Anja Berndt

ORCID: 0000-0002-4992-8227
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About
Contact & Profiles
Research Areas
  • Cytomegalovirus and herpesvirus research
  • Herpesvirus Infections and Treatments
  • Ubiquitin and proteasome pathways
  • Toxoplasma gondii Research Studies
  • Cancer-related Molecular Pathways
  • Viral-associated cancers and disorders
  • Immunotherapy and Immune Responses
  • Interdisciplinary Research and Collaboration
  • Sustainability and Climate Change Governance
  • Cancer, Hypoxia, and Metabolism
  • Glycosylation and Glycoproteins Research
  • HIV Research and Treatment
  • Innovative Approaches in Technology and Social Development

UK Research and Innovation
2021

Biotechnology and Biological Sciences Research Council
2021

University of Leeds
2014

University of Bristol
2012-2013

Friedrich-Alexander-Universität Erlangen-Nürnberg
2006-2009

We previously showed that open reading frame (ORF) UL26 of human cytomegalovirus, a member the US22 multigene family betaherpesviruses, encodes novel tegument protein, which is imported into cells in course viral infection. Moreover, we demonstrated pUL26 contains strong transcriptional activation domain and capable stimulating major immediate-early (IE) enhancer-promoter. Since this suggested an important function during initiation replicative cycle, sought to ascertain relevance by...

10.1128/jvi.02585-05 article EN Journal of Virology 2006-05-12

The human cytomegalovirus (HCMV) immediate-early 2 (IE2) transactivator has previously been shown to form intranuclear, dot-like accumulations in association with subnuclear structures known as promyelocytic leukemia protein (PML) nuclear bodies or ND10. We recently observed that IE2 can even after infection of PML knockdown cells, which lack genuine To further analyze the determinants localization, a recombinant HCMV expressing fused enhanced green fluorescent was constructed. infected...

10.1128/jvi.01009-07 article EN Journal of Virology 2007-07-12

ABSTRACT The major transactivator protein IE2p86 of human cytomegalovirus (HCMV) has previously been shown to undergo posttranslational modification by the covalent attachment SUMO proteins, termed SUMOylation, which occurs at two lysine residues located amino acid positions 175 and 180. Mutation acceptor lysines resulted in abrogation SUMOylation mammalian cells a strong reduction IE2p86-mediated transactivation. In this paper, we identify an additional interaction motif (SIM) within...

10.1128/jvi.01525-09 article EN Journal of Virology 2009-10-08

Responsible research and innovation (RRI) has been the preferred idiom for interrogating social, ethical political dimensions of science, technology roughly a decade. The uptake RRI into prominent policy organisations resulted in proliferation frameworks as makers have attempted to articulate what it means them enact RRI. Here, we draw on our experience developing an framework ERA Cofund Biotechnology. We discuss three ways that treating form knowledge production allowed us engage with...

10.1080/23299460.2021.1935584 article EN cc-by Journal of Responsible Innovation 2021-05-04

Post-translational modifications of proteins are essential for cell function. Covalent modification by SUMO (small ubiquitin-like modifier) plays a role in multiple processes, including transcriptional regulation, DNA damage repair, protein localization and trafficking. Factors affecting trafficking particularly crucial neurons because their polarization, morphological complexity functional specialization. SUMOylation has emerged as major mediator intranuclear nucleo-cytoplasmic...

10.3390/biom2020256 article EN cc-by Biomolecules 2012-05-14

The γ‑herpesviruses Epstein-Barr virus and Kaposi's sarcoma‑associated herpesvirus are successful pathogens, each infecting a large proportion of the human population. These viruses persist for life host may contribute to number malignancies, which there currently no cures. Large‑scale proteomic-based approaches provide an excellent means increasing collective understanding proteomes these complex elucidating their numerous interactions within infected cell. large‑scale studies important...

10.3892/mco.2014.341 article EN Molecular and Clinical Oncology 2014-07-09

Monobodies are small recombinant proteins designed to bind with high affinity target proteins. have been generated mimic the SIM [SUMO (small ubiquitin-like modifier)-interacting motif] present in many SUMO proteins, but their properties not determined cells. In study we characterize of two SUMO1-specific monobodies (hS1MB4 and hS1MB5) HEK (human embyronic kidney)-293 HeLa cells examine ability purify substrates from cell lines rat brain. Both hS1MB4 hS1MB5 compared favourably commercially...

10.1042/bj20130241 article EN Biochemical Journal 2013-09-19
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