Selected publications

M. B. Dolinska, K. L. Young, 2nd, C. Kassouf, E. K. Dimitriadis, P. T. Wingfield and Y. V. Sergeev: Protein Stability and Functional Characterization of Intra-Melanosomal Domain of Human Recombinant Tyrosinase-Related Protein 1. Int J Mol Sci, 21(1) (2020) doi:10.3390/ijms21010331

K. L. Young, II, C. Kassouf, M. B. Dolinska, D. E. Anderson and Y. V. Sergeev: Human Tyrosinase: Temperature-Dependent Kinetics of Oxidase Activity. Int J Mol Sci, 21(3) (2020) doi:10.3390/ijms21030895

F. W. Ortiz and Y. V. Sergeev: Global computational mutagenesis of domain structures associated with inherited eye disease. Sci Rep, 9(1), 3676 (2019) doi:10.1038/s41598-019-39905-9

M. B. Dolinska, P. T. Wingfield, K. L. Young, 2nd and Y. V. Sergeev: The TYRP1-mediated protection of human tyrosinase activity does not involve stable interactions of tyrosinase domains. Pigment Cell Melanoma Res, 32(6), 753-765 (2019) doi:10.1111/pcmr.12791

N. J. Kus, M. B. Dolinska, K. L. Young, 2nd, E. K. Dimitriadis, P. T. Wingfield and Y. V. Sergeev: Membrane-associated human tyrosinase is an enzymatically active monomeric glycoprotein. PLoS One, 13(6), e0198247 (2018) doi:10.1371/journal.pone.0198247

M. B. Dolinska, P. T. Wingfield and Y. V. Sergeev: Purification of Recombinant Human Tyrosinase from Insect Larvae Infected with the Baculovirus Vector. Curr Protoc Protein Sci, 89, 6 15 1-6 15 12 (2017) doi:10.1002/cpps.37

M. B. Dolinska, N. J. Kus, S. K. Farney, P. T. Wingfield, B. P. Brooks and Y. V. Sergeev: Oculocutaneous albinism type 1: link between mutations, tyrosinase conformational stability, and enzymatic activity. Pigment Cell Melanoma Res, 30(1), 41-52 (2017) doi:10.1111/pcmr.12546

C. L. McCafferty and Y. V. Sergeev: Global computational mutagenesis provides a critical stability framework in protein structures. PLoS One, 12(12), e0189064 (2017) doi:10.1371/journal.pone.0189064

C. L. McCafferty and Y. V. Sergeev: Dataset of eye disease-related proteins analyzed using the unfolding mutation screen. Sci Data, 3, 160112 (2016) doi:10.1038/sdata.2016.112

C. L. McCafferty and Y. V. Sergeev: In silico Mapping of Protein Unfolding Mutations for Inherited Disease. Sci Rep, 6, 37298 (2016) doi:10.1038/srep37298

M. B. Dolinska, E. Kovaleva, P. Backlund, P. T. Wingfield, B. P. Brooks and Y. V. Sergeev: Albinism-causing mutations in recombinant human tyrosinase alter intrinsic enzymatic activity. PLoS One, 9(1), e84494 (2014) doi:10.1371/journal.pone.0084494

Y. V. Sergeev, M. B. Dolinska and P. T. Wingfield: Thermodynamic analysis of weak protein interactions using sedimentation equilibrium. Curr Protoc Protein Sci, 77, 20 13 1-20 13 15 (2014) doi:10.1002/0471140864.ps2013s77

Y. V. Sergeev, R. C. Caruso, M. R. Meltzer, N. Smaoui, I. M. MacDonald and P. A. Sieving: Molecular modeling of retinoschisin with functional analysis of pathogenic mutations from human X-linked retinoschisis. Hum Mol Genet, 19(7), 1302-13 (2010) doi:10.1093/hmg/ddq006

Y. V. Sergeev, S. Vitale, P. A. Sieving, A. Vincent, A. G. Robson, A. T. Moore, A. R. Webster and G. E. Holder: Molecular modeling indicates distinct classes of missense variants with mild and severe XLRS phenotypes. Hum Mol Genet, 22(23), 4756-67 (2013) doi:10.1093/hmg/ddt329

Protein Biochemistry & Molecular Modeling Group key staff

Key staff table
Name Title Email Phone
Monika Dolinska, Ph.D. Biologist dolinskam@nei.nih.gov 301-451-7493
Milan Patel Postbac Fellow milan.patel@nih.gov
Yuri Sergeev, Ph.D. Head sergeevy@nei.nih.gov 301-594-7053
Paul Varghese Postbac Fellow paul.varghese@nih.gov
Samuel Wachamo Postbac Fellow samuel.wachamo@nih.gov
Last updated: December 10, 2020