Olga Vinogradova Lab

K. Nguyen, T. Strauss, B. Refaeli, R. Hiller, O. Vinogradova, and D. Khananshvili, “19F‐NMR Probing of Ion‐Induced Conformational Changes in Detergent‐Solubilized and Nanodisc‐Reconstituted NCX_Mj”, Int. J. Mol. Sci. 2024, 25, 6909, DOI:10.3390/ijms25136909

K. Nguyen, Y. Jin, M. Howell, C.C. Hsiao, A.J. Wiemer, and O. Vinogradova, “Mutations to the BTN2A1 linker region impact its homodimerization and its cytoplasmic interaction with phosphoantigen bound BTN3A1”, Journal of Immunology 2023, 211, 1-11, DOI:10.4049/jimmunol.2200949

R. Puthenveetil, E.T. Christenson, and O. Vinogradova, "New Horizons in Structural Biology of Membrane Proteins: Experimental Evaluation of the Role of Conformational Dynamics and Intrinsic Flexibility", Review, Membranes 2022, 12, 227, DOI:10.3390/membranes12020227.

C.C. Hsiao, K. Nguyen, Y. Jin, O. Vinogradova, and A.J. Wiemer, “Ligand-induced interactions between Butyrophilin 2A1 and 3A1 internal domains in the HMBPP receptor complex”, Cell Chemical Biology 2022, 29, 1–11, DOI:10.1016/j.chembiol.2022.01.004 https://doi.org/10.1016/j.chembiol.2022.01.004

B. J. Aneskievich, Shamilov, and O. Vinogradova, "Intrinsic disorder in integral membrane proteins', PMBTS 2021, Book Chapter. DOI:10.1016/bs.pmbts.2021.06.002. https://www.sciencedirect.com/science/article/pii/S1877117321000880

R. Shamilov, O. Vinogradova, and B.J. Aneskievich, “The Anti-Inflammatory Protein TNIP1 Is Intrinsically Disordered with Structural Flexibility Contributed by Its AHD1-UBAN Domain”, Biomolecules 2020, 10(11), 1531, DOI: 10.3390/biom10111531. https://www.mdpi.com/2218-273X/10/11/1531

R. Puthenveetil, and O. Vinogradova, “Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments”, JBC 2019, Review. DOI: 10.1074/jbc.REV119.009178. http://www.jbc.org/content/294/44/15914

P. Katyal, Y. Yang, Y. Fu, J. Iandosca, O. Vinogradova, and Y. Lin, "Binding and backbone dynamics of protein under topological constraint: calmodulin as a model system", Chem.Comm 2018, https://pubs.rsc.org/en/content/articlelanding/2018/cc/c8cc03977a

K. Nguyen, E. Zecca, O. Vinogradova, and D.S. Kalonia, "NMR as a Semi-Quantitative Tool for Evaluating Protein Surface Hydrophobicity", SciFed Pharmaceutics Journal 2018, https://olga-vinogradova.media.uconn.edu/wp-content/uploads/sites/1741/2021/09/2018_SFPJ_Kalonia.pdf

R. Puthenveetil, S. Kumar, M.J. Caimano, A. Dey, A. Anand, O. Vinogradova, and J.D. Radolf, “The major outer sheath protein forms distinct conformers and multimeric complexes in the outer membrane and periplasm of Treponema denticola”,  Scientific Reports 2017, https://www.nature.com/articles/s41598-017-13550-6

K. Nguyen, J. Li, R. Puthenveetil, X. Lin, C.C. Hsiao, O. Vinogradova, and A.J. Wiemer, “The butyrophilin 3A1 intracellular domain undergoes a conformational change involving the juxtamembrane region”, FASEB Journal 2017, BTN3A1.

R. Shippy, X. Lin, S. Agabiti, J. Li, B. Zangari, B. Foust, C.C. Hsiao, O. Vinogradova, D.F. Wiemer, and  A.J. Wiemer, “Phosphinophosphonates and their tris-pivaloyloxymethyl prodrugs reveal a negatively cooperative butyrophilin activation mechanism”, Journal of Medicinal Chemistry 2017, DOI: 10.1021/acs.jmedchem.6b00965

P. Katyal, Y. Yang,  O. Vinogradova, and Y. Lin, "Expression of Cellulolytic Enzyme as a Fusion Protein That Reacts Specifically With a Polymeric Scaffold", Methods in Enzymology 2017, http://dx.doi.org/10.1016/bs.mie.2016.12.003.

K. Nguyen, R. Puthenveetil, and O. Vinogradova, “Investigation of the adaptor protein PLIC-2 in multiple pathways”, Biochem Biophys Rep. 2017, http://dx.doi.org/10.1016/j.bbrep.2017.01.013.

R. Puthenveetil, K. Nguyen, and O. Vinogradova, “Nanodiscs and Solution NMR: preparation, application and challenges”, Nanotechnology Reviews 2017, ISSN (Online) 2191-9097, ISSN (Print) 2191-9089, DOI: https://doi.org/10.1515/ntrev-2016-0076. Open access copy: PubMed central.

S. Fiorucci, X. Lin, K. Sadoul, G. Fournet, D. Bouvard, O. Vinogradova, B. Joseph, and M.R. Block, “Targeting Integrin-dependent Adhesion and Signaling with 3-Arylquinoline and 3-Aryl-2-quinolone Derivatives: A new Class of Integrin Antagonists”, PLoS One 2015, 10, e0141205.

A. Anand, M. LeDoyt, C. Karanian, A. Luthra, M. Koszelak-Rosenblum3, M.G. Malkowski,  R. Puthenveetil, O. Vinogradova, and J.D. Radolf “Bipartite Topology of Treponema pallidum Repeat Proteins C/D and I: Outer Membrane Insertion and Porin Function Requires a C-terminal β-barrel Domain”, JBC 2015, 290, 12313–12331. Tpr-MOSP

X. Lin and O. Vinogradova, "Phospho-Tyrosine(s) vs. Phos¬phatidylinositol Binding in Shc Mediated Integrin Signaling", AJMB 2015, 5: 17-31. Phospho-Tyr-Ins

V. Gorbatyuk, K. Nguyen, N.P. Podolnikova, L. Deshmukh, X. Lin, T.P. Ugarova and O. Vinogradova, “Skelemin Association with aIIbβ3 Integrin: A Structural Model”, Biochemistry 2014, 53: 6766-6775. Skelemin-tertiary-complex

C.C. Hsiao, X. Lin, R.J. Barney, R.R. Shippy, J. Li, O. Vinogradova, D.F. Wiemer, and A.J. Wiemer, “Synthesis of a novel phosphoantigen prodrug that potently activates Vγ9Vδ2 T-lymphocytes”, Chemistry & Biology 2014, 21:945–954. Butyrophilin-phosphoantigen

P. Katyal, R. Puthenveetil and O. Vinogradova, “Structural Insights into the Recognition of β3 Integrin Cytoplasmic Tail by SH3 Domain of Src Kinase”, Protein Science 2013, 22: 1358-65. SH3-Src

R. Puthenveetil and O. Vinogradova, “Optimization of the Design and Preparation of Nanoscale Phospholipid Bilayers for its Application to Solution NMR”, Proteins 2013, 81: 1222-1231. Minimal-Nanodiscs

O. Vinogradova,  and J. Qin, “NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions”. Springer, Topics in Current Chemistry  2012, NMR of Proteins and Small Biomolecules. [review] NMR of weak protein interactions

X. Z. West, N. Meller, N. L. Malinin, L. Deshmukh, J. Meller, G.H. Mahabeleshwar, M.E. Weber, B.A. Kerr, O. Vinogradova, T.V. Byzova (2012) “Integrin β3 crosstalk with VEGFR accommodating tyrosine phosphorylation as a regulatory switch”, PLos One 2012, 7:e31071.[top 25% citations] B3-VEGFR

D. Bona, L. Deshmukh, V. Gorbatyuk, O. Vinogradova, D. A. Kendall, “Structural Studies of a Signal Peptide in Complex with Signal Peptidase I Cytoplasmic Domain: the Stabilizing Effect of Membrane-Mimetics on the Acquired Fold”, Proteins 2011, 80, 807-817.

Deshmukh, N. Meller, N. Alder, T. Byzova, O. Vinogradova, “Tyrosine Phosphorylation as a Conformational Switch: A Case Study of Integrin β3 Cytoplasmic Tail”, JBC 2011, 47, 40943-53. B3-phosphorylation

Deshmukh, V. Gorbatyuk, O. Vinogradova, “Integrin β₃ Phosphorylation Dictates its Complex with Shc PTB Domain”, JBC 2010, 285, 34875-84. Shc-PTB

J. M. Beierlein, L. Deshmukh, K. M. Frey, O. Vinogradova, A. C. Anderson. “The Solution Structure of Bacillus anthracis Dihydrofolate Reductase Yields Insight into the Analysis of Structure-Activity Relationships for Novel Inhibitors”, Biochemistry 2009, 48, 4100-4108. [chosen as a "recommended" read by the Faculty of 1000]

L. Deshmukh, L. Wu, R. P. Guttmann, O. Vinogradova, “NMR Structural Characterization of the Penta-Peptide Calpain Inhibitor”, FEBS Letters 2009, 583, 135-40.

Tyukhtenko, L. Deshmukh, V. Kumar, J. Lary, J. Cole, V. Lemmon, O. Vinogradova, “Characterization of neuron specific L1-CAM cytoplasmic tail: Naturally disordered in solution it exercises different binding modes for different adaptor proteins”, Biochemistry 2008, 47, 4160-4168. [chosen as a “Hot Article”] L1-CAM

Deshmukh, S. Tyukhtenko, J. Liu, J.E.B. Fox, J. Qin and O. Vinogradova, “Structural Insight into the Interaction between Platelet Integrin a_IIbb₃ and Cytoskeletal Protein Skelemin”, JBC 2007, 288, 32349-32356. Skelemin

Mao, J. Yang, M. Pesho, O. Vinogradova, J. Qin, and E. Plow, “Regulation of Integrin AlphaIIbBeta3 Activation by Distinct Regions of its Cytoplasmic Tails”, Biochemistry 2006, 45, 6656-62.

J. Vaynberg, T. Fukuda, K. Chen, O. Vinogradova, A. Velyvis, Y. Tu, L. Ng, C. Wu, and J. Qin, “Structure of an Ultraweak Protein-Protein Complex and Its Crucial Role in Regulation of Cell Morphology and Motility”, Molecular Cell 2005, 17, 513-523. [chosen as a "recommended" read by the Faculty of 1000]

J. Qin, O. Vinogradova, E.F. Plow, “Integrin bidirectional signaling: a molecular view”, PLoS Biol. 2004, 6, 726-9. Review.

O. Vinogradova, J. Vaynberg, X. Kong, T. Haas, E.F. Plow, J. Qin, “Membrane-mediated structural transition at the cytoplasmic face during integrin activation”, Proc. Natl. Acad. Sci. 2004, 101, 4094-99. Integrins-membrane

A. Velyvis, J. Vaynberg, Y. Yang, O. Vinogradova, Y. Zhang, C. Wu, J. Qin, “Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling”, Nature Structural Biology 2003, 10(7), 558-64.

O. Vinogradova, A. Velyvis, A. Velyviene, B. Hu, T. Haas, E.F. Plow, J. Qin, “A structural mechanism of integrin a_IIbb₃ “inside-out” activation as regulated by its cytoplasmic face”, Cell 2002, 110, 587-97. [chosen as an "exceptional" read by the Faculty of 1000] Integrins-Cell

O. Vinogradova, T. Haas, E.F. Plow, J. Qin, "Structural Basis for Integrin Activation by the Cytoplasmic Tail of the a_IIb Subunit”, Proc. Natl. Acad. Sci.  2000, 97, 1450-1455. Integrins-PNAS

L. Czerski, O. Vinogradova, C.R. Sanders, "NMR-Based Amide Hydrogen-Deuterium Exchange Measurements for Complex Membrane Proteins: Development and Critical Evaluation”, J. of. Mag. Res. 2000, 142, 111-119.

L. Tsai, P.A. Szweda, O. Vinogradova, and L.I. Szweda, "Structural Characterization and Immunochemical Detection of a Fluorophore Derived from 4-Hydroxy-2-nonenal and Lysine”, Proc. Natl. Acad. Sci.  1998, 95, 7975-7980.

O. Vinogradova, F. Soennichsen, and C.R. Sanders, "On Choosing a Detergent for Solution NMR Studies of Membrane Proteins”, J. of BioMol. NMR 1998, 4, 381-386. Detergents-BioNMR

O. Vinogradova, C. Carlin, F.D. Soennichsen, and C.R. Sanders, "A Membrane Setting for the Sorting Motifs Present in the Adenovirus E3-13.7 Protein which Down-Regulates the Epidermal Growth Factor Receptor", J. Biol. Chem. 1998, 273, 17343-17350.

O. Vinogradova, P. Badola, L.. Czerski, F.D. Sonnichsen, and C.R. Sanders, "E.Coli Diacylglycerol Kinase: A Case Study in the Application of Solution NMR Methods to an Integral Membrane Protein”, Biophysical J. 1997, 72, 2688-2701.