Faculty

Kalina Hristova

Professor

Secondary Appointment: Biomedical Engineering

Research Interests

Biomaterials and the Structure and Physics of Biomembranes

Education
  • Ph.D. 1994, Duke University
  • M.S. 1988, University of Sofia
  • B.S. 1987, University of Sofia
Experience
  • 2011 - Present:  Professor, Materials Science and Engineering, Johns Hopkins University, Baltimore, MD
  • 2007 - 2011:  Associate Professor, Materials Science and Engineering, Johns Hopkins University, Baltimore, MD
  • 2001 - 2007:  Assistant Professor, Materials Science and Engineering, Johns Hopkins University, Baltimore, MD
  • 1994 - 2001:  Post-doctoral Associate/Research Scientist, Physiology and Biophysics, University of California at Irvine, Irvine, CA
  • 1991 - 1994:  Research Assistant, Mechanical Engineering and Materials Science, Duke University, Durham, NC
  • 1988 - 1991:  Research Fellow, Institute of Solid State Physics, Bulgarian Academy of Sciences, Sofia, Bulgaria
Research Areas
  • Structure, assembly, and function of biological membranes, including:
  • Cell signaling
  • Membrane cell biology
  • Structure of membrane proteins
  • Peptide–bilayer interactions
  • Structure of membranes and lipid bilayers
  • Membrane permeabilization
  • Interfacial films
  • Antimicrobial peptides
  • Surface engineering
  • Biomimetics
  • Biosurface interactions
Awards
  • 2016:  Elected Fellow: American Physical Society
  • 2016:  Elected Treasurer: The Biophysical Society
  • 2014:  Elected to Council, The Biophysical Society
  • 2011:  Chair, 2012 FASEB Research Conference (Molecular Biophysics of Cellular Membranes)
  • 2011:  Chair, 2012 Membrane Structure and Assembly
  • 2011:  Marlin U. Zimmerman Faculty Scholar, Whiting School of Engineering
  • 2007:  The Margaret Oakley Dayhoff Award, Biophysical Society
  • 2000:  Career Development Award, UC-Irvine
  • 1988:  Gold Badge of Scientific Merit, University of Sofia
Journal Articles
  • Wiedman, G., Kim, S. Y., Zapata-Mercado, E., Wimley, W. C., Hristova, K. (2017).  pH-Triggered, Macromolecule-Sized Poration of Lipid Bilayers by Synthetically Evolved Peptides.  Journal of the American Chemical Society.  139(2).  937-945.
  • Singh, D. R., Ahmed, F., Paul, M. D., Gedam, M., Pasquale, E. B., Hristova, K. (2017).  The {SAM} domain inhibits EphA2 interactions in the plasma membrane .  Biochimica et Biophysica Acta (BBA) - Molecular Cell Research .  1864(1).  31 - 38.
  • Hristova, K., Del Piccolo, N., Sarabipour, S. (2017).  A New Method to Study Heterodimerization of Membrane Proteins and its Application to Fibroblast Growth Factor Receptors.  Journal of Biological Chemistry.
  • Singh, D. R., Pasquale, E. B., Hristova, K. (2016).  A small peptide promotes EphA2 kinase-dependent signaling by stabilizing EphA2 dimers .  Biochimica et Biophysica Acta (BBA) - General Subjects .  1860(9).  1922 - 1928.
  • Sarabipour, S., Hristova, K. (2016).  Effect of the achondroplasia mutation on {FGFR3} dimerization and {FGFR3} structural response to fgf1 and fgf2: A quantitative {FRET} study in osmotically derived plasma membrane vesicles .  Biochimica et Biophysica Acta (BBA) - Biomembranes .  1858(7, Part A).  1436 - 1442.
  • King, C., Stoneman, M., Raicu, V., Hristova, K. (2016).  Fully quantified spectral imaging reveals in vivo membrane protein interactions.  Integr. Biol..  8(2).  216-229.
  • Sarabipour, S., Hristova, K. (2016).  Pathogenic Cysteine Removal Mutations in {FGFR} Extracellular Domains Stabilize Receptor Dimers and Perturb the {TM} Dimer Structure .  Journal of Molecular Biology .  428(20).  3903 - 3910.
  • Komin, A., Russell, L., Hristova, K., Searson, P. (2016).  Peptide-based strategies for enhanced cell uptake, transcellular transport, and circulation: Mechanisms and challenges .  Advanced Drug Delivery Reviews .   - .
  • Sarabipour, S., Ballmer-Hofer, K., Hristova, K. (2016).  VEGFR-2 conformational switch in response to ligand binding.  eLife.  5.  e13876.
  • Sarabipour, S., Hristova, K. (2016).  Mechanism of FGF receptor dimerization and activation.  Nature Communications.  7.
  • Sarabipour, S., Chan, R. B., Zhou, B., Di Paolo, G., Hristova, K. (2015).  Analytical characterization of plasma membrane-derived vesicles produced via osmotic and chemical vesiculation .  Biochimica et Biophysica Acta (BBA) - Biomembranes .  1848(7).  1591 - 1598.
  • Sarabipour, S., Del Piccolo, N., Hristova, K. (2015).  Characterization of Membrane Protein Interactions in Plasma Membrane Derived Vesicles with Quantitative Imaging Forster Resonance Energy Transfer.  Accounts of Chemical Research.  48(8).  2262-2269.
  • Del Piccolo, N., Placone, J., Hristova, K. (2015).  Effect of Thanatophoric Dysplasia Type I Mutations on FGFR3 Dimerization.  Biophysical Journal.  108(2).  272-278.
  • Singh, D. R., Ahmed, F., King, C., Gupta, N., Salotto, M., Pasquale, E. B., Hristova, K. (2015).  EphA2 unliganded dimers suppress EphA2 pro-tumorigenic signaling.  Journal of Biological Chemistry.
  • Hristova, K., Hinderliter, A. (2015).  Of Rafts and Lipid Chain Lengths .  Biophysical Journal .  108(9).  2096 - .
  • He, L., Hristova, K. (2015).  Quantification of the Effects of Mutations on Receptor Tyrosine Kinase (RTK) Activation in Mammalian Cells.  Receptor Tyrosine Kinases: Methods and Protocols.  1233.  81-87.
  • Wiedman, G., Wimley, W. C., Hristova, K. (2015).  Testing the limits of rational design by engineering pH sensitivity into membrane-active peptides.  Biochimica et Biophysica Acta (BBA) - Biomembranes.  1848(4).  951-957.
  • Singh, D., Cao, Q., King, C., Salotto, M., Ahmed, F., Zhou, X., Pasquale, E., Hristova, K. (2015).  Unliganded EphA3 dimerization promoted by the SAM domain.  Biochemical Journal.  471(1).  101–109.
  • Sarabipour, S., Hristova, K. (2015).  {FGFR3} Unliganded Dimer Stabilization by the Juxtamembrane Domain .  Journal of Molecular Biology .  427(8).  1705 - 1714.
  • Wiedman, G., Fuselier, T., He, J., Searson, P., Hristova, K., Wimley, W. C. (2014).  A Novel Functional Class of Pore-Forming Peptides.  Biophysical Journal.  106(2).  85A-86A.
  • Singh, D. R., King, C., Placone, J., Cao, Q., Ghosh, P., Hristova, K. (2014).  Dimerization of FGFR3 in Living Cells.  Biophysical Journal.  106(2).  480A-480A.
  • Sarabipour, S., Hristova, K. (2014).  FGF1 and FGF2 Induced FGFR3 Dimerization in Plasma Membrane Derived Vesicles.  Biophysical Journal.  106(2).  103A-103A.
  • Wiedman, G., Fuselier, T., He, J., Searson, P., Hristova, K., Wimley, W. C. (2014).  Highly Efficient Macromolecule-Sized Poration of Lipid Bilayers by a Synthetically Evolved Peptide.  Journal of the American Chemical Society.  136(12).  4724-4731.
  • Kavran, J. M., McCabe, J. M., Byrne, P. O., Connacher, M. K., Wang, Z., Ramek, A., Sarabipour, S., Shan, Y., Shaw, D. E., Hristova, K., Cole, P. A., Leahy, D. J. (2014).  How IGF-1 Activates its Receptor.  Elife.  3.
  • Kavran, J. M., McCabe, J. M., Byrne, P. O., Connacher, M. K., Wang, Z., Ramek, A., Sarabipour, S., Shan, Y., Shaw, D. E., Hristova, K., Cole, P. A., Leahy, D. J. (2014).  How IGF-1 activates its receptor.  eLife.  3.
  • Wimley, W. C., Hristova, K. (2014).  Interfacially active peptides and proteins Preface.  Biochimica Et Biophysica Acta-Biomembranes.  1838(9).  2139-2139.
  • Placone, J., He, L., Del Piccolo, N., Hristova, K. (2014).  Strong dimerization of wild-type ErbB2/Neu transmembrane domain and the oncogenic Val664Glu mutant in mammalian plasma membranes.  Biochimica Et Biophysica Acta-Biomembranes.  1838(9).  2326-2330.
  • King, C. R., Sarabipour, S., Byrne, P., Leahy, D., Hristova, K. (2014).  The FRET Signatures of Non-Interacting Proteins in Cellular Membranes.  Biophysical Journal.  106(2).  719A-719A.
  • King, C., Sarabipour, S., Byrne, P., Leahy, D. J., Hristova, K. (2014).  The FRET Signatures of Noninteracting Proteins in Membranes: Simulations and Experiments.  Biophysical Journal.  106(6).  1309-1317.
  • Sarabipour, S., King, C., Hristova, K. (2014).  Uninduced high-yield bacterial expression of fluorescent proteins.  Analytical Biochemistry.  449.  155-157.
  • Cruz, J., Mihailescu, M., Wiedman, G., Herman, K., Searson, P., Wimley, W. C., Hristova, K. (2013).  A Membrane-Translocating Peptide Penetrates into Bilayers without Significant Bilayer Perturbations.  Biophysical Journal.  104(11).  2419-2428.
  • He, J., Kauffman, W. B., Fuselier, T., Naveen, S. K., Voss, T. G., Hristova, K., Wimley, W. C. (2013).  Direct Cytosolic Delivery of Polar Cargo to Cells by Spontaneous Membrane-translocating Peptides.  Journal of Biological Chemistry.  288(41).  29974-29986.
  • Wiedman, G., Herman, K., Searson, P., Wimley, W. C., Hristova, K. (2013).  Electrical Response of Bilayers to the Bee Venom Toxin Melittin.  Biophysical Journal.  104(2).  65A-65A.
  • Wiedman, G., Herman, K., Searson, P., Wimley, W., Hristova, K. (2013).  Electrical response of lipid bilayers to the bee venom toxin melittin using electrochemical impedance spectroscopy.  Abstracts of Papers of the American Chemical Society.  245.
  • He, J., Fuselier, T., Hristova, K., Wimley, W. C. (2013).  Exploring the Sequence Determinants of Spontaneous Membrane-Translocating Peptides.  Biophysical Journal.  104(2).  250A-250A.
  • Sarabipour, S., Hristova, K. (2013).  FGFR3 Transmembrane Domain Interactions Persist in the Presence of Its Extracellular Domain.  Biophysical Journal.  105(1).  165-171.
  • Sarabipour, S., Hristova, K. (2013).  Glycophorin A transmembrane domain dimerization in plasma membrane vesicles derived from CHO, HEK 293T, and A431 cells.  Biochimica Et Biophysica Acta-Biomembranes.  1828(8).  1829-1833.
  • Hristova, K., Sarabipour, S. (2013).  GpA dimerization in plasma membrane vesicles derived from CHO, HEK 293T, and A431 cells.  Abstracts of Papers of the American Chemical Society.  245.
  • Sarabipour, S., Hristova, K. (2013).  GpA Dimerization in Plasma Membranes of CHO, HEK293T and A431 Cells.  Biophysical Journal.  104(2).  223A-223A.
  • Chen, F., Sarabipour, S., Hristova, K. (2013).  Multiple Consequences of a Single Amino Acid Pathogenic RTK Mutation: The A391E Mutation in FGFR3.  Plos One.  8(2).
  • Hristova, K. (2013).  Production of plasma membrane vesicles with chloride salts and their utility as a cell membrane mimetic for biophysical characterization of membrane protein interactions.  Abstracts of Papers of the American Chemical Society.  245.
  • He, J., Fuselier, T., Hristova, K., Wimley, W. C. (2013).  Sequence determinants of spontaneous membrane-translocating peptides.  Abstracts of Papers of the American Chemical Society.  245.
  • Bocharov, E. V., Lesovoy, D. M., Goncharuk, S. A., Goncharuk, M. V., Hristova, K., Arseniev, A. S. (2013).  Structure of FGFR3 Transmembrane Domain Dimer: Implications for Signaling and Human Pathologies.  Structure.  21(11).  2087-2093.
  • Wiedman, G., Herman, K., Searson, P., Wimley, W. C., Hristova, K. (2013).  The electrical response of bilayers to the bee venom toxin melittin: Evidence for transient bilayer permeabilization.  Biochimica Et Biophysica Acta-Biomembranes.  1828(5).  1357-1364.
  • He, J., Hristova, K., Wimley, W. C. (2012).  A Highly Charged Voltage-Sensor Helix Spontaneously Translocates across Membranes.  Angewandte Chemie-International Edition.  51(29).  7150-7153.
  • He, L., Hristova, K. (2012).  Consequences of replacing EGFR juxtamembrane domain with an unstructured sequence.  Scientific Reports.  2.
  • Placone, J., Hristova, K. (2012).  Direct Assessment of the Effect of the Gly380Arg Achondroplasia Mutation on FGFR3 Dimerization Using Quantitative Imaging FRET.  Plos One.  7(10).
  • Wiedman, G., Wimley, W., Searson, P., Hristova, K. (2012).  Effect of Melittin and Gain-of-Function Melittin Analogs, Discovered by High-Throughput Screening, on Bilayer Properties: An Electrical Impedance Spectroscopy Study.  Biophysical Journal.  102(3).  91A-91A.
  • He, L., Serrano, C., Niphadkar, N., Shobnam, N., Hristova, K. (2012).  Effect of the G375C and G346E Achondroplasia Mutations on FGFR3 Activation.  Plos One.  7(4).
  • Ohsfeldt, E., Huang, S., Baycin-Hizal, D., Kristoffersen, L., Le, T. T., Li, E., Hristova, K., Betenbaugh, M. (2012).  Increased expression of the integral membrane proteins EGFR and FGFR3 in anti-apoptotic Chinese hamster ovary cell lines.  Biotechnology and Applied Biochemistry.  59(3).  155-162.
  • Lin, J., Motylinski, J., Krauson, A. J., Wimley, W. C., Searson, P., Hristova, K. (2012).  Interactions of Membrane Active Peptides with Planar Supported Bilayers: An Impedance Spectroscopy Study.  Langmuir.  28(14).  6088-6096.
  • Stahl, P. J., Cruz, J. C., Li, Y., Yu, S. M., Hristova, K. (2012).  On-the-resin N-terminal modification of long synthetic peptides.  Analytical Biochemistry.  424(2).  137-139.
  • He, L., Hristova, K. (2012).  Physical-chemical principles underlying RTK activation, and their implications for human disease.  Biochimica Et Biophysica Acta-Biomembranes.  1818(4).  995-1005.
  • Hristova, K. (2012).  Platforms for Characterization of Membrane Protein Interactions.  Biophysical Journal.  102(3).  439A-439A.
  • Del Piccolo, N., Placone, J., He, L., Agudelo, S. C., Hristova, K. (2012).  Production of Plasma Membrane Vesicles with Chloride Salts and Their Utility as a Cell Membrane Mimetic for Biophysical Characterization of Membrane Protein Interactions.  Analytical Chemistry.  84(20).  8650-8655.
  • Wimley, W. C., Hristova, K. (2012).  The Isolated S4 Voltage Sensor Helix Translocates Spontaneously Across Membranes.  Biophysical Journal.  102(3).  615A-615A.
  • Li, E., Wimley, W. C., Hristova, K. (2012).  Transmembrane helix dimerization: Beyond the search for sequence motifs.  Biochimica Et Biophysica Acta-Biomembranes.  1818(2).  183-193.
  • Hristova, K., Wimley, W. C. (2011).  A Look at Arginine in Membranes.  Journal of Membrane Biology.  239(1-2).  49-56.
  • Jesus Sanchez-Martin, M., Hristova, K., Pujol, M., Gomara, M. J., Haro, I., Asuncion Alsina, M., Antonia Busquets, M. (2011).  Analysis of HIV-1 fusion peptide inhibition by synthetic peptides from E1 protein of GB virus C.  Journal of Colloid and Interface Science.  360(1).  124-131.
  • Wimley, W. C., Hristova, K. (2011).  Antimicrobial Peptides: Successes, Challenges and Unanswered Questions.  Journal of Membrane Biology.  239(1-2).  27-34.
  • Schick, S., Hristova, K. (2011).  Assembly of the M2 tetramer is strongly modulated by lipid chain length.  Abstracts of Papers of the American Chemical Society.  241.
  • Chen, L., Hristova, K. (2011).  Characterization of Lipid Asymmetry in Plasma Membrane-Derived Vesicles.  Biophysical Journal.  100(3).  338-338.
  • Sarabipour, S., Li, E., Hristova, K. (2011).  Effect of FGFR3 Juxtamembrane Domain on FGFR3 Dimerization.  Biophysical Journal.  100(3).  546-546.
  • He, L., Shobnam, N., Wimley, W. C., Hristova, K. (2011).  FGFR3 Heterodimerization in Achondroplasia, the Most Common Form of Human Dwarfism.  Journal of Biological Chemistry.  286(15).  13272-13281.
  • He, L., Hoffmann, A. R., Serrano, C., Hristova, K., Wimley, W. C. (2011).  High-Throughput Selection of Transmembrane Sequences That Enhance Receptor Tyrosine Kinase Activation.  Journal of Molecular Biology.  412(1).  43-54.
  • Lin, J., Krauson, A. J., Wimley, W. C., Searson, P., Hristova, K. (2011).  Interactions of Membrane Active Peptides with Planar Supported Bilayers: an Impedance Spectroscopy Study.  Biophysical Journal.  100(3).  351-351.
  • Marks, J. R., Placone, J., Hristova, K., Wimley, W. C. (2011).  Peptides with multiple arginine residues can spontaneously translocate across lipid bilayer membranes.  Abstracts of Papers of the American Chemical Society.  241.
  • Marks, J. R., Hristova, K., Wimley, W. C. (2011).  Peptides with Multiple Arginines can Spontaneously Translocate across Lipid Vesicle Membranes and across Living Cell Membranes.  Biophysical Journal.  100(3).  494-494.
  • Placone, J., Hristova, K. (2011).  Probing Skeletal Dysplasias Caused by Mutations of FGFR3 Using Qi-FRET.  Biophysical Journal.  100(3).  547-547.
  • He, L., Agudelo, S. C., Hristova, K. (2011).  Role of EGFR Juxtamembrane Domain in EGFR Activation.  Biophysical Journal.  100(3).  418-418.
  • He, L., Shobnam, N., Hristova, K. (2011).  Specific inhibition of a pathogenic receptor tyrosine kinase by its transmembrane domain.  Biochimica Et Biophysica Acta-Biomembranes.  1808(1).  253-259.
  • Marks, J. R., Placone, J., Hristova, K., Wimley, W. C. (2011).  Spontaneous Membrane-Translocating Peptides by Orthogonal High-Throughput Screening.  Journal of the American Chemical Society.  133(23).  8995-9004.
  • Cruz, J. C., Mihailescu, M., Wimley, W., Hristova, K. (2011).  Studies of Membrane-Active Peptides Using Neutron Diffraction.  Biophysical Journal.  100(3).  334-334.
  • Chen, F., Degin, C., Laederich, M., Horton, W., Hristova, K. (2011).  The A391E Mutation Enhances FGFR3 Activation in the Absence of Ligand.  Biophysical Journal.  100(3).  419-419.
  • Chen, F., Degnin, C., Laederich, M., Horton, W. A., Hristova, K. (2011).  The A391E mutation enhances FGFR3 activation in the absence of ligand.  Biochimica Et Biophysica Acta-Biomembranes.  1808(8).  2045-2050.
  • Serrano, C. M., He, L., Hoffman, A., Wimley, W. C., Hristova, K. (2011).  The Homodimerization Propensities of Transmembrane Helices Selected from a Combinatorial Library Characterized using In Vivo Phosphorylation and Dimerization Assays.  Biophysical Journal.  100(3).  419-419.
  • Chen, F., Hristova, K. (2011).  The Physical Basis of FGFR3 Response to fgf1 and fgf2.  Biochemistry.  50(40).  8576-8582.
  • Schick, S., Chen, L., Li, E., Lin, J., Koeper, I., Hristova, K. (2010).  Assembly of the M2 Tetramer Is Strongly Modulated by Lipid Chain Length.  Biophysical Journal.  99(6).  1810-1817.
  • Lin, J., Szymanski, J., Searson, P., Hristova, K. (2010).  Design of a Biologically Relevant Supported Bilayer Platform for the Study of Membrane Active Peptides.  Biophysical Journal.  98(3).  285A-285A.
  • Lin, J., Szymanski, J., Searson, P., Hristova, K. (2010).  Effect of a Polymer Cushion on the Electrical Properties and Stability of Surface-Supported Lipid Bilayers.  Langmuir.  26(5).  3544-3548.
  • Lin, J., Szymanski, J., Searson, P., Hristova, K. (2010).  Electrically addressable, biologically relevant surface supported bilayers.  Abstracts of Papers of the American Chemical Society.  240.
  • Lin, J., Szymanski, J., Searson, P., Hristova, K. (2010).  Electrically Addressable, Biologically Relevant Surface-Supported Bilayers.  Langmuir.  26(14).  12054-12059.
  • Chen, L., Novicky, L. J., Merzlyakov, M., Hristova, K. (2010).  Energetics of Glycophorin A Dimerization in Mammalian Plasma Membranes.  Biophysical Journal.  98(3).  224A-224A.
  • Chen, L., Novicky, L., Merzlyakov, M., Hristov, T., Hristova, K. (2010).  Measuring the Energetics of Membrane Protein Dimerization in Mammalian Membranes.  Journal of the American Chemical Society.  132(10).  3628-3635.
  • Marks, J. R., Krauson, A. J., Hristova, K., Wimley, W. C. (2010).  Membrane-Active Peptides: Stable Pore-Forming or Cell-Penetrating Peptides Selected With Orthogonal High-Throughput Screening.  Biophysical Journal.  98(3).  85A-85A.
  • He, L., Horton, W., Hristova, K. (2010).  Physical Basis behind Achondroplasia, the Most Common Form of Human Dwarfism.  Journal of Biological Chemistry.  285(39).  30103-30114.
  • Sarabipour, S., Hristova, K. (2010).  Quantitative Measurements of Receptor Interactions in Mammalian Cells: Implications for Human Pathologies.  Biophysical Journal.  98(3).  245A-246A.
  • Li, E., Hristova, K. (2010).  Receptor tyrosine kinase transmembrane domains Function, dimer structure and dimerization energetics.  Cell Adhesion & Migration.  4(2).  249-254.
  • Chen, L., Placone, J., Novicky, L., Hristova, K. (2010).  The Extracellular Domain of Fibroblast Growth Factor Receptor 3 Inhibits Ligand-Independent Dimerization.  Science Signaling.  3(150).
  • He, L., Hristova, K. (2010).  The Physical Basis Behind Achondroplasia, the Most Common Form of Human Dwarfism.  Biophysical Journal.  98(3).  246A-246A.
  • Li, E., Placone, J., Hristova, K. (2009).  EGFR ligand-mediated activation: insights from a quantitative study in mammalian membranes.  Faseb Journal.  23.
  • Chen, L., Merzlyakov, M., Cohen, T., Shai, Y., Hristova, K. (2009).  Energetics of ErbB1 Transmembrane Domain Dimerization in Lipid Bilayers.  Biophysical Journal.  96(11).  4622-4630.
  • Soong, R., Merzlyakov, M., Hristova, K. (2009).  Hill Coefficient Analysis of Transmembrane Helix Dimerization.  Journal of Membrane Biology.  230(1).  49-55.
  • O’Connor, S., Li, E., Majors, B. S., He, L., Placone, J., Baycin, D., Betenbaugh, M., Hristova, K. (2009).  Increased expression of the integral membrane protein ErbB2 in Chinese hamster ovary cells expressing the anti-apoptotic gene Bcl-x(L).  Protein Expression and Purification.  67(1).  41-47.
  • Snider, C., Jayasinghe, S., Hristova, K., White, S. H. (2009).  MPEx: A tool for exploring membrane proteins.  Protein Science.  18(12).  2624-2628.
  • Hristova, K. (2009).  New tools for studies of membrane protein dimerization in mammalian membranes.  Abstracts of Papers of the American Chemical Society.  237.
  • Walkenhorst, W. F., Merzlyakov, M., Hristova, K., Wimley, W. C. (2009).  Polar residues in transmembrane helices can decrease electrophoretic mobility in polyacrylamide gels without causing helix dimerization.  Biochimica Et Biophysica Acta-Biomembranes.  1788(6).  1321-1331.
  • Li, E., Merzlyakov, M., Lin, J., Searson, P., Hristova, K. (2009).  Utility of surface-supported bilayers in studies of transmembrane helix dimerization.  Journal of Structural Biology.  168(1).  53-60.
  • Han, X., Hristova, K. (2009).  Viewing the Bilayer Hydrocarbon Core Using Neutron Diffraction.  Journal of Membrane Biology.  227(3).  123-131.
  • Posokhov, Y. O., Merzlyakov, M., Hristova, K., Ladokhin, A. S. (2008).  A simple "proximity" correction for Forster resonance energy transfer efficiency determination in membranes using lifetime measurements.  Analytical Biochemistry.  380(1).  134-136.
  • Chang, W. K., Wimley, W. C., Searson, P., Hristova, K., Merzlyakov, M. (2008).  Characterization of antimicrobial peptide activity by electrochemical impedance spectroscopy.  Biochimica Et Biophysica Acta-Biomembranes.  1778(10).  2430-2436.
  • Hristova, K. (2008).  COLL 52-Structural characterization of proteins in multilayers.  Abstracts of Papers of the American Chemical Society.  236.
  • Lin, J., Merzlyakov, M., Hristova, K., Searson, P. (2008).  Impedance spectroscopy of bilayer membranes on single crystal silicon.  Biointerphases.  3(2).  FA33-FA40.
  • He, L., Hristova, K. (2008).  Pathogenic Activation of Receptor Tyrosine Kinases in Mammalian Membranes.  Journal of Molecular Biology.  384(5).  1130-1142.
  • Han, X., Hristova, K., Wimley, W. C. (2008).  Protein folding in membranes: Insights from neutron diffraction studies of a membrane beta-sheet oligomer.  Biophysical Journal.  94(2).  492-505.
  • Li, E., Placone, J., Merzlyakov, M., Hristova, K. (2008).  Quantitative measurements of protein interactions in a crowded cellular environment.  Analytical Chemistry.  80(15).  5976-5985.
  • Merzlyakov, M., Li, E., Hristova, K. (2008).  Surface supported bilayer platform for studies of lateral association of proteins in membranes (Mini Review).  Biointerphases.  3(2).  FA80-FA84.
  • Han, X., Hristova, K. (2007).  Direct measurements of bilayer hydrocarbon core thickness in the presence of membrane proteins.  Biophysical Journal.  558A-558A.
  • You, M., Spangler, J., Li, E., Han, X., Ghosh, P., Hristova, K. (2007).  Effect of pathogenic cysteine mutations on FGFR3 transmembrane domain dimerization in detergents and lipid bilayers.  Biochemistry.  46(39).  11039-11046.
  • Nikolov, V., Lin, J., Merzlyakov, M., Hristova, K., Searson, P. (2007).  Electrical measurements of bilayer membranes formed by Langmuir-Blodgett deposition on single-crystal silicon.  Langmuir.  23(26).  13040-13045.
  • Sahalov, H., O’Brien, B., Stebe, K. J., Hristova, K., Searson, P. (2007).  Influence of applied potential on the impedance of alkanethiol SAMs.  Langmuir.  23(19).  9681-9685.
  • Li, E., Chen, F., Merzlyakov, M., Placone, J., Hristova, K. (2007).  Measurements of FGFR3 dimerization in the plasma membrane using Forster resonance energy transfer.  Biophysical Journal.  558A-558A.
  • Chen, L., Krishnamoothy, G., Cui, J., Sept, D., Hristova, K. (2007).  Measuring the dimerization of FGFR3 transmembrane domain in cell membrane.  Biophysical Journal.  558A-558A.
  • O’Connor, S. K., He, L., Li, E., Betenbaugh, M., Hristova, K. (2007).  Membrane protein expression in anti-apoptotic mammalian cells.  Biophysical Journal.  392A-392A.
  • Merzlyakov, M., Chen, L., Li, E., Hristova, K. (2007).  Quantitative FRET imaging of membrane protein interactions in cells.  Biophysical Journal.  558A-558A.
  • He, L., Li, E., O’Connor, S., Placone, J., Hristova, K. (2007).  Studies of molecular mechanism of FGFR3 associated pathogenesis in cells.  Biophysical Journal.  558A-558A.
  • Merzlyakov, M., Chen, L., Hristova, K. (2007).  Studies of receptor tyrosine kinase transmembrane domain interactions: The EmEx-FRET method.  Journal of Membrane Biology.  215(2-3).  93-103.
  • Searson, P., Nikolov, V., Merzlyakov, M., Tomich, J., Hristova, K. (2007).  Supported bilayers with functional ion channels.  Biophysical Journal.  251A-251A.
  • Soong, R., Herrera, A., Majumdar, A., Tomich, J., Hristova, K. (2007).  Towards high-resolution structure of FGFR3 transmembrane domains through H-1-H-1 NOESY and TOCSY NMR studies.  Biophysical Journal.  558A-558A.
  • Nikolov, V., Radisic, A., Hristova, K., Searson, P. (2006).  Bias-dependent admittance in hybrid bilayer membranes.  Langmuir.  22(17).  7156-7158.
  • Li, E., Hristova, K., Merzlyakov, M. (2006).  COLL 583-Energetics of receptor tyrosine kinase dimerization.  Abstracts of Papers of the American Chemical Society.  232.
  • Merzlyakov, M., Li, E., Hristova, K. (2006).  Directed assembly of surface-supported bilayers with transmembrane helices.  Langmuir.  22(3).  1247-1253.
  • Li, E., You, M., Hristova, K. (2006).  FGFR3 dimer stabilization due to a single amino acid pathogenic mutation.  Journal of Molecular Biology.  356(3).  600-612.
  • Hristova, K., Li, E., Merzlyakov, M. (2006).  FGFR3 transmembrane domain dimerization in lipid bilayers: probing the energetics behind an autosomal dominant growth disorder.  Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire.  84(6).  1072-1072.
  • Han, X., Mihailescu, M., Hristova, K. (2006).  Neutron diffraction studies of fluid bilayers with transmembrane proteins: Structural consequences of the achondroplasia mutation.  Biophysical Journal.  91(10).  3736-3747.
  • Hristova, K. (2006).  PHYS 60-Probing membrane protein interactions in surface supported bilayers.  Abstracts of Papers of the American Chemical Society.  232.
  • Li, E., Hristova, K. (2006).  Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies.  Biochemistry.  45(20).  6241-6251.
  • Merzlyakov, M., Li, E., Casas, R., Hristova, K. (2006).  Spectral Forster resonance energy transfer detection of protein interactions in surface-supported bilayers.  Langmuir.  22(16).  6986-6992.
  • Merzlyakov, M., Li, E., Gitsov, I., Hristova, K. (2006).  Surface-supported bilayers with transmembrane proteins: Role of the polymer cushion revisited.  Langmuir.  22(24).  10145-10151.
  • You, M., Li, E., Hristova, K. (2006).  The achondroplasia mutation does not alter the dimerization energetics of the fibroblast growth factor receptor 3 transmembrane domain.  Biochemistry.  45(17).  5551-5556.
  • Merzlyakov, M., You, M., Li, E., Hristova, K. (2006).  Transmembrane helix heterodimerization in lipid bilayers: Probing the energetics behind autosomal dominant growth disorders.  Journal of Molecular Biology.  358(1).  1-7.
  • Hristova, K., White, S. H. (2005).  An experiment-based algorithm for predicting the partitioning of unfolded peptides into phosphatidylcholine bilayer interfaces.  Biochemistry.  44(37).  12614-12619.
  • You, M., Li, E., Wimley, W. C., Hristova, K. (2005).  Forster resonance energy transfer in liposomes: Measurements of transmembrane helix dimerization in the native bilayer environment.  Analytical Biochemistry.  340(1).  154-164.
  • Hristova, K., Merzlyakov, M., Li, E. (2005).  Probing membrane protein dimerization in supported lipid bilayers.  Abstracts of Papers of the American Chemical Society.  229.  U632-U632.
  • Li, E., You, M., Hristova, K. (2005).  Sodium dodecyl sulfate - Polyacrylamide gel electrophoresis and Forster resonance energy transfer suggest weak interactions between fibroblast growth factor receptor 3 (FGFR3) transmembrane domains in the absence of extracellular domains and ligands.  Biochemistry.  44(1).  352-360.
  • Iwamoto, T., You, M., Li, E., Spangler, J., Tomich, J. M., Hristova, K. (2005).  Synthesis and initial characterization of FGFR3 transmembrane domain: consequences of sequence modifications.  Biochimica Et Biophysica Acta-Biomembranes.  1668(2).  240-247.
  • Li, E., Hristova, K. (2004).  Imaging forster resonance energy transfer measurements of transmembrane helix interactions in lipid bilayers on a solid support.  Langmuir.  20(21).  9053-9060.
  • Li, E., You, M., Hristova, K. (2004).  Measurements of transmembrane helix dimerization in lipid bilayer environments.  Biophysical Journal.  86(1).  375A-375A.
  • Li, E. W., Gallagher, G., Werbin, J., You, M., Hristova, K. (2003).  Mimicking transmembrane signaling events.  Biophysical Journal.  84(2).  294A-294A.
  • White, S. H., Hristova, K., Tobias, D. J. (2002).  Determination of dynamic 3D structures of membranes from 1D data: Molecular dynamics/absolute scale refinement (MoDAS).  Abstracts of Papers American Chemical Society.  224(1-2).  35-PHYS 35.
  • Hristova, K., White, S. H. (2001).  Effect of lipid headgroups on peptide partitioning into bilayer interfaces.  Biophysical Journal.  80(1).  544A-544A.
  • Jayasinghe, S., Hristova, K., White, S. H. (2001).  Energetics, stability, and prediction of transmembrane helices.  Journal of Molecular Biology.  312(5).  927-934.
  • White, S. H., Ladokhin, A. S., Jayasinghe, S., Hristova, K. (2001).  How membranes shape protein structure.  Journal of Biological Chemistry.  276(35).  32395-32398.
  • Jayasinghe, S., Hristova, K., White, S. H. (2001).  MPtopo: A database of membrane protein topology.  Protein Science.  10(2).  455-458.
  • Hristova, K., Dempsey, C. E., White, S. H. (2001).  Structure, location, and lipid perturbations of melittin at the membrane interface.  Biophysical Journal.  80(2).  801-811.
  • Hristova, K., White, S. H. (2000).  Complete structure of dioleoylphosphatidylcholine (DOPC) bilayers as a function of hydration.  Biophysical Journal.  78(1).  21A-21A.
  • Hristova, K., White, S. H. (2000).  Free energies of transfer of C- and N-termini of peptides into octanol and POPC bilayers: An appendix to the first experimentally determined hydrophobicity scales.  Biophysical Journal.  78(1).  14A-14A.
  • Jayasinghe, S., Hristova, K., White, S. H. (2000).  MPEx & MPtopo: Tools for membrane protein topology analysis.  Biophysical Journal.  78(1).  158A-158A.
  • Hristova, K., Wimley, W. C., Mishra, V. K., Anantharamiah, G. M., Segrest, J. P., White, S. H. (1999).  An amphipathic alpha-helix at a membrane interface: A structural study using a novel X-ray diffraction method.  Journal of Molecular Biology.  290(1).  99-117.
  • Hristova, K., White, S. H. (1999).  Disposition of melittin in fluid lipid bilayers determined by x-ray diffraction.  Biophysical Journal.  76(1).  A219-A219.
  • Hristova, K., White, S. H. (1998).  Determination of the hydrocarbon core structure of fluid dioleoylphosphocholine (DOPC) bilayers by x-ray diffraction using specific bromination of the double-bonds: Effect of hydration.  Biophysical Journal.  74(5).  2419-2433.
  • White, S. H., Wimley, W. C., Ladokhin, A., Hristova, K. (1998).  Protein folding in membranes: Pondering the nature of the bilayer milieu.  Kongelige Danske Videnskabernes Selskab Biologiske Skrifter.  49(0).  99-106.
  • Hristova, K., Selsted, M. E., White, S. H. (1997).  Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins.  Journal of Biological Chemistry.  272(39).  24224-24233.
  • Hristova, K., Selsted, M. E., White, S. H. (1996).  Interactions of monomeric rabbit neutrophil defensins with bilayers: Comparison with dimeric human defensin HNP-2.  Biochemistry.  35(36).  11888-11894.
  • Petrov, A. G., Miller, B. A., Hristova, K., Usherwood, P. N. (1993).  FLEXOELECTRIC EFFECTS IN MODEL AND NATIVE MEMBRANES CONTAINING ION CHANNELS.  European Biophysics Journal with Biophysics Letters.  22(4).  289-300.
Books
  • Lin, J., Hristova, K., Searson, P. (2013).  Electrically Addressable, Biologically Relevant Surface-Supported Bilayers.  769-820.
Book Chapters
  • Merzlyakov, M., Hristova, K. (2008).  FORSTER RESONANCE ENERGY TRANSFER MEASUREMENTS OF TRANSMEMBRANE HELIX DIMERIZATION ENERGETICS.  Fluorescence Spectroscopy.  450.  107-127.
  • White, S. H., Wimley, W. C., Ladokhin, A. S., Hristova, K. (1998).  Protein folding in membranes: Determining energetics of peptide-bilayer interactions.  Methods in Enzymology; Energetics of biological macromolecules, Part B.  295.  62-87.
  • Biophysics seminar series .  UT Southwestern Medical Center, Dallas, TX.  2017
  • Chemistry seminar series.  Lehigh University, Bethlehem, PA .  2016
  • Chemistry Seminar Series.  University of West Virginia, Morgantown, WV.  2016
  • Biomembrane Frontiers II Workshop: Emergent Design of Biomembranes .  UC Davis, CA .  2016
  • "Liposomes, Exosomes, and Virosomes: From Modeling Complex Membrane Processes to Medical Diagnostics and Drug Delivery", Biophysical Society Thematic Meeting .  Ascona, Switzerland.  2016
  • Molecular Cell Biology seminar.  The Norwegian Radium Hospital, Oslo, Norway.  2016
  • The Fourth International Conference on Analytical and Nanoanalytical Methods for Biomedical and Environmental Sciences.  Brasov, Romania.  2016
  • Chemistry seminar series.  University of Wisconsin, Madison, WI.  2016
  • "Biophysics 101 Lecture", Biophysical Society Annual Meeting .  Los Angeles, CA .  2016
  • "Receptor Tyrosine Kinases: Insight into dimerization, structure, and function", 2015 Workshop on Tethered Membranes.  Singapore.  2015
  • Membrane Active Peptides and Proteins.  Shanghai, China.  2015
  • Chemistry Seminar Series.  2015
  • Optical Micro-spectroscopy & Molecular Imaging.  2015
  • Biological Membranes and Membrane Proteins: Challenges for Theory and Experiments.  Telluride, CO.  2015
  • Canadian Chemical Society Annual Meeting.  Ottawa, Canada.  2015
  • Biochemistry and Molecular Biology seminar.  2014
  • Chemistry/Biochemistry Seminar Series.  2014
  • International Theoretical Course, ""Advances in Lipid-Protein Interactions: Understanding its Importance and Modulation in Cell Physiology".  Cuernavaca, Morelos, México.  2014
  • FASEB Science Research Conference, "Molecular Biophysics of Membranes".  Big Sky, MO.  2014
  • Third International Conference on Analytical and Nanoanalytical Methods for Biomedical and Environmental Sciences.  Brasov, Romania.  2014
  • Advanced Methods and Applications in Quantitative Fluorescence.  2013
  • Physics/Biology seminar series.  Philadelphia, PA.  2013
  • Chemistry/Biochemistry seminar series.  Wilmington, NC.  2013
  • Membrane Protein Folding and Functioning.  Telluride, CO.  2013
  • Biological Membranes and Membrane Proteins: Challenges for Theory and Experiment.  Snowmass Village, CO.  2013
  • Theoretical Molecular Biophysics seminar series.  Berlin, Germany.  2013
  • Institute for Bioscience and Biotechnology Research seminar series.  Rockville, MD.  2013
  • Membrane Biochemistry and Biophysics and Molecular Signaling series.  Rockville, MD.  2013
  • NSF-UWM Symposium: Open Forum for Innovation in Two-Photon Microspectroscopy.  Milwaukee, WI.  2013
  • "Imaging the EGFR bio-system; from molecules to man” conference.  London, UK.  2012
  • Physics, Chemistry, and Biology of Membrane Proteins.  Tempe, AZ.  2012
  • Biophysics and Biophysical Chemistry seminar series.  2012
  • "Systems for Membrane Protein Reconstitution", Biophysical Society Annual Meeting.  San Diego, CA.  2012
  • Australian Society of Biophysics Meeting.  Wollongong, Australia.  2011
  • School of Pharmacy Seminar Series.  2011
  • Biochemistry and Biophysics Seminar Series.  2011
  • "Membrane Protein Structure and Function", ACS 241st National Meeting.  Anaheim, CA.  2011
  • "Peptides in Biotechnology and Biomedicine", Joint 66th Southwest and 62nd Southeastern Regional Meeting of the ACS.  New Orleans, LA.  2010
  • Materials Chemistry Seminar Series.  2010
  • Physics Seminar Series.  2010
  • Biochemistry Seminar Series.  2010
  • Membrane Protein Interest Group seminar series.  Bethesda, MD.  2010
  • BioNanoSciences Symposium.  2010
  • Gordon Research Conference on Biointerface Science.  Les Diablerets, Switzerland.  2010
  • Medicinal Physics and Biophysics Seminar Series.  2010
  • Frontiers in Membrane and Membrane Protein Biophysics: Experiments and Theory Experiments and Theory.  Irvine, CA.  2010
  • "Receptor Tyrosine Kinases: Biology and Cancer", FASEB Research Conference.  Carefree, AZ.  2010
  • Biophysics of Membrane-Active Peptides.  Bad Honnef, Germany.  2010
  • Chemistry of Biopolymers seminar series.  2010
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