The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction (Q57976446)

Francesca Cantini

3

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Antonio Rosato

Antonio Rosato

8

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Isabella C Felli

Isabella C Felli

4

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Roberta Pierattelli

Roberta Pierattelli

7

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Ivano Bertini

2

Ivano Bertini

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Leonardo Gonnelli

5

Leonardo Gonnelli

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Nick Hadjiliadis

6

Nick Hadjiliadis

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author name string

Petros Voulgaris

https://scigraph.springernature.com/pub.10.1038/nchembio797

9

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publication date

28 May 2006

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published in

Nature Chemical Biology

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volume

2

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issue

7

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page(s)

367-368

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exact match

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cites work

Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

Copper-mediated homo-dimerisation for the HAH1 metallochaperone

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1.

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

Copper-dependent protein-protein interactions studied by yeast two-hybrid analysis.

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

An atomic-level investigation of the disease-causing A629P mutant of the Menkes protein, ATP7A.

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone, HAH1p

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

Kinetic analysis of the interaction of the copper chaperone Atox1 with the metal binding sites of the Menkes protein

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

Understanding copper trafficking in bacteria: interaction between the copper transport protein CopZ and the N-terminal domain of the copper ATPase CopA from Bacillus subtilis

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021

Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO797

7 January 2021