Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.

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Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.

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Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.

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Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.

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Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.

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Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.

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Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.

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P1476

Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p

@en

P2093

Gabriel Žoldák

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P2860

Spectral and kinetic properties of the Fet3 protein from Saccharomyces cerevisiae, a multinuclear copper ferroxidase enzyme.

In vitro unfolding of yeast multicopper oxidase Fet3p variants reveals unique role of each metal site.

Role of copper in folding and stability of cupredoxin-like copper-carrier protein CopC.

Discrete roles of copper ions in chemical unfolding of human ceruloplasmin.

Role of cofactors in folding of the blue-copper protein azurin.

The copper-iron connection in biology: structure of the metallo-oxidase Fet3p.

Molecular dynamics of a thermostable multicopper oxidase from Thermus thermophilus HB27: structural differences between the apo and holo forms.

FET3P, ceruloplasmin, and the role of copper in iron metabolism.

Role of cofactors in metalloprotein folding.

Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase.

P31

scholarly article

P356

10.3390/IJMS19010269

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Pernilla Wittung-Stafshede

Gabriel Zoldak

Erik Sedlák

P577

2018-01-16T00:00:00Z

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P698

29337899

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P932

5796215

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