The latest

The Structure of Metal Binding Domain 1 of the Copper Transporter ATP7B Reveals Mechanism of a Singular Wilson Disease Mutation.

Yu, C.H., Lee, W., Nokhrin, S.,  and Dmitriev, O.Y. (2018) Sci. Rep. 8581.

The metal chaperone Atox1 regulates the activity of the human copper transporter ATP7B by modulating domain dynamics.

Yu, C.H., Yang, N., Bothe, J., Tonelli, M., Nokhrin, S., Braiterman, L., Dolgova, N.V., Lutsenko, S. and Dmitriev, O.Y. (2017)  J. Biol. Chem., 292: 18169-18177.

Binding of Copper and Cisplatin to Atox1 is Mediated by Glutathione through the Formation of Metal-Sulfur Clusters.

Dolgova, N.V., Yu. C., Cvitkovic, J.P., Hodak, M., Nienaber, K., Summers, K.L., Cotelesage, J., Bernholc, J., Kaminski, G.A., Pickering, I.J., George, G.N., and  Dmitriev, O.Y. (2017), Biochemistry,  56: 3129–3141

Dynamics of the metal binding domains and regulation of the human copper transporters ATP7B and ATP7A.

Yu, C.H., Dolgova, N.V., and Dmitriev, O.Y.  (2017) IUBMB Life, 69: 226-235

Nanobodies as Probes for Protein Dynamics in Vitro and in Cells

Dmitriev, O.Y., Lutsenko, S., and Muyldermans,  S. (2016) J. Biol. Chem., 291: 3767-3775

Interactions Between Metal-Binding Domains Modulate Intracellular Targeting of Cu(I)-ATPase ATP7B, as Revealed by Nanobody Binding

Huang, Y., Nokhrin, S., Hassanzadeh-Ghassabeh, G., Yu, C., Yang,H., Barry, A.N.,  Tonelli, M.. Markley, J.L., Muyldermans,  S., Dmitriev, O.Y., Lutsenko, S. (2014) J. Biol. Chem., 289:32682-93

The use of nanopore analysis for discovering drugs which bind to α-synuclein for treatment of Parkinson's disease

Tavassoly, O., Kakish, J., Nokhrin, S., Dmitriev, O.Y. and Lee, J.S. (2014) Eur. J. Med. Chem. 88:42-54

Cu(II) and dopamine bind to α-synuclein and cause large conformational changes.

Tavassoly, O., Nokhrin, S., Dmitriev, O.Y. and Lee, J.S. (2014) FEBS J., 281(12):2738-53

Copper chaperone Atox1 interacts with the metal-binding domain of Wilson disease protein in cisplatin detoxification.

Dolgova, N.V., Nokhrin, S., Yu, C., George, G.N., and Dmitriev, O.Y. (2013) Biochem. J. 454:147-56

One-Step Amino Acid Selective Isotope Labeling of Proteins in Prototrophic E. coli Strains,

O’Grady, C., Rempel, B.L., Sokaribo, A. and Dmitriev, O.Y. (2012) Anal. Biochem. 426, 126-128

Molecular Events Initiating Exit of a Copper-Transporting ATPase ATP7B from the Trans-Golgi Network

Hasan, N.M., Gupta, A., Polishchuk, E.,  Yu, C.H., Polishchuk, Dmitriev, O.Y.  and Lutsenko, S. (2012)  J. Biol.Chem. 287, 36041–36050

Cell-free synthesis of membrane subunits of ATP synthase in phospholipid bicelles: NMR shows subunit a fold similar to the protein in the cell membrane.

Uhlemann, E.E., Pierson, H.E, Fillingame, R.H. and Dmitriev, O.Y.  Protein Sci. 21, 279-288

Interaction With Monomeric Subunit c Drives Insertion of ATP Synthase Subunit a into the Membrane and Primes a-c Complex Formation.

Pierson, H.E., Uhlemann, E.E. and Dmitriev, O.Y. (2011) J. Biol.Chem. 286, 38583-38591

Difference in Stability of the N-Domain Underlies Distinct Intracellular Properties of the E1064A and H1069Q Mutants of Cu-transporting ATPase ATP7B.

Dmitriev, O.Y., Bhattacharjee, A., Nokhrin, S., Uhlemann, E.E., and Lutsenko, S. (2011) J. Biol.Chem. 286, 16355-16362

Disease Mutation or Polymorphism? Cellular Copper Levels Determine the Phenotype of the Arg875 Variant of ATP7B/Wilson Disease

Gupta, A., Bhattacharjee, A., Dmitriev, O., Nokhrin, S., Braiterman, L., Hubbard, A., Lutsenko, S. (2011) Proc.Natl.Acad.Sci. USA, 108, 5390-5395

Mechanism Of Tumor Resistance To Cisplatin Mediated by the Copper Transporter ATP7B

Dmitriev, O.Y. (2011) Biochem. Cell Biol. 89, 138-147

Crystallization and Preliminary X-ray studies of the N-domain of the Wilson Disease Associated Protein

Liu, L., O'Grady,  C., Dalrymple, S.A., Prasad, L.,  Dmitriev, O. Y., and Delbaere, L.T. (2009) Acta Crystallographica F 65:621-624

The soluble metal-binding domain of copper transporter ATP7B binds and detoxifies cisplatin.

Dolgova, N.V., Olson, D., Lutsenko, S., and Dmitriev, O. Y.  (2009) Biochem. J, 419, 51-56

Interaction of Transmembrane Helices in ATP Synthase Subunit a in Solution as Revealed by Spin-Label Difference NMR

Dmitriev, O. Y., Freedman, K. H., Hermolin, J. and Fillingame, R.H. (2008) Biochim. Biophys. Acta (Bioenergetics), 1777: 227-237

Function and Regulation of Human Copper-Transporting ATPases

Lutsenko, S., Barnes, N.L., Bartee, M.Y., Dmitriev, O.Y. (2007) Physiol. Revs., 87: 1011-1046

The Rigid Connecting Loop Stabilizes Hairpin Folding of the Two Helices of the ATP Synthase Subunit c.

Dmitriev, O. and Fillingame, R.H. (2007)  Protein Science 16: 2118-2122

Solution Structure of the N-domain of Wilson Disease Protein: Unique Nucleotide-Binding Environment and Effects of Disease Mutations

Dmitriev, O., Tsivkovskii, R., Abildgaard, F., Morgan, C.T.,  Markley, J.L. and   Lutsenko, S. (2006) Proc. Natl. Acad. Sci. USA 103: 5302-5307

NMR assignment of the Wilson Disease Associated Protein N-Domain

Dmitriev, O., Tsivkovskii, R., Abildgaard, F., and   Lutsenko, S. (2006) J. Biomol. NMR, 36,  Suppl. 1:61