O. Dmitriev

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

Corey H Yu, Woonghee Lee, S. Nokhrin, 2018, Scientific Reports.

Crystallization and preliminary X-ray studies of the N-domain of the Wilson disease associated protein.

L. Prasad, L. Delbaere, O. Dmitriev, 2009, Acta crystallographica. Section F, Structural biology and crystallization communications.

Subunit a of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent

R. H. Fillingame, K. Altendorf, O. Dmitriev, 2004, FEBS letters.

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

R. H. Fillingame, O. Dmitriev, H. Pierson, 2012, Protein science : a publication of the Protein Society.

One-step amino acid selective isotope labeling of proteins in prototrophic Escherichia coli strains.

A. Sokaribo, S. Nokhrin, O. Dmitriev, 2012, Analytical biochemistry.

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

Douglas J. H. Olson, S. Lutsenko, O. Dmitriev, 2009, The Biochemical journal.

The KH domain facilitates the substrate specificity and unwinding processivity of DDX43 helicase.

M. Cygler, A. Kusalik, V. Vidhyasagar, 2020, The Journal of biological chemistry.

Defining the domain of binding of F1 subunit epsilon with the polar loop of F0 subunit c in the Escherichia coli ATP synthase.

R. H. Fillingame, Y. Zhang, O. Dmitriev, 1999, The Journal of biological chemistry.

Letter to the Editor: Backbone 1H, 15N and 13C Assignments for the Subunit a of the E. Coli ATP Synthase

J. Markley, R. H. Fillingame, F. Abildgaard, 2004, Journal of biomolecular NMR.

Function and regulation of human copper-transporting ATPases.

Svetlana Lutsenko, Oleg Y Dmitriev, S. Lutsenko, 2007, Physiological reviews.

Solution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutations.

J. Markley, F. Abildgaard, S. Lutsenko, 2006, Proceedings of the National Academy of Sciences of the United States of America.

Structural interpretations of F0 rotary function in the Escherichia coli F1F0 ATP synthase

R. H. Fillingame, O. Dmitriev, Robert H. Fillingame, 2000 .

Structure of Ala20 → Pro/Pro64 → Ala Substituted Subunit c ofEscherichia coli ATP Synthase in Which the Essential Proline Is Switched between Transmembrane Helices*

R. H. Fillingame, O. Dmitriev, 2001, The Journal of Biological Chemistry.

The Oligomeric Subunit c Rotor in the Fo Sector of ATP Synthase: Unresolved Questions in Our Understanding of Function

R. H. Fillingame, O. Dmitriev, Weiping Jiang, 2000, Journal of bioenergetics and biomembranes.

Nanobodies as Probes for Protein Dynamics in Vitro and in Cells*

Serge Muyldermans, S. Muyldermans, Svetlana Lutsenko, 2015, The Journal of Biological Chemistry.

Coupling H(+) transport to rotary catalysis in F-type ATP synthases: structure and organization of the transmembrane rotary motor.

R. H. Fillingame, W. Jiang, R H Fillingame, 2000, The Journal of experimental biology.

Engineered Protein Model of the ATP synthase H+- Channel Shows No Salt Bridge at the Rotor-Stator Interface

O. Dmitriev, H. Pierson, E. Uhlemann, 2018, Scientific Reports.

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

O. Dmitriev, H. Pierson, E. Uhlemann, 2011, The Journal of Biological Chemistry.

Mechanics of coupling proton movements to c‐ring rotation in ATP synthase

R. H. Fillingame, O. Dmitriev, Robert H Fillingame, 2003, FEBS letters.

Reconstitution of the F0 Complex of Escherichia coll ATP Synthase from Isolated Subunits

R. H. Fillingame, K. Altendorf, O. Dmitriev, 1995 .

Reconstitution of the Fo complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by co-incorporation of wild-type and mutant subunit c after purification in organic solvent.

R. H. Fillingame, K. Altendorf, O. Dmitriev, 1995, European journal of biochemistry.

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

G. George, S. Nokhrin, O. Dmitriev, 2013, The Biochemical journal.

Mechanism of tumor resistance to cisplatin mediated by the copper transporter ATP7B.

O. Dmitriev, 2011, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Difference in Stability of the N-domain Underlies Distinct Intracellular Properties of the E1064A and H1069Q Mutants of Copper-transporting ATPase ATP7B*

S. Lutsenko, S. Nokhrin, O. Dmitriev, 2011, The Journal of Biological Chemistry.

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

Jeremy S. Lee, Omid Tavassoly, S. Nokhrin, 2014, The FEBS journal.

At sixes and sevens: a cryptic domain in the metal binding chain of the human copper transporter ATP7A.

M. Tonelli, Woonghee Lee, O. Dmitriev, 2021, Biophysical journal.

Nanobodies against the metal binding domains of ATP7B as tools to study copper transport in the cell.

S. Muyldermans, N. Dolgova, S. Lutsenko, 2020, Metallomics : integrated biometal science.

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

M. Tonelli, L. Braiterman, N. Dolgova, 2017, The Journal of Biological Chemistry.

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

N. Dolgova, O. Dmitriev, Corey H. Yu, 2017, IUBMB Life - A Journal of the International Union of Biochemistry and Molecular Biology.

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

R. Polishchuk, E. Polishchuk, S. Lutsenko, 2012, The Journal of Biological Chemistry.

expression in an infant rat model absorption, tissue distribution, and copper transporter Effects of copper supplementation on copper

L. Braiterman, B. Eipper, S. Kelleher, 2011 .

Coupling proton movements to c-ring rotation in F(1)F(o) ATP synthase: aqueous access channels and helix rotations at the a-c interface.

R. H. Fillingame, C. Angevine, Oleg Y Dmitriev, 2002, Biochimica et biophysica acta.

Defining the Domain of Binding of F1 Subunit ε with the Polar Loop of F0 Subunit c in theEscherichia coli ATP Synthase*

R. H. Fillingame, O. Dmitriev, Ying Zhang, 1999, The Journal of Biological Chemistry.

The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c

Oleg Y Dmitriev, Robert H Fillingame, O. Dmitriev, 2007, Protein science : a publication of the Protein Society.

Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ.

R. H. Fillingame, O. Dmitriev, 2002, Biochimica et biophysica acta.

Structure of the subunit c oligomer in the F1Fo ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme.

R. H. Fillingame, R H Fillingame, P C Jones, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Structure of the Membrane Domain of Subunit b of the Escherichia coli F0F1 ATP Synthase*

R. H. Fillingame, O. Dmitriev, Phil C. Jones, 1999, The Journal of Biological Chemistry.

Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase.

R. H. Fillingame, W. Jiang, O. Dmitriev, 1998, Biochimica et biophysica acta.

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

S. Muyldermans, J. Markley, Yiping Huang, 2014, The Journal of Biological Chemistry.

The KH domain facilitates the substrate specificity and unwinding processivity of DDX43 helicase

M. Cygler, A. Kusalik, V. Vidhyasagar, 2020, The Journal of biological chemistry.

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

Jeremy S. Lee, Omid Tavassoly, S. Nokhrin, 2014, European journal of medicinal chemistry.

Molecular Architecture of the Copper-Transporting ATPase ATP7B

S. Lutsenko, O. Dmitriev, S. Jayakanthan, 2019, Clinical and Translational Perspectives on WILSON DISEASE.

MEMO1 is a Metal Containing Regulator of Iron Homeostasis in Cancer Cells

Frederick S. Vizeacoumar, Franco J. Vizeacoumar, F. Vizeacoumar, 2023, bioRxiv.

Interaction of transmembrane helices in ATP synthase subunit a in solution as revealed by spin label difference NMR.

R. H. Fillingame, O. Dmitriev, J. Hermolin, 2008, Biochimica et biophysica acta.

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

George A. Kaminski, J. Bernholc, M. Hodak, 2017, Biochemistry.

One-step amino acid selective isotope labeling of proteins in prototrophic Escherichia coli strains.

A. Sokaribo, S. Nokhrin, O. Dmitriev, 2012, Analytical biochemistry.

F0F1‐ATPase from Vibrio alginolyticus Subunit composition and proton pumping activity

S. Papa, V. Skulachev, O. Dmitriev, 1991, FEBS Letters.

The F1‐ATPase of vibrio alginolyticus

V. Skulachev, O. Dmitriev, V. Grinkevich, 1989, FEBS letters.

The properties and structure of the membrane ATPase from Vibrio alginolyticus

B. Chernyak, O. Dmitriev, 1988 .

NMR assignment of the Wilson disease associated protein N-domain

F. Abildgaard, S. Lutsenko, O. Dmitriev, 2006, Journal of biomolecular NMR.

Cellular copper levels determine the phenotype of the Arg875 variant of ATP7B/Wilson disease protein

L. Braiterman, A. Hubbard, S. Lutsenko, 2011, Proceedings of the National Academy of Sciences.