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Kalina Hristova

Johns Hopkins University · Materials Science and Engineering

Active 1988–2026

h-index52
Citations10.5k
Papers32095 last 5y
Funding$15.5M1 active

Academic metrics are sourced from OpenAlex and public funding records; values may differ from Google Scholar.

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About

Kalina Hristova is a professor of materials science and engineering at Johns Hopkins University. Her research focuses on the structure and assembly of biological membranes, studying the thermodynamic and structural principles that underlie membrane protein folding and signal transduction across membranes. Her lab primarily investigates receptor tyrosine kinases (RTKs), which are often dysregulated in cancer, aiming to understand their function through novel quantitative methodologies she has pioneered. Her work has contributed to a better understanding of RTK activation, membrane-active peptides, and their mechanisms of action, which have applications in drug delivery. Hristova's current research projects include exploring ligand functional selectivity of membrane receptors, the role of the membrane protein interactome, RTK-associated pathogenesis, pH-sensitive peptides for endosomal release, and peptides capable of permeating cellular barriers.

Research topics

  • Chemistry
  • Biophysics
  • Cell biology
  • Biology
  • Biochemistry

Selected publications

  • Applications and evolution of melittin, the quintessential membrane active peptide

    Biochemical Pharmacology · 2021-09-17 · 144 citations

    reviewOpen accessCorresponding
  • Ligand bias in receptor tyrosine kinase signaling

    Journal of Biological Chemistry · 2020-10-29 · 61 citations

    reviewOpen accessSenior authorCorresponding

    Ligand bias is the ability of ligands to differentially activate certain receptor signaling responses compared with others. It reflects differences in the responses of a receptor to specific ligands and has implications for the development of highly specific therapeutics. Whereas ligand bias has been studied primarily for G protein-coupled receptors (GPCRs), there are also reports of ligand bias for receptor tyrosine kinases (RTKs). However, the understanding of RTK ligand bias is lagging behind…

  • Determining the statistical significance of the difference between arbitrary curves: A spreadsheet method

    PLoS ONE · 2023-10-31 · 39 citations

    articleOpen access1st authorCorresponding

    We present a simple, spreadsheet-based method to determine the statistical significance of the difference between any two arbitrary curves. This modified Chi-squared method addresses two scenarios: A single measurement at each point with known standard deviation, or multiple measurements at each point averaged to produce a mean and standard error. The method includes an essential correction for the deviation from normality in measurements with small sample size, which are typical in biomedical s…

  • Quantifying the strength of heterointeractions among receptor tyrosine kinases from different subfamilies: Implications for cell signaling

    Journal of Biological Chemistry · 2020-05-28 · 38 citations

    articleOpen accessSenior authorCorresponding

    Receptor tyrosine kinases (RTKs) are single-pass membrane proteins that control vital cell processes such as cell growth, survival, and differentiation. There is a growing body of evidence that RTKs from different subfamilies can interact and that these diverse interactions can have important biological consequences. However, these heterointeractions are often ignored, and their strengths are unknown. In this work, we studied the heterointeractions of nine RTK pairs, epidermal growth factor rece…

  • Structural basis for the transmembrane signaling and antidepressant-induced activation of the receptor tyrosine kinase TrkB

    Nature Communications · 2024-10-29 · 12 citations

    articleOpen access

    Neurotrophin receptors of the Trk family are involved in the regulation of brain development and neuroplasticity, and therefore can serve as targets for anti-cancer and stroke-recovery drugs, antidepressants, and many others. The structures of Trk protein domains in various states upon activation need to be elucidated to allow rational drug design. However, little is known about the conformations of the transmembrane and juxtamembrane domains of Trk receptors. In the present study, we employ NMR…

Recent grants

Frequent coauthors

  • William C. Wimley

    Tulane University

    66 shared
  • Pavel Krejčı́

    University Hospital Brno

    43 shared
  • Elena B. Pasquale

    Discovery Institute

    41 shared
  • Bohumil Fafílek

    38 shared
  • Taylor P. Light

    Champions Oncology (United States)

    36 shared
  • Edwin Li

    The University of Texas at Austin

    32 shared
  • Nuala Del Piccolo

    Imperial College London

    29 shared
  • Pooja Dudeja

    Institute of Animal Physiology of the Slovak Academy of Sciences

    27 shared

Awards & honors

  • Biophysical Society’s Dayhoff award
  • Fellow of the American Physical Society
  • Fellow of the American Institute for Medical and Biological…

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