Copper transfer to the N-terminal domain of the Wilson disease protein (ATP7B): X-ray absorption spectroscopy of reconstituted and chaperone-loaded metal binding domains and their interaction with exogenous ligands

2004 ◽  
Vol 98 (5) ◽  
pp. 765-774 ◽  
Author(s):  
Martina Ralle ◽  
Svetlana Lutsenko ◽  
Ninian J. Blackburn
Metallomics ◽  
2019 ◽  
Vol 11 (9) ◽  
pp. 1472-1480 ◽  
Author(s):  
Kumaravel Ponnandai Shanmugavel ◽  
Pernilla Wittung-Stafshede

Using a yeast assay, we identified the roles of ATP7B's six metal-binding domains in internal copper transport and soluble chaperone capacity.


2010 ◽  
Vol 114 (10) ◽  
pp. 3698-3706 ◽  
Author(s):  
Agustina Rodriguez-Granillo ◽  
Alejandro Crespo ◽  
Dario A. Estrin ◽  
Pernilla Wittung-Stafshede

Biochemistry ◽  
2008 ◽  
Vol 47 (28) ◽  
pp. 7423-7429 ◽  
Author(s):  
Lucia Banci ◽  
Ivano Bertini ◽  
Francesca Cantini ◽  
Amy C. Rosenzweig ◽  
Liliya A. Yatsunyk

BioMetals ◽  
2016 ◽  
Vol 30 (1) ◽  
pp. 27-35 ◽  
Author(s):  
Ranjeet Kumar ◽  
Candan Ariöz ◽  
Yaozong Li ◽  
Niklas Bosaeus ◽  
Sandra Rocha ◽  
...  

Metallomics ◽  
2017 ◽  
Vol 9 (7) ◽  
pp. 981-988 ◽  
Author(s):  
Kumaravel Ponnandai Shanmugavel ◽  
Dina Petranovic ◽  
Pernilla Wittung-Stafshede

A double deleted yeast system was developed to probe activity of human ATP7B variants in the presence of human Atox1.


Biochemistry ◽  
2006 ◽  
Vol 45 (20) ◽  
pp. 6495-6509 ◽  
Author(s):  
Massimiliano Stola ◽  
Francesco Musiani ◽  
Stefano Mangani ◽  
Paola Turano ◽  
Niyaz Safarov ◽  
...  

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