Lab Intranet
Email: lutsenko@ohsu.edu
Office phone: 503-494-6953
Fax: 503-494-8393
- B.S. (Hon.), Biochemistry, 1984
- Moscow State University, Moscow, Russia
- Ph.D., Protein Chemistry, 1989
- Institute of Bioorganic Chemistry, Moscow, Russia
Dr. Lutsenko's teaching:
- CON615 (Graduate course, PMCB, 1st year)
- Biochemistry of membrane transport
[Lecture 1] [Lecture 2] [Lecture 3] - Cell Structure and Function (Medical students)
- Membrane Proteins and Lipids [PPT] [PDF
Color]
Cellular Organelles [PPT] [PDF Color]
Membrane Transport I [PPT] [PDF Color]
Membrane Transport II [PPT] [PDF Color]
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Barnes,N.,Tsivkovskii,R.,Tsivkovskaia,N.,Lutsenko,S.
(2005) The copper-transporting ATPases, Menkes and Wilson disease proteins, have distinct roles in adult and developing cerebellum J. Biol. Chem. Epub:ahead of print.
Pubmed
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Efremov,R.,Kosinsky,Y.A.,Nolde,D.E.,Tsivkovskii,R.,Arseniev,A.S.,Lutsenko,S.
(2004) Molecular modeling of the nucleotide-binding domain of the Wilson' disease protein: location of the ATP-binding site, domain dynamics, and potential effects of the major disease mutations. Biochem J. :Epub.
Pubmed
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Morgan,C.T.,Tsivkovskii,R.,Kosinsky,Y.A.,Efremov,R.,Lutsenko,S.
(2004) The distinct functional properties of the nucleotide-binding domain of ATP7B, the human Copper-transporting ATPase. Analysis of the wilson disease mutations E1064A, H1069Q, R1151H, and C1104F. J. Biol. Chem. :Epub.
Pubmed
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Ralle,M.,Lutsenko,S.,Blackburn,N.J.
(2004) 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 J. Inorg. Biochem. 98:765-74.
Pubmed
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Walker,J.M.,Huster,D.,Ralle,M.,Morgan,C.T.,Blackburn,N.J.,Lutsenko,S.
(2004) The N-terminal metal-binding site 2 of the Wilsons disease protein plays a key role in the transfer of copper from Atox1 J. Biol. Chem. 279:15376-84.
Pubmed
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Huster,D.,Lutsenko,S.
(2003) The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein J. Biol. Chem. 278:32212-8.
Pubmed
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Lutsenko,S.,Tsivkovskii,R.,Walker,J.M.
(2003) Functional properties of the human copper-transporting ATPase ATP7B (the Wilson's disease protein) and regulation by metallochaperone Atox1. Ann. NY Acad. Sci. 986:204-11.
Pubmed
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Tsivkovskii,R.,Purnat,T.,Lutsenko,S.
(2003) Copper-transporting ATPases: The key regulators of intracellular copper concentrations. Handbook of ATPases (eds. Futai, Kaplan, Wada) Wiley-VCH Verlag GmbH, Weinheim:in press.
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Ralle,M.,Lutsenko,S.,Blackburn,N.J.
(2003) X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines. J. Biol. Chem. 278:23163-70.
Pubmed
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Tsivkovskii,R.,Efremov,R.,Lutsenko,S.
(2003) The Role of the Invariant His1069 in Folding and Function of Wilson’s disease Protein, the Human Copper-transporting ATPase ATP7B. J. Biol. Chem. 278:13302-8.
Pubmed
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Gerbasi,V.,Lutsenko,S.,Lewis,E.J.
(2003) A Mutation in the ATP7B Copper Transported Causes Reduced Dopamine ß-Hydroxylase and Norepinephrine in Mouse Adrenal. Neurochem. Res. 28:867-73.
Pubmed
Designed and maintained
by Tina D. Purnat (purnatt@ohsu.edu).
Last update: July 25, 2004.
The Lutsenko Laboratory, Department
of Biochemistry and Molecular Biology, MRB 624, Mail Code L224,
Oregon Health & Science University, 3181 SW Sam Jackson Pk Rd, Portland,
OR 97239-3098
503-494-7501 (tel), 503-494-8393 (fax)
under grant number MCB-0110057. Any opinions, findings, and conclusions or recommendations
expressed in this material are those of the author(s) and do not necessarily reflect the views of the National Science Foundation.