About

Vera Moiseenkova-Bell is a Professor of Systems Pharmacology and Translational Therapeutics at the University of Pennsylvania's Perelman School of Medicine. She serves as the Faculty Director of the Electron Microscopy Resource Laboratory and the Beckman Center for Cryo Electron Microscopy. Her educational background includes a Master of Science in Laser Biophysics from Moscow State University and a PhD in Cellular Physiology & Molecular Biophysics from the University of Texas Medical Branch. Her research focuses on the structure, function, and pharmacology of ion channels, with significant contributions to understanding the gating mechanisms of TRPV channels and the structural insights into ion channel function. She has authored numerous publications in the field, emphasizing her expertise in cryo-electron microscopy and molecular biophysics.

Research topics

• Computational biology
• Chemistry
• Computer Science
• Artificial Intelligence
• Biology
• Cell biology
• Biophysics

Selected publications

• Visualization of TRPML1-containing lysosomes in situ

  Biophysical Journal · 2024 · 1 citations

  Senior authorCorresponding
  • Computer Science
  • Artificial Intelligence
  • Chemistry
  DOI

• Structural and functional studies of TRPML1 in situ

  Biophysical Journal · 2024 · 1 citations

  Senior authorCorresponding
  • Computational biology
  • Biology
  • Chemistry
  DOI

• Using biochemistry and biophysics to extinguish androgen receptor signaling in prostate cancer

  Journal of Biological Chemistry · 2020 · 31 citations

  • Chemistry
  • Cell biology
  • Biology

  Castration resistant prostate cancer (CRPC) continues to be androgen receptor (AR) driven. Inhibition of AR signaling in CRPC could be advanced using state-of-the-art biophysical and biochemical techniques. Structural characterization of AR and its complexes by cryo-electron microscopy would advance the development of N-terminal domain (NTD) and ligand-binding domain (LBD) antagonists. The structural basis of AR function is unlikely to be determined by any single structure due to the intrinsic disorder of its NTD, which not only interacts with coregulators but likely accounts for the constitutive activity of AR-splice variants (SV), which lack the LBD and emerge in CRPC. Using different AR constructs lacking the LBD, their effects on protein folding, DNA binding, and transcriptional activity could reveal how interdomain coupling explains the activity of AR-SVs. The AR also interacts with coregulators that promote chromatin looping. Elucidating the mechanisms involved can identify vulnerabilities to treat CRPC, which do not involve targeting the AR. Phosphorylation of the AR coactivator MED-1 by CDK7 is one mechanism that can be blocked by the use of CDK7 inhibitors. CRPC gains resistance to AR signaling inhibitors (ARSI). Drug resistance may involve AR-SVs, but their role requires their reliable quantification by SILAC-mass spectrometry during disease progression. ARSI drug resistance also occurs by intratumoral androgen biosynthesis catalyzed by AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase), which is unique in that its acts as a coactivator of AR. Novel bifunctional inhibitors that competitively inhibit AKR1C3 and block its coactivator function could be developed using reverse-micelle NMR and fragment-based drug discovery.

  PublisherOA PDFDOI

Frequent coauthors

• Bridget M. McVeigh

  Translational Therapeutics (United States)

  8 shared

• Elaine M. Mihelc

  University of Pennsylvania

  4 shared

• Gary A. Bradshaw

  Center for Systems Biology

  4 shared

• Marian Kalocsay

  The University of Texas MD Anderson Cancer Center

  4 shared

• Aria E. Garrett

  Translational Therapeutics (United States)

  4 shared

• Robyn J. Eisert

  Boston VA Research Institute

  4 shared

• Shrawan Kumar Mageswaran

  University of Pennsylvania

  2 shared

• Yi‐Wei Chang

  2 shared

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