Publications

2023

  • Wirth, D., Özdemir, E. & Hristova, K. Quantification of ligand and mutation-induced bias in EGFR phosphorylation in direct response to ligand binding. Nat Commun 14, 7579 (2023).
  • McKenzie DM, Wirth D, Pogorelov TV, Hristova K. Utility of FRET in studies of membrane protein oligomerization: The concept of the effective dissociation constant. Biophys J. 2023 Oct 17;122(20):4113-4120.
  • Karl Kelly, Del Piccolo Nuala, Light Taylor, Roy Tanaya, Dudeja Pooja, Ursachi Vlad-Constantin, Fafilek Bohumil, Krejci Pavel, Hristova Kalina (2023) Ligand bias underlies differential signaling of multiple FGFs via FGFR1 eLife 12:RP88144
  • Khan A, Killick R, Wirth D, Hoogland D, Hristova K, Ulmschneider JP, King CR, Ulmschneider MB. Masking the transmembrane region of the amyloid β precursor protein as a safe means to lower amyloid β production. Alzheimers Dement (N Y). 2023 Nov 8;9(4):e12428.
  • Karl K, Rajagopal S, Hristova K. Quantitative assessment of ligand bias from bias plots: The bias coefficient “kappa”. Biochim Biophys Acta Gen Subj. 2023 Oct;1867(10):130428.
  • Hristova K, Wimley WC. Determining the statistical significance of the difference between arbitrary curves: A spreadsheet method. PLoS One. 2023 Oct 31;18(10):e0289619.
  • Karl Kelly, Del Piccolo Nuala, Light Taylor, Roy Tanaya, Dudeja Pooja, Ursachi Vlad-Constantin, Fafilek Bohumil, Krejci Pavel, Hristova Kalina (2023) Bias in FGFR1 signaling in response to FGF4, FGF8, and FGF9 eLife 12:RP88144
  • Bertalan, E., Ashok A. Jain, H., Hristova, K., Wimley, W. C., & Bondar, A. (2023). Mechanisms by which water-mediated hydrogen-bond networks govern pH-dependent reactions at membrane interfaces. Biophysical Journal, 122(3), 342a.

2022

  • Wirth D, Paul MD, Pasquale EB, Hristova K. Direct quantification of ligand-induced lipid and protein microdomains with distinctive signaling properties. ChemSystemsChem. 2022 Sep;4(5):e202200011.
  • Bartzoka F, Gonzalez-Magaldi M, Byrne PO, Callery NI, Hristova K, Leahy DJ. Activity of EGFR transmembrane region variants indicates specific transmembrane dimers are not required for EGFR activity. Biochem J. 2022 Dec 19;479(24):2465-2475.
  • Zapata-Mercado E, Biener G, McKenzie DM, Wimley WC, Pasquale EB, Raicu V, Hristova K. The efficacy of receptor tyrosine kinase EphA2 autophosphorylation increases with EphA2 oligomer size. J Biol Chem. 2022 Oct;298(10):102370.
  • Zapata-Mercado E, Azarova EV, Hristova K. Effect of osmotic stress on live cell plasma membranes, probed via Laurdan general polarization measurements. Biophys J. 2022 Jun 21;121(12):2411-2418.
  • Gomez-Soler, M., Gehring, M. P., Lechtenberg, B. C., Zapata-Mercado, E., Ruelos, A., Matsumoto, M. W., Hristova, K., & Pasquale, E. B. Ligands with different dimeric configurations potently activate the EphA2 receptor and reveal its potential for biased signaling. (2022) Iscience 25 (3), 103870
  • Karl, K., Del Piccolo, N., Krejci, P., & Hristova, K. Bias in FGFR1 signaling in response to FGF4, FGF8, and FGF9.  (2022). bioRxiv
  • Dornhaus A, Smith B, Hristova K, Buckley LB. How Can We Fully Realize the Potential of Mathematical and Biological Models to Reintegrate Biology? (2022) Integr Comp Biol. 5;61(6):2244-2254.
  • Sullivan B, Light T, Vu V, Kapustka A, Hristova K, Leckband D. Mechanical disruption of E-cadherin complexes with epidermal growth factor receptor actuates growth factor-dependent signaling. (2022 ) Proc Natl Acad Sci U S A. 25;119(4):e2100679119.

2021

  • Kim SY, Bondar AN, Wimley WC, Hristova K. pH-triggered pore-forming peptides with strong composition-dependent membrane selectivity. (2021) Biophys J.  16;120(4):618-630
  • Paul MD, Hristova K. Interactions between Ligand-Bound EGFR and VEGFR2. (2021) J Mol Biol. 25;433(13):167006
  • Wirth D, McCall A, Hristova K. Neural network strategies for plasma membrane selection in fluorescence microscopy images. (2021) Biophys J. 15;120(12):2374-2385
  • Ahmed F, Zapata-Mercado E, Rahman S, Hristova K. The Biased Ligands NGF and NT-3 Differentially Stabilize Trk-A Dimers.  (2021) Biophys J. 5;120(1):55-63
  • Paul MD, Rainwater R, Zuo Y, Gu L, Hristova K. Probing Membrane Protein Association Using Concentration-Dependent Number and Brightness. (2021) Angew Chem Int Ed Engl. 15;60(12):6503-6508
  • Vu V, Light T, Sullivan B, Greiner D, Hristova K, Leckband D. P120 catenin potentiates constitutive E-cadherin dimerization at the plasma membrane and regulates trans binding. (2021) Curr Biol. 26;31(14):3017-3027.e7
  • Light TP, Gomez-Soler M, Wang Z, Karl K, Zapata-Mercado E, Gehring MP, Lechtenberg BC, Pogorelov TV, Hristova K, Pasquale EB. A cancer mutation promotes EphA4 oligomerization and signaling by altering the conformation of the SAM domain. (2021) J Biol Chem. 297(1):100876
  • Linville RM, Komin A, Lan X, DeStefano JG, Chu C, Liu G, Walczak P, Hristova K, Searson PC. Reversible blood-brain barrier opening utilizing the membrane active peptide melittin in vitro and in vivo. (2021) Biomaterials. 275:120942
  • Dornhaus A, Smith B, Hristova K, Buckley LB. How can we fully realize the potential of mathematical and biological models to reintegrate biology? (2021) Integr Comp Biol. 23:icab142
  • Sun L , Hristova K , Wimley WC . Membrane-selective nanoscale pores in liposomes by a synthetically evolved peptide: implications for triggered release. (2021) Nanoscale. 28;13(28):12185-12197
  • Franco ML, Nadezhdin KD, Light TP, Goncharuk SA, Soler-Lopez A, Ahmed F, Mineev KS, Hristova K, Arseniev AS, Vilar M. Interaction between the transmembrane domains of neurotrophin receptors p75 and TrkA mediates their reciprocal activation. (2021) J Biol Chem. 297(2):100926
  • Karl K, Hristova K. Pondering the mechanism of receptor tyrosine kinase activation: The case for ligand-specific dimer microstate ensembles. (2021)Curr Opin Struct Biol. 13;71:193-199
  • Light TP, Brun D, Guardado-Calvo P, Pederzoli R, Haouz A, Neipel F, Rey FA, Hristova K, Backovic M. Human herpesvirus 8 molecular mimicry of ephrin ligands facilitates cell entry and triggers EphA2 signaling. (2021) PLoS Biol. 9;19(9):e3001392
  • Wirth D, Özdemir E, King C, Ahlswede L, Schneider D, Hristova K. Quantitative characterization of tetraspanin 8 homointeractions in the plasma membrane.(2021) Biochem J.5;478(19):3643-3654
  • Guha S, Ferrie RP, Ghimire J, Ventura CR, Wu E, Sun L, Kim SY, Wiedman GR, Hristova K, Wimley WC. Applications and evolution of melittin, the quintessential membrane active peptide. (2021) Biochem Pharmacol. 17;193:114769

2020

  • Singh DR, King C, Salotto M, Hristova K. Revisiting a controversy: The effect of EGF on EGFR dimer stability. (2020) Biochim Biophys Acta Biomembr.  1;1862(1):183015
  • Paul MD, Grubb HN, Hristova K. Quantifying the strength of heterointeractions among receptor tyrosine kinases from different subfamilies: Implications for cell signaling. (2020) J Biol Chem. 17;295(29):9917-9933
  • Komin A, Bogorad MI, Lin R, Cui H, Searson PC, Hristova K. A peptide for transcellular cargo delivery: Structure-function relationship and mechanism of action. (2020) J Control Release. 10;324:633-643.
  • Byrne PO, Hristova K, Leahy DJ. EGFR forms ligand-independent oligomers that are distinct from the active state. (2020) J Biol Chem. 18;295(38):13353-13362
  • Paredes SD, Kim S, Rooney MT, Greenwood AI, Hristova K, Cotten ML. Enhancing the membrane activity of Piscidin 1 through peptide metallation and the presence of oxidized lipid species: Implications for the unification of host defense mechanisms at lipid membranes. (2020) Biochim Biophys Acta Biomembr. 1;1862(7):183236.
  • Wu E, Jenschke RM, Hristova K, Wimley WC. Rational Modulation of pH-Triggered Macromolecular Poration by Peptide Acylation and Dimerization. (2020) J Phys Chem B. 8;124(40):8835-8843.
  • Ahmed F, Paul MD, Hristova K. The biophysical basis of receptor tyrosine kinase ligand functional selectivity: Trk-B case study. (2020) Biochem J. 11;477(23):4515-4526.
  • Karl K, Paul MD, Pasquale EB, Hristova K. Ligand bias in receptor tyrosine kinase signaling. J Biol Chem. 25;295(52):18494-18507

2019

  • M. D. Paul and K. Hristova. The transition model of RTK activation: a quantitative framework for understanding RTK signaling and RTK modulator activity. (2019) Cytokine and Growth Factor Reviews. 49:23-31
  • W. Wimley and K. Hristova. The Mechanism of Membrane Permeabilization by Peptides: Still an enigma. (2019) Australian Journal of Chemistry. 73(3):96-103
  • D. Singh, C. King, M. Salotto, and K. Hristova. Revisiting a controversy: The effect of EGF on EGFR dimer stability. (2020) BBA-Biomembranes. 1862(1):183015
  • S.Y. Kim, A.E. Pittman, E. Zapata-Mercado, G.M. King, W.C. Wimley, and K. Hristova. Mechanism of action of peptides that cause the pH-triggered macromolecular poration of lipid bilayers. (2019) Journal of the American Chemical Society, 141:6706-6718. J117.
  • M. Paul and K. Hristova. The RTK Interactome: Overview and perspective on RTK Hetero-interactions. (2019) Chemical Reviews, 119, pp 5881–5921.
  • M. Gomez-Soler, M. Petersen Gehring, B.C. Lechtenberg, E. Zapata-Mercado, K. Hristova, and E.B. Pasquale. Engineering nanomolar peptide ligands that differentially modulate EphA2 receptor signaling. (2019) Journal of Biological Chemistry. 294(22):8791-8805
  • C. King and K. Hristova. Direct measurements of VEGF:VEGFR2 binding affinities reveal the coupling between ligand binding and receptor dimerization. (2019) Journal of Biological Chemistry. (JBC Editor’s Pick) 

2018

  • D.R. Sing, P. Kanvinde, C. King, E. B. Pasquale, and K. Hristova. The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures. (2018) Communications Biology 1:15.
  • C. King, D. Wirth, S. Workman, and K. Hristova. Interactions between NRP1 and VEGFR2 molecules in the plasma membrane. (2018) BBA-Biomembranes. 1860:2118-2125.
  • S. Li, S. Y. Kim, A. E. Pittman, G. M. King, W. Wimley, and K. Hristova. Potent macromolecule-sized poration of lipid bilayers by the macrolittins, a synthetically evolved family of pore-forming peptides. (2018) Journal of the American Chemical Society, 140:6441-6447. J114.
  •  S.M.Walsh, S. Mathiasen,  … K. Hristova, B. Kobilka, D.L. Farrens, and D. Stamou. Single Proteoliposome High-Content Analysis Reveals Differences in the Homo-Oligomerization of GPCRs. (2018) Biophysical Journal, 115:300-312
  • F. Ahmed and K. Hristova. Dimerization of the Trk receptors in the plasma membrane: effects of their cognate ligands. (2018) Biochemical Journal, 475:3669-3685.

2017

  • D.R. Singh, F. Ahmed, M. Paul, M. Gedham, E.B. Pasquale, and K. Hristova. The SAM domain inhibits EphA2 interactions in the plasma membrane. (2017) BBA-Molecular Cell Research, Oct 21;1864:31-3
  • N. Del Piccolo, S. Sarabipour, and K. Hristova. A New Method to Study Heterodimerization of Membrane Proteins and its Application to Fibroblast Growth Factor Receptors. (2017) Journal of Biological Chemistry, 292:1288-1301
  • G. Wiedman, S.Y. Kim, E. Zapata-Mercado, W.C.Wimley, and K. Hristova. PH-Triggered, Macromolecule-Sized Poration of Lipid Bilayers by Synthetically Evolved Peptides. (2017) Journal of the American Chemical Society, 139:937-945 (highlighted in JACS Spotlight)
  • C. King, V. Raicu, and K. Hristova. Understanding the FRET Signatures of Interacting Membrane Proteins. (2017) Journal of Biological Chemistry, 292:5291-5310.
  • J. He, L.I. Melnik, A. Komin, G. Wiedman, T. Fuselier, C.F. Morris, C.G. Starr, P.C. Searson, W.R. Gallaher, K. Hristova, R.F. Garry, W.C. Wimley. Ebola Virus Delta Peptide is a Viroporin. (2017) Journal of Virology, in press. (highlighted in: JHU News Releases, JHU Hub, Aug 22, Whiting School of Engineering News, News-Medical.net, ScienceDaily.com, MedicalXpress.com, Global Biodefense, Homeland Preparedness News,  Science Codex, ADC Voice, ScienMag, MyInforms.com, CheckTheScience.com, Bright Surf News, Healthcare Purchasing News, LongRoom.com, My-News-Site.com, Press Release Point, Eurekalert, Science Newsline, Jersey Tribune, Newswise)
  • D.R. Singh, F. Ahmed, S. Sarabipour, and K. Hristova. Intracellular domain contacts contribute to Ecadherin constitutive dimerization in the plasma membrane. (2017) Journal of Molecular Biology, 429:2231-2245.
  • D. Del Piccolo and K. Hristova. Quantifying the Interaction between EGFR Dimers and Grb2 in Live Cells. (2017) Biophysical Journal, 113:1353-1364. (recommended in F1000Prime as being of special significance)
  • C. King, D. Wirth, S. Workman, and K. Hristova. Cooperative interactions between VEGFR2 extracellular Ig-like subdomains ensure VEGFR2 dimerization. (2017) BBA-General Subjects, 1861:2559-2567.

2016

  • Peptide-based strategies for enhanced cell uptake, transcellular transport, and circulation: Mechanisms and challenges. Komin A, Russell LM, Hristova K, Searson PC. Adv Drug Deliv Rev. 2016
  • A small peptide promotes EphA2 kinase-dependent signaling by stabilizing EphA2 dimers. Singh DR, Pasquale EB, Hristova K. Biochim Biophys Acta. 2016 Sep;1860(9):1922-8.
  • 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. Sarabipour S, Hristova K. Biochim Biophys Acta. 2016 Jul;1858(7 Pt A):1436-42.
  • VEGFR-2 conformational switch in response to ligand binding. Sarabipour S, Ballmer-Hofer K, Hristova K. eLife 2016;5:e13876
  • Fully quantified spectral imaging reveals in vivo membrane protein interactions. King C, Stoneman M, Raicu V, Hristova K. Integr Biol (Camb). 2016 Feb 15;8(2):216-29.
  • Mechanism of FGF receptor dimerization and activation. Sarabipour S, Hristova K. Nat Commun. 2016 Jan 4;7:10262.

2015

  • Analytical characterization of plasma membrane-derived vesicles produced via osmotic and chemical vesiculation. Sarabipour S, Chan RB, Zhou B, Di Paolo G, Hristova K. Biochim Biophys Acta. 2015 Jul;1848(7):1591-8.
  • EphA2 Receptor Unliganded Dimers Suppress EphA2 Pro-tumorigenic Signaling. Singh DR, Ahmed F, King C, Gupta N, Salotto M, Pasquale EB, Hristova K. J Biol Chem. 2015 Nov 6;290(45):27271-9.
  • Characterization of membrane protein interactions in plasma membrane derived vesicles with quantitative imaging Förster resonance energy transfer. Sarabipour S, Del Piccolo N, Hristova K. Acc Chem Res. 2015 Aug 18;48(8):2262-9.
  • Unliganded EphA3 dimerization promoted by the SAM domain. Singh DR, Cao Q, King C, Salotto M, Ahmed F, Zhou XY, Pasquale EB, Hristova K. Biochem J. 2015 Oct 1;471(1):101-9. doi: 10.1042/BJ20150433.
  • FGFR3 unliganded dimer stabilization by the juxtamembrane domain. Sarabipour S, Hristova K. J Mol Biol. 2015 Apr 24;427(8):1705-14.
  • Effect of thanatophoric dysplasia type I mutations on FGFR3 dimerization. Del Piccolo N, Placone J, Hristova K. Biophys J. 2015 Jan 20;108(2):272-8.
  • Testing the limits of rational design by engineering pH sensitivity into membrane-active peptides. Wiedman G, Wimley WC, Hristova K. Biochim Biophys Acta. 2015 Apr;1848(4):951-7.

2014

  • Wiedman G, Fuselier T, He J, Searson PC, Hristova K, Wimley WC. “Highly efficient macromolecule-sized poration of lipid bilayers by a synthetically evolved Peptide.” J Am Chem Soc. 2014 Mar 26;136(12):4724-31. doi: 10.1021/ja500462s. Epub 2014 Mar 13.
  • King C, Sarabipour S, Byrne P, Leahy DJ, Hristova K, “The FRET Signatures of Noninteracting Proteins in Membranes: Simulations and Experiments.” Biophysical Journal. 2014 March 18; 106 (6): 1309-1317. doi: 10.1016/j.bpj.2014.01.039. Epub 2014 March 18.
  • Placone J, He L, Del Piccolo N, Hristova K. “Strong dimerization of wild-type ErbB2/Neu transmembrane domain and the oncogenic Val664Glu mutant in mammalian plasma membranes.” Biochim Biophys Acta. 2014 Mar 11. pii: S0005-2736(14)00095-9. doi: 10.1016/j.bbamem.2014.03.001. [Epub ahead of print]
  • Sarabipour S, King C, Hristova K. “Uninduced high-yield bacterial expression of fluorescent proteins.” Analytical Biochemistry. 2014 Mar 15;449:155-7. doi: 10.1016/j.ab.2013.12.027. Epub 2013 Dec 28.

2013

  • Bocharov EV, Lesovoy DM, Goncharuk SA, Goncharuk MV, Hristova K, Arseniev AS, “Structure of FGFR3 transmembrane domain dimer: implications for signaling and human pathologies.” Structure. 2013 Nov 5;21(11):2087-93. doi: 10.1016/j.str.2013.08.026. Epub 2013 Oct 10.
  • He J, Kauffman WB, Fuselier T, Naveen SK, Voss TG, Hristova K, Wimley WC, “Direct cytosolic delivery of polar cargo to cells by spontaneous membrane-translocating peptides.”  J Biol Chem. 2013 Oct 11;288(41):29974-86. doi: 10.1074/jbc.M113.488312. Epub 2013 Aug 27.
  • Sarabipour S, Hristova K, “FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain.” Biophys J. 2013 Jul 2;105(1):165-71. doi: 10.1016/j.bpj.2013.05.053.
  • Cruz J, Mihailescu M, Wiedman G, Herman K, Searson PC, Wimley WC, Hristova K, “A membrane-translocating peptide penetrates into bilayers without significant bilayer perturbations.” Biophys J. 2013 Jun 4;104(11):2419-28. doi: 10.1016/j.bpj.2013.04.043.
  • Sarabipour S, Hristova K, “Glycophorin A transmembrane domain dimerization in plasma membrane vesicles derived from CHO, HEK 293T, and A431 cells”  Biochim Biophys Acta. 2013 Aug;1828(8):1829-33. doi: 10.1016/j.bbamem.2013.03.022. Epub 2013 Apr 2.
  • Chen F, Sarabipour S, Hristova K, “Multiple consequences of a single amino acid pathogenic RTK mutation: the A391E mutation in FGFR3.”  PLoS One. 2013;8(2):e56521. doi: 10.1371/journal.pone.0056521. Epub 2013 Feb 20.
  • Wiedman G, Herman K, Searson P, Wimley WC, Hristova K, “The electrical response of bilayers to the bee venom toxin melittin: evidence for transient bilayer permeabilization.” Biochim Biophys Acta. 2013 May;1828(5):1357-64. doi: 10.1016/j.bbamem.2013.01.021. Epub 2013 Feb 4.

2012

  • He L, Hristova K “Consequences of replacing EGFR juxtamembrane domain with an unstructured sequence”, Sci Rep. 2012; 2:854
  • Del Piccolo N, Placone J, He L, Agudelo SC, Hristova K “Production of plasma membrane vesicles with chloride salts and their utility as a cell membrane mimetic for biophysical characterization of membrane protein interactions.”, Anal Chem. 2012 Oct 16; 84(20), 8650-5
  • Placone J, Hristova K “Direct assessment of the effect of the Gly380Arg achondroplasia mutation on FGFR3 dimerization using quantitative imaging FRET “, PLoS One. 2012; 7(10):e46678
  • Del Piccolo N, Placone J, He L, Agudelo SC, Hristova K “Production of plasma membrane vesicles with chloride salts and their utility as a cell membrane mimetic for biophysical characterization of membrane protein interactions.”, Anal Chem. 2012 Oct 16; 84(20), 8650-5
  • He J, Hristova K, Wimley WC “A highly charged voltage-sensor helix spontaneously translocates across membranes”, Angew Chem Int Ed Engl. 2012 Jul 16; 51(29), 7150-3
  • He L, Serrano C, Niphadkar N, Shobnam N, Hristova K “Effect of the G375C and G346E achondroplasia mutations on FGFR3 activation”, PLoS One. 2012; 7(4):e34808
  • Ohsfeldt E, Huang SH, Baycin-Hizal D, Kristoffersen L, Le TM, Li E, Hristova K, Betenbaugh MJ, “Increased expression of the integral membrane proteins EGFR and FGFR3 in anti-apoptotic Chinese hamster ovary cell lines” Biotechnol Appl Biochem. 2012 May-Jun;59(3):155-62. doi: 10.1002/bab.1000. Epub 2012 Feb 17.
  • Lin J, Motylinski J, Krauson AJ, Wimley WC, Searson PC, Hristova K. “Interactions of membrane active peptides with planar supported bilayers: an impedance spectroscopy study.”, Langmuir. 2012 Apr 10; 28(14):6088-96
  • Patrick Stahl, Juan Cruz,Y Li, Michael Yu, Kalina Hristova. “On-the-resin N-terminal modification of long synthetic peptides”, Anal Biochem. 2012 May 15;424(2), 137-9
  • Edwin Li, William Wimley, Kalina Hristova “Transmembrane helix dimerization: Beyond the search for sequence motifs “, Biochimica et Biophysica Acta 2012 Feb;1818(2), 183-93

2011

  • Fenghao Chen, Kalina Hristova “The physical basis of FGFR3 response to fgf1 and fgf2”, Biochemistry 2011 50(40):8576-82, In press
  • Lijuan He, Andrew Hoffmann, Christopher Serrano, Kalina Hristova, William Wimley “High-throughput selection of transmembrane sequences that enhance receptor tyrosine kinase activation”, Journal Molecular Biology 2011 412(1):43-54, In press
  • Lijuan He, Kalina Hristova, “Physical-chemical principles underlying RTK activation, and their implications for human disease”, Biochimica et Biophysica Acta (BBA) – Biomembranes 2011, In press
  • Maria Jesus Sanchez-Martin, Kalina Hristova, Montserrat Pujol, Maria J. Gomara, Isabel Haro, M. Asuncin Alsina and M. Antonia Busquets, “Analysis of HIV-1 fusion peptide inhibition by synthetic peptides from E1 protein of GB virus C”, Journal of Colloid and Interface Science 2011, In press
  • Jessica R. Marks, Jesse Placone, Kalina Hristova, and William C. Wimley, “Spontaneous Membrane-Translocating Peptides by Orthogonal High-Throughput Screening”, Journal of the American Chemical Society 2011, In press
  • Fenghao Chen, Catherine Degnin, Melanie Laederich, William A. Horton and Kalina Hristova, “The A391E mutation enhances FGFR3 activation in the absence of ligand”, Biochimica et Biophysica Acta (BBA) – Biomembranes 2011, In press
  • Lijuan He, Nadia Shobnam, William Wimley and Kalina Hristova, “FGFR3 Heterodimerization In Achondroplasia, The Most Common Form of Human Dwarfism”, The Journal of Biological Chemistry 2011, 286 (15), 13272-81
  • Kalina Hristova and William Wimley, “Antimicrobial peptides: Successes, challenges and unanswered questions”, Journal of Membrane Biology 2011, 239 (1-2), 27-34
  • Kalina Hristova and William Wimley, “A look at arginine in membranes”, Journal of Membrane Biology 2011, 239 (1-2), 49-56
  • Lijuan He, Nadia Shobnam, and Kalina Hristova, “Specific inhibition of pathogenic receptor tyrosine kinase activation by its transmembrane domain”, Biochimica et Biophysica Acta (BBA) – Biomembranes 2011, 1808 (1), 253-259

2010

  • Lirong Chen, Jesse Placone, Lawrence Novicky, and Kalina Hristova, “The extracellular domain of fibroblast growth factor receptor 3 inhibits ligand-independent dimerization”, Science Signaling 2010, 3 (150), ra86
  • Sandra Schick, Lirong Chen, Edwin Li, Janice Lin, Ingo K�per, and Kalina Hristova, “Assembly of the M2 tetramer is strongly modulated by lipid chain length”, Biophysical Journal 2010, 99 (6), 1810-1817
  • Lijuan He, William Horton, and Kalina Hristova, “The physical basis behind achondroplasia, the most common form of human dwarfism”, Journal of Biological Chemistry 2010, 285 (39), 30103-30114
  • Edwin Li and Kalina Hristova, “Receptor tyrosine kinase transmembrane domains: Function, dimer structure and dimerization energetics”, Cell Adhesion and Migration 2010, 49 (2), 249-254
  • Janice Lin, John Szymanski, Peter C. Searson, and Kalina Hristova, “Electrically Addressable, Biologically Relevant Surface-Supported Bilayers”, Langmuir 2010, 26 (14), 12054-12059
  • Lirong Chen, Lawrence Novicky, Mikhail Merzlyakov, Tihomir Hristov, and Kalina Hristova, “Measuring the Energetics of Membrane Protein Dimerization in Mammalian Membranes”, Journal of the American Chemical Society 2010, 132 (10), 3628-3635
  • Janice Lin, John Szymanski, Peter C. Searson, and Kalina Hristova, “Effect of a Polymer Cushion on the Electrical Properties and Stability of Surface-Supported Lipid Bilayers”, Langmuir 2010, 26 (5), 3544-3548

2009

  • Edwin Li, Mikhail Merzlyakov, Janice Lin, Peter C. Searson, an Kalina Hristova, “Utility of surface-supported bilayers in studies of transmembrane helix dimerization”, Journal of Structural Biology 2009, 168 (1), 53-60
  • Craig Snider, Sajith Jayasinghe, Kalina Hristova and Stephen H. White, “MPEx: A tool for exploring membrane proteins”, Protein Science 2009, 18 (12), 2624-2628
  • Ricky Soong, Mikhail Merzlyakov, and Kalina Hristova, “Hill Coefficient Analysis of Transmembrane Helix Dimerization”, Journal of Membrane Biology 2009, 230 (1), 49-55
  • William F. Walkenhorst, Mikhail Merzlyakov, Kalina Hristova, and William C. Wimley, “Polar residues in transmembrane helices can decrease electrophoretic mobility in polyacrylamide gels without causing helix dimerization”, Biochmica et Biophysica Acta-Biomembranes 2009, 1788 (6), 1321-1331
  • Shannon O’Connor, Edwin Li, Brian S. Majors, Lijuan He, Jesse Placone, Deniz Baycin, Michael J. Betenbaugh, and Kalina Hristova, “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 2009, 67 (1), 41-47
  • Lirong Chen, Mikhail Merzlyakov, Tomer Cohen, Yechei Shai, and Kalina Hristova, “Energetics of ErbB1 Transmembrane Domain Dimerization in Lipid Bilayers”, Biophysical Journal 2009, 96 (11), 4622-4630
  • Xue Han and Kalina Hristova, “Viewing the Bilayer Hydrocarbon Core Using Neutron Diffraction”, Journal of Membrane Biology 2009, 227 (3), 123-131

2008

  • Lijuan He and Kalina Hristova, “Pathogenic Activation of Receptor Tyrosine Kinases in Mammalian Membranes”, Journal of Molecular Biology 2008, 384 (5), 1130-1142
  • Janice Lin, Mikhail Merzlyakov, Kalina Hristova, and Peter C. Searson, “Impedance spectroscopy of bilayer membranes on single crystal silicon”, Biointerphases 2008, 3 (2), FA33-FA40
  • Mikhail Merzlyakov, Edwin Li, and Kalina Hristova, “Surface supported bilayer platform for studies of lateral association of proteins in membranes (Mini Review)”, Biointerphases 2008, 3 (2), FA80-FA84
  • William K. Chang, William C. Wimley, Peter C. Searson, Kalina Hristova, and Mikhail Merzlyakov, “Characterization of antimicrobial peptide activity by electrochemical impedance spectroscopy”, Biochmica et Biophysica Acta-Biomembranes 2008, 1778 (10), 2430-2436
  • Edwin Li, Jesse Placone, Mikhail Merzlyakov, and Kalina Hristova, “Quantitative measurements of protein interactions in a crowded cellular environment”, Analytical Chemistry 2008, 80 (15), 5976-5985
  • Yevgen O. Posokhov, Mikhail Merzlyakov, Kalina Hristova, and Alexey S. Ladokhin, “A simple “proximity” correction for Forster resonance energy transfer efficiency determination in membranes using lifetime measurements”, Analytical Biochemistry 2008, 380 (1), 134-136
  • Xue Han, Kalina Hristova, and William C. Wimley, “Protein Folding in Membranes: Insights from Neutron Diffraction Studies of a Membrane beta-sheet Oligomer”, Biophysical Journal 2008, 94 (2), 492-505

2007

  • pubsVesselin Nikolov, Janice Lin, Mikhail Merzlyakov, Kalina Hristova, and Peter C. Searson, “Electrical measurements of bilayer membranes formed by Langmuir-Blodgett deposition on single-crystal silicon”, Langmuir 2007 23 (26), 13040-13045
  • Sahalov, Harmonie, Brigid O’Brien, Kathleen J. Stebe, Kalina Hristova, and Peter C. Searson, “Influence of applied potential on the impedance of alkanethiol SAMs”, Langmuir 2007 23 (19), 9681-9685
  • Mikhail Merzlyakov, Lirong Chen, and Kalina Hristova “Studies of receptor tyrosine kinase transmembrane domain dimerization: The EmEx-FRET method”, Journal of Membrane Biology 2007, 215 (2-3), 93-13
  • Min You, Jamie Spangler, Edwin Li, Xue Han, Pijush Ghosh, and Kalina Hristova “Effect of pathogenic cysteine mutations on FGFR3 transmembrane domain dimerization in detergents and lipid bilayers”, Biochemistry 2007, 46 (39), 11039-11046

2006

  • Mikhail Merzlyakov, Edwin Li, Rachel Casas, and Kalina Hristova, “Surface-supported bilayers with transmembrane proteins: Role of the polymer cushion revisited”, Langmuir 2006, 22 (24), 10145-10151
  • Xue Han, Mihaella Mihailescu, and Kalina Hristova, “Neutron diffraction studies of fluid bilayers with transmembrane proteins: Structural consequences of the achondroplasia mutation”, Biophysical Journal 2006, 91 (10), 3736-3747
  • Vesselin Nikolov, Aleksandar Radisic, Kalina Hristova, and Peter Searson, “Bias-Dependent Admittance in Hybrid Bilayer Membranes”, Langmuir 2006, 22 (17), 7156-7158
  • Mikhail Merzlyakov, Edwin Li, Rachel Casas, and Kalina Hristova, “Spectral Forster Resonance Energy Transfer Detection of Protein Interactions in Surface-Supported Bilayers”, Langmuir 2006, 22 (16), 6986-6992
  • Edwin Li and Kalina Hristova, “Role of Receptor Tyrosine Kinase Transmembrane Domains in Cell Signaling and Human Pathologies”, Biochemistry 2006, 45 (20), 6241-6251
  • Edwin Li, Min You, and Kalina Hristova “FGFR3 Dimer stabilization due to a single amino acid pathogenic mutation.” Journal of Molecular Biology 2006, 356 (3), 600 – 612
  • Mikhail Merzlyakov, Edwin Li, and Kalina Hristova, “Directed Assembly of surface-supported bilayers with transmembrane helices.” Langmuir 2006, 22 (3), 1247-1253
  • Mikhail Merzlyakov, Min You, Edwin Li, and Kalina Hristova, “Transmembrane helix heterodimerization in lipid bilayers: probing the energetics behind autosomal dominant growth disorders”, Journal of Molecular Biology 2006, 358 (1), 1-7
  • Min You, Edwin Li, and Kalina Hristova, “The achondroplasia mutation does not alter the dimerization energetics of FGFR3 transmembrane domain”, Biochemistry 2006, 45 (17), 5551-5556

2005

  • Edwin Li, Min You, and Kalina Hristova, “SDS-PAGE and FRET suggest weak interactions between FGFR3 TM domains in the absence of extracellular domains and ligands”, Biochemistry 2005, 44 (1), 352 – 360
  • Min You, Edwin Li, William Wimley, Kalina Hristova, Förster resonance energy transfer in liposomes: Measurements of transmembrane helix dimerization in the native bilayer environment, Analytical Biochemistry 2005, 340 (1), 154-164
  • Takeo Iwamoto, Min You, Edwin Li, Jamie Spangler, John M. Tomich and Kalina Hristova, Synthesis and initial characterization of FGFR3 transmembrane domain: consequences of sequence modifications, Biochimica at Biophysica Acta-Biomembranes 2005, 1668 (2), 240-247
  • Kalina Hristova and S. H. White, “An experiment-based algorithm for predicting the partitioning of unfolded peptides into phosphatidylcholine bilayer interfaces.”. Biochemistry 2005, 44 (37), 12614 – 12619

2004

  • Edwin Li and Kalina Hristova, Imaging Förster Resonance Energy Transfer measurements of transmembrane helix interactions in lipid bilayers on a solid support, Langmuir 2004 , 20 (21), 9053-9060.