Vitaliya Sagulenko

ORCID: 0000-0002-9075-6025
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About
Contact & Profiles
Research Areas
  • Inflammasome and immune disorders
  • Kawasaki Disease and Coronary Complications
  • interferon and immune responses
  • Heme Oxygenase-1 and Carbon Monoxide
  • Biomedical Research and Pathophysiology
  • Cell death mechanisms and regulation
  • Microtubule and mitosis dynamics
  • Transgenic Plants and Applications
  • Immune Response and Inflammation
  • Legume Nitrogen Fixing Symbiosis
  • Neuroblastoma Research and Treatments
  • Plant tissue culture and regeneration
  • Cancer Genomics and Diagnostics
  • Genetic factors in colorectal cancer
  • Coastal wetland ecosystem dynamics
  • Macrophage Migration Inhibitory Factor
  • IL-33, ST2, and ILC Pathways
  • Protein Degradation and Inhibitors
  • Toxin Mechanisms and Immunotoxins
  • Chromatin Remodeling and Cancer
  • DNA Repair Mechanisms
  • Genomic variations and chromosomal abnormalities
  • Immunotherapy and Immune Responses
  • Phagocytosis and Immune Regulation
  • Chromosomal and Genetic Variations

The University of Queensland
2010-2024

German Cancer Research Center
2007-2012

Heidelberg University
2012

All-Russian Research Institute of Agricultural Microbiology
2004

The University of Texas Health Science Center at Houston
2001

Abstract Inflammasomes are large protein complexes induced by a wide range of microbial, stress, and environmental stimuli that function to induce cell death inflammatory cytokine processing. Formation an inflammasome involves dramatic relocalization the adapter apoptosis-associated speck-like containing caspase recruitment domain (ASC) into single speck. We have developed flow cytometric assay for formation, time flight evaluation, which detects change in ASC distribution within cell. The...

10.4049/jimmunol.1401110 article EN The Journal of Immunology 2014-11-18

Mouse p202 containing two hemopoietic expression, interferon inducibility, nuclear localization (HIN) domains antagonizes AIM2 inflammasome signaling and potentially modifies lupus susceptibility. We found that only HIN1 of binds double-stranded DNA (dsDNA), while HIN2 forms a homotetramer. Crystal structures revealed dsDNA is bound on face opposite the site used in IFI16. The structure dimer dimers, analogous to binding being dimerization interface. Electron microscopy imaging showed...

10.1016/j.celrep.2013.06.024 article EN cc-by-nc-nd Cell Reports 2013-07-01

ABSTRACT The VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) system, type IV secretion pathway required for delivery T-DNA and effector proteins to plant cells during infection. In this study, we examined effects virB11 mutations on VirB protein accumulation, T-pilus production, substrate translocation. Strains synthesizing derivatives with in nucleoside triphosphate binding site (Walker A motif) accumulated wild-type levels but failed produce or export...

10.1128/jb.183.20.5813-5825.2001 article EN Journal of Bacteriology 2001-10-15

ABSTRACT Agrobacterium tumefaciens transfers oncogenic T-DNA and effector proteins to plant cells via a type IV secretion pathway. This transfer system, assembled from the products of virB operon, is thought consist transenvelope mating channel T pilus. When screened for presence VirB VirE proteins, material sheared cell surface octopine strain A348 was seen possess detectable levels VirB2 pilin, VirB5, VirB7 outer membrane lipoprotein. Material most gene deletion mutants also possessed...

10.1128/jb.183.12.3642-3651.2001 article EN Journal of Bacteriology 2001-06-15

Abstract Inflammasomes are protein complexes that promote caspase activation, resulting in processing of IL-1β and cell death, response to infection cellular stresses. have been anticipated contribute autoimmunity. The New Zealand Black (NZB) mouse develops anti-erythrocyte Abs is a model autoimmune hemolytic anemia. These mice also develop anti-nuclear typical lupus. In this article, we show NZB macrophages deficient inflammasome responses DNA virus fungal infection. Absent melanoma 2...

10.4049/jimmunol.1402859 article EN The Journal of Immunology 2015-06-27

Caspase-8 is required for extrinsic apoptosis, but also central preventing a pro-inflammatory receptor interacting protein kinase (RIPK) 3-mixed lineage domain-like (MLKL)-dependent cell death pathway termed necroptosis.Despite these critical cellular functions, the impact of capase-8 deletion in myeloid lineage, which forms basis innate immune responses, has remained unclear.In recent article Arthritis Research & Therapy, Cuda et al. report that cell-restricted caspase-8 loss leads to very...

10.1186/s13075-015-0910-0 article EN cc-by Arthritis Research & Therapy 2016-01-06

Caspase-1 location in cells has been studied with fluorochrome-labeled inhibitors of caspase-1 (FLICA reagents). We report that FLICA reagents have limited cell-membrane permeability. This impacts experimental design as intact membranes, including knockout cells, are not appropriate controls for inflammasome-induced gasdermin D membrane pores. is an inflammatory initiator caspase responsible the maturation pro-inflammatory cytokines IL-1β and IL-18 pyroptotic cell death. Inhibitors important...

10.1002/eji.202350515 article EN cc-by European Journal of Immunology 2024-02-15

The migrational propensity of neuroblastoma is affected by cell identity, but the mechanisms behind divergence remain unknown. Using RNAi and time-lapse imaging, we show that ADRN-type NB cells exhibit RAC1- kalirin-dependent nucleokinetic (NUC) migration relies on several integral components neuronal migration. Inhibition NUC RAC1 kalirin-GEF1 inhibitors occurs without hampering proliferation ADRN identity. three clinically relevant expression dichotomies, reveal most up-regulated mRNAs in...

10.26508/lsa.201900332 article EN cc-by Life Science Alliance 2021-03-03

10.17615/914c-st02 article EN Carolina Digital Repository (University of North Carolina at Chapel Hill) 2013-01-01
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