Evidence for noncooperative metal binding to the alpha domain of human metallothionein.
about
Metalation kinetics of the human α-metallothionein 1a fragment is dependent on the fluxional structure of the apo-protein.Metal exchange in metallothioneins: a novel structurally significant Cd(5) species in the alpha domain of human metallothionein 1a.Mammalian metallothioneins: properties and functions.The "magic numbers" of metallothionein.Mammalian metallothionein in toxicology, cancer, and cancer chemotherapy.Challenging conventional wisdom: single domain metallothioneins.Defining the metal binding pathways of human metallothionein 1a: balancing zinc availability and cadmium seclusion.MT1A binds cadmium
P2860
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P2860
Evidence for noncooperative metal binding to the alpha domain of human metallothionein.
description
2007 nî lūn-bûn
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2007年の論文
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2007年学术文章
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2007年学术文章
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2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
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2007年學術文章
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2007年學術文章
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name
Evidence for noncooperative metal binding to the alpha domain of human metallothionein.
@en
Evidence for noncooperative metal binding to the alpha domain of human metallothionein.
@nl
type
label
Evidence for noncooperative metal binding to the alpha domain of human metallothionein.
@en
Evidence for noncooperative metal binding to the alpha domain of human metallothionein.
@nl
prefLabel
Evidence for noncooperative metal binding to the alpha domain of human metallothionein.
@en
Evidence for noncooperative metal binding to the alpha domain of human metallothionein.
@nl
P2860
P1433
P1476
Evidence for noncooperative metal binding to the alpha domain of human metallothionein.
@en
P2093
Kelly E Rigby Duncan
Martin J Stillman
P2860
P304
P356
10.1111/J.1742-4658.2007.05762.X
P407
P577
2007-03-27T00:00:00Z