Janna M. Bigalke

ORCID: 0000-0002-3473-4390
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About
Contact & Profiles
Research Areas
  • Herpesvirus Infections and Treatments
  • Cytomegalovirus and herpesvirus research
  • RNA regulation and disease
  • RNA Research and Splicing
  • Signaling Pathways in Disease
  • RNA and protein synthesis mechanisms
  • Genomics and Chromatin Dynamics
  • Superconducting Materials and Applications
  • Radiopharmaceutical Chemistry and Applications
  • Caveolin-1 and cellular processes
  • Particle Accelerators and Free-Electron Lasers
  • Mechanisms of cancer metastasis
  • Calibration and Measurement Techniques
  • Vector-borne infectious diseases
  • Parvovirus B19 Infection Studies
  • Neuropeptides and Animal Physiology
  • Amino Acid Enzymes and Metabolism
  • Spacecraft and Cryogenic Technologies
  • Protein Degradation and Inhibitors
  • Hepatitis Viruses Studies and Epidemiology
  • HIV Research and Treatment
  • Proteoglycans and glycosaminoglycans research
  • Congenital heart defects research
  • Enzyme Structure and Function
  • Viral Infections and Immunology Research

AstraZeneca (Sweden)
2018-2019

Tufts University
2014-2017

Boston University
2016

Max Planck Institute of Molecular Physiology
2010-2011

Max Planck Society
2010

University of Lübeck
2005

Most DNA viruses replicate in the nucleus and exit it either by passing through nuclear pores or rupturing envelope. Unusually, herpesviruses have evolved a complex mechanism of escape whereby nascent capsids bud at inner membrane to form perinuclear virions that subsequently fuse with outer membrane, releasing into cytosol. Although this general scheme is accepted field, players their roles are still debated. Recent studies illuminated critical mechanistic features enigmatic process...

10.1146/annurev-virology-110615-042215 article EN Annual Review of Virology 2016-08-02

Signaling through the receptor tyrosine kinase RET is essential during normal development. Both gain- and loss-of-function mutations are involved in a variety of diseases, yet molecular details activation have remained elusive. We reconstituted complete extracellular region signaling complex together with Neurturin (NRTN) GFRα2 determined its structure at 5.7-Å resolution by cryo-EM. The proteins form an assembly RET-GFRα2 RET-NRTN interfaces. Two key interaction points required for domain...

10.1126/sciadv.aau4202 article EN cc-by-nc Science Advances 2019-07-05

Transcription elongation is regulated by the cellular protein Hexim1, which inhibits phosphorylation of RNA polymerase II interacting with positive transcription factor P-TEFb. Hexim1 binds directly to Cyclin T1 P-TEFb its coiled coil domain that subdivided into a highly polar N-terminal segment containing nonconservative residues in dimer interface and C-terminal an evolutionarily conserved sequence composition. Here we show noncanonical composition first required for interaction while...

10.1021/bi902072f article EN Biochemistry 2010-03-08

The protocol describes the production and crystallization of soluble form nuclear egress complex (NEC) from Herpes simplex virus 1 Pseudorabies virus. NEC is a heterodimer that consists conserved proteins UL31 UL34. oligomerization deforms inner membrane around capsid in infected cells, thereby mediating budding into perinuclear space during egress. We have successfully developed for large-scale preparation highly pure two different viruses prokaryotic expression system, which enabled us to...

10.21769/bioprotoc.1872 article EN BIO-PROTOCOL 2016-01-01
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