Orsolya Tőke

ORCID: 0000-0002-1741-1573
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About
Contact & Profiles
Research Areas
  • Drug Transport and Resistance Mechanisms
  • Protein Structure and Dynamics
  • Antimicrobial Peptides and Activities
  • Liver Disease Diagnosis and Treatment
  • Lipid Membrane Structure and Behavior
  • Protein Interaction Studies and Fluorescence Analysis
  • Molecular spectroscopy and chirality
  • Advanced NMR Techniques and Applications
  • Protein Kinase Regulation and GTPase Signaling
  • Electron Spin Resonance Studies
  • Metabolism and Genetic Disorders
  • Solid-state spectroscopy and crystallography
  • Pediatric Hepatobiliary Diseases and Treatments
  • Glycosylation and Glycoproteins Research
  • Enzyme Structure and Function
  • Luminescence and Fluorescent Materials
  • DNA and Nucleic Acid Chemistry
  • Neuroscience and Neuropharmacology Research
  • Analytical Chemistry and Chromatography
  • Microfluidic and Capillary Electrophoresis Applications
  • Molecular Sensors and Ion Detection
  • Immune Response and Inflammation
  • Monoclonal and Polyclonal Antibodies Research
  • Supramolecular Chemistry and Complexes
  • Protein Tyrosine Phosphatases

HUN-REN Research Centre for Natural Sciences
2016-2025

Institute of Molecular Life Sciences
2022

Hungarian Academy of Sciences
1995-2019

Institute of Organic Chemistry
2013-2017

Eötvös Loránd University
1995-2009

Washington University in St. Louis
2004-2005

Genaera (United States)
2004

Intrinsically disordered proteins lack a stable tertiary structure and form dynamic conformational ensembles due to their characteristic physicochemical properties amino acid composition. They are abundant in nature responsible for large variety of cellular functions. While numerous bioinformatics tools have been developed silico disorder prediction the last decades, there is need experimental methods verify state. CD spectroscopy widely used protein secondary analysis. It usable wide...

10.3389/fmolb.2022.863141 article EN cc-by Frontiers in Molecular Biosciences 2022-05-03

Glutamate (Glu) and gamma-aminobutyric acid (GABA) transporters play important roles in regulating neuronal activity. Glu is removed from the extracellular space dominantly by glial transporters. In contrast, GABA mainly taken up neurons. However, transporter subtypes share their localization with expression confined to same subpopulation of astrocytes, raising possibility cooperation between transport processes.Here we used diverse biological models both vitro vivo explore interplay these...

10.1371/journal.pone.0007153 article EN cc-by PLoS ONE 2009-09-23

Abstract Transcription factor phosphorylation at specific sites often activates gene expression, but how environmental cues quantitatively control transcription is not well-understood. Activating protein 1 factors are phosphorylated by mitogen-activated kinases (MAPK) in their transactivation domains (TAD) so-called phosphoswitches, which a hallmark response to growth factors, cytokines or stress. We show that the ATF2 TAD controlled functionally distinct signaling pathways (JNK and p38)...

10.1038/s41467-020-19582-3 article EN cc-by Nature Communications 2020-11-13

Human ileal bile acid-binding protein (hI-BABP), a member of the family intracellular lipid-binding proteins, has key role in enterohepatic circulation salts. The two internal binding sites hI-BABP exhibit positive cooperativity accompanied by site preference glycocholate (GCA) and glycochenodeoxycholate (GCDA), most abundant salts human body. Previous study Q51A its apo state, mutant with lost site-selectivity, suggests that disruption hydrogen-bonding network vicinity C/D-turn long-range...

10.1016/j.jsb.2025.108202 article EN cc-by-nc-nd Journal of Structural Biology 2025-04-01

Human ileal bile acid binding protein (I-BABP) is a member of the family intracellular lipid-binding proteins and thought to play role in enterohepatic circulation salts. Our group has previously shown that human I-BABP binds two molecules glycocholate (GCA) with low intrinsic affinity but an extraordinary high degree positive cooperativity. Besides strong cooperativity, exhibits site selectivity its interactions GCA glycochenodeoxycholate (GCDA), major salts humans. In this study, on basis...

10.1021/bi051781p article EN Biochemistry 2005-12-24

For efficient targeting of oncogenic K-Ras interaction sites, a mechanistic picture the Ras-cycle is necessary. Herein, we used NMR relaxation techniques and molecular dynamics simulations to decipher role slow in wild-type three P-loop mutants K-Ras. Our measurements reveal dominant two-state conformational exchange on ms timescale both GDP- GTP-bound The identified low-populated higher energy state GDP-loaded has conformation reminiscent nucleotide-bound/Mg2+ -free characterized by...

10.1002/chem.202201449 article EN cc-by-nc-nd Chemistry - A European Journal 2022-07-04

Human ileal bile acid binding protein (I-BABP), a member of the family intracellular lipid proteins, is thought to play role in enterohepatic circulation salts. Previously, we have shown by stopped-flow fluorescence analysis that positive cooperativity exhibited I-BABP its interactions with glycocholate (GCA) and glycochenodeoxycholate (GCDA), two primary salts humans, related slow conformational change protein. In this study, used backbone 15N relaxation nuclear magnetic resonance (NMR)...

10.1021/bi201588q article EN Biochemistry 2012-02-13

Cooperative ligand binding to human ileal bile acid protein (I-BABP) was studied using the stopped-flow fluorescence technique. The kinetic data obtained for wild-type are in agreement with a four-step mechanism where after fast conformational change on millisecond time scale, ligands bind sequential manner, followed by another, slow scale of seconds. This last step is more pronounced case glycocholate (GCA), salt that binds high positive cooperativity and absent mutant I-BABP proteins lack...

10.1021/bi700030r article EN Biochemistry 2007-04-14

Besides aiding digestion, bile salts are important signal molecules exhibiting a regulatory role in metabolic processes. Human ileal acid binding protein (I-BABP) is an intracellular carrier of the epithelial cells distal small intestine and has key enterohepatic circulation salts. Positive cooperativity combined with site selectivity glycocholate glycochenodeoxycholate, two most abundant human body, make I-BABP unique member family lipid proteins. Solution NMR structure ternary complex...

10.1111/febs.13610 article EN FEBS Journal 2015-11-27

The inclusion of protonated (-)-tetrahydropalmatine (THP+) and dehydrocorydaline (DHC+), natural alkaloids, in the cavity cucurbit[7]uril was monitored real time by a spectrofluorimetric method water at various temperatures. Both guests produced 1 : complexes enthalpy controlled processes without any detectable intermediates. tight entrance CB7 imposed substantial steric hindrance for encapsulation making entry into host several orders magnitude slower than diffusion. Despite ∼6 kJ mol-1...

10.1039/c8cp07231k article EN cc-by Physical Chemistry Chemical Physics 2019-01-01

Human ileal bile acid-binding protein (I-BABP), a member of the family intracellular lipid binding proteins plays key role in cellular trafficking and metabolic regulation salts. The has two internal and, according to recent study, an additional superficial site binds di- trihydroxy salts with positive cooperativity high degree site-selectivity. Previously, apo form, we have identified extensive network conformational fluctuations on millisecond time scale, which cease upon ligation....

10.1021/bi500553f article EN Biochemistry 2014-07-29
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