Stefanos A. Tsiftsoglou

ORCID: 0000-0001-9813-1022
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About
Contact & Profiles
Research Areas
  • Complement system in diseases
  • Blood Coagulation and Thrombosis Mechanisms
  • Erythrocyte Function and Pathophysiology
  • SARS-CoV-2 and COVID-19 Research
  • COVID-19 Clinical Research Studies
  • Blood groups and transfusion
  • Transgenic Plants and Applications
  • Amyotrophic Lateral Sclerosis Research
  • Heme Oxygenase-1 and Carbon Monoxide
  • Epigenetics and DNA Methylation
  • Hemoglobin structure and function
  • Glycosylation and Glycoproteins Research
  • Kawasaki Disease and Coronary Complications
  • Inflammation biomarkers and pathways
  • CRISPR and Genetic Engineering
  • Acute Myeloid Leukemia Research
  • Histone Deacetylase Inhibitors Research
  • Porphyrin Metabolism and Disorders
  • Enzyme Structure and Function
  • Reproductive System and Pregnancy
  • Neuroinflammation and Neurodegeneration Mechanisms
  • Phagocytosis and Immune Regulation
  • Agriculture and Biological Studies
  • Pluripotent Stem Cells Research
  • Coagulation, Bradykinin, Polyphosphates, and Angioedema

Aristotle University of Thessaloniki
2021-2025

International Hellenic University
2024-2025

Academy of Athens
2020

Boston Children's Hospital
2013

Newcastle University
2011

University of Oxford
2002-2011

Harvard University
2008-2009

Boston University
2008

Boston Biomedical Research Institute
2008

Tsinghua University
2005

Amyotrophic Lateral Sclerosis (ALS) is an adult-onset, progressive, motor neuron degenerative disease, in which the role of inflammation not well established. Innate and adaptive immunity were investigated CNS Superoxide Dismutase 1 (SOD1)(G93A) transgenic mouse model ALS. CD4+ CD8+ T cells infiltrated SOD1(G93A) spinal cords during disease progression. Cell-specific flow cytometry gene expression profiling showed significant phenotypic changes microglia, including dendritic cell receptor...

10.1073/pnas.0804610105 article EN Proceedings of the National Academy of Sciences 2008-11-08

The complement system is a key component of innate and adaptive immune responses. Complement regulation critical for prevention control disease. We have determined the crystal structure regulatory enzyme human factor I (fI). FI in proteolytically inactive form, demonstrating that it circulates zymogen-like state despite being fully processed to mature sequence. Mapping functional data from mutants fI onto suggests this form maintained by noncatalytic heavy-chain allosterically modulating...

10.1073/pnas.1102167108 article EN Proceedings of the National Academy of Sciences 2011-07-18

The factors that allow self‐reactive B cells to escape negative selection and become activated remain poorly defined. Using a BCR knock‐in mouse strain, we identify pathway by which ‐cell nucleolar self‐antigens is complement dependent. Deficiency in component C 4 led breakdown the elimination of autoreactive clones at transitional stage, characterized relative increase their response range stimuli, entrance into follicles, greater propensity form GC s. mixed BM chimeras, found myeloid...

10.1002/eji.201343412 article EN European Journal of Immunology 2013-06-10

Abstract Complement factor I (fI) plays a major role in the regulation of complement system. It circulates an active form and has very restricted specificity, cleaving only C3b or C4b presence cofactor such as H (fH), receptor type 1, membrane protein, C4-binding protein. Using peptide-7-amino-4-methylcoumarin derivatives, we investigated substrate specificity fI. There is no previous report synthetic cleavage by fI, but five substrates were found this study. A survey 15 range inhibitors...

10.4049/jimmunol.173.1.367 article EN The Journal of Immunology 2004-07-01

Factor I (fI) is a major regulator of complement. As protease it has very restricted specificity, cleaving only C3b or C4b in the presence cofactor such as factor H (fH). Cleavage by fI yields iC3b, opsonin. The cleavage occurs through formation ternary complex between enzyme, substrate, and cofactor. catalytic subunit fI, SP domain, accommodates substrate recognition cleavage. role heavy chain within catalysis unknown. Using partial proteolysis affinity chromatography an intact form domain...

10.1021/bi047680t article EN Biochemistry 2005-03-29

Abstract Heme (iron protoporphyrin IX) is an essential regulator conserved in all known organisms. We investigated the kinetics of intracellular accumulation hemin (oxidized form) human transformed proerythroid K562 cells using [ 14 C]‐hemin and observed that it time temperature‐dependent, affected by presence serum proteins, as well amphipathic/hydrophobic properties hemin. Hemin‐uptake exhibited saturation a function concentration added, suggesting involvement carrier‐cell surface...

10.1002/jcp.30595 article EN Journal of Cellular Physiology 2021-10-07

Tumor malignant cells are characterized by dysregulation of mitochondrial bioenergetics due to the 'Warburg effect'. In present study, this metabolic imbalance was explored as a potential target for novel cancer chemotherapy. Imatinib (IM) downregulates expression levels

10.3892/ijo.2024.5630 article EN cc-by-nc-nd International Journal of Oncology 2024-02-27

Complement receptor 1-related protein Y (CrrY) is an important cell-surface regulator of complement that unique to rodent species.The structure rat CrrY domains 1-4 has been determined in two distinct crystal forms and reveals a 70 bend between 3 4. Comparisons this with those other regulators suggests rearrangement interface may occur on forming the regulatory complex C3b.

10.1107/s1744309111016551 article EN cc-by Acta Crystallographica Section F Structural Biology and Crystallization Communications 2011-06-22

Poster Sessions C217 spacer-and RPEL-actins, which bind weakly in solution.Cytoplasmic MRTF-A localization resting fibroblasts requires spacer-actin binding.The bipartite importin {alpha-beta} binding site is buried the pentameric assembly, explaining how elevated G-actin concentrations prevent nuclear import.The structures show actin loads onto RPEL domain, and reveal a molecular mechanism by can control activity of one its ligands.

10.1107/s0108767311094608 article EN Acta Crystallographica Section A Foundations of Crystallography 2011-08-22
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