Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in? - Wikidata - awgldk - TriplyDB

Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in?

Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in?

http://www.wikidata.org/entity/Q39383441

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Chemistry of mammalian metallothioneins and their interaction with amyloidogenic peptides and proteins.Intracellular metal binding and redox behavior of human DJ-1.Differential reactivity of closely related zinc(II)-binding metallothioneins from the plant Arabidopsis thaliana.

P2860

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P2860

Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in?

http://www.wikidata.org/entity/Q39383441

description

2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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2017年學術文章

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name

Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in?

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Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in?

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Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in?

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Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in?

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Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in?

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Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in?

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International Journal of Molecular Sciences

P1476

Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in?

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Afsana Mahim

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David H Petering

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Creative Commons Attribution

P2860

The Functions of Metallothionein and ZIP and ZnT Transporters: An Overview and Perspective

Metal responsive transcription factor 1 (MTF-1) regulates zinc dependent cellular processes at the molecular level

Charting the travels of copper in eukaryotes from yeast to mammals

Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2

Biochemistry of mobile zinc and nitric oxide revealed by fluorescent sensors.

Zinc and cadmium can promote rapid nuclear translocation of metal response element-binding transcription factor-1

The transcription factor MTF-1 mediates metal regulation of the mouse ZnT1 gene

Metalation kinetics of the human α-metallothionein 1a fragment is dependent on the fluxional structure of the apo-protein.

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

Counting the zinc-proteins encoded in the human genome.

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scholarly article

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10.3390/IJMS18061289

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2017-06-17T00:00:00Z

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inorganic compound

transport protein

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