metallothioneins: Implications for charge‐state analysis for structural determination

Domain Selection in Metallothionein 1A: Affinity-Controlled Mechanisms of Zinc Binding and Cadmium Exchange

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