Sara Bologna

ORCID: 0000-0002-2709-8322
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About
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Research Areas
  • Advanced Fluorescence Microscopy Techniques
  • Protein Structure and Dynamics
  • Parkinson's Disease Mechanisms and Treatments
  • Protein Interaction Studies and Fluorescence Analysis
  • Neurological disorders and treatments
  • Photosynthetic Processes and Mechanisms
  • Ubiquitin and proteasome pathways
  • Advanced Electron Microscopy Techniques and Applications
  • Supramolecular Self-Assembly in Materials
  • Alzheimer's disease research and treatments
  • Hemoglobin structure and function
  • Analytical Chemistry and Chromatography
  • Advanced MRI Techniques and Applications
  • Lanthanide and Transition Metal Complexes
  • Wnt/β-catenin signaling in development and cancer
  • Force Microscopy Techniques and Applications
  • Cancer-related gene regulation
  • S100 Proteins and Annexins
  • Photochemistry and Electron Transfer Studies
  • Photoreceptor and optogenetics research
  • Botulinum Toxin and Related Neurological Disorders
  • Genetic Neurodegenerative Diseases
  • Chemical Synthesis and Analysis
  • Mesoporous Materials and Catalysis
  • Computational Drug Discovery Methods

Central European Institute of Technology
2024

Interuniversity Consortium for Magnetic Resonance
2018-2023

University of Florence
2018-2023

University of Parma
2004-2005

Istituto Nazionale per la Fisica della Materia
2004

Abstract Background Aggregation of α-synuclein (α-syn) is a prominent feature Parkinson’s disease (PD) and other synucleinopathies. Currently, α-syn seed amplification assays (SAAs) using cerebrospinal fluid (CSF) represent the most promising diagnostic tools for However, CSF itself contains several compounds that can modulate aggregation in patient-dependent manner, potentially undermining unoptimized SAAs preventing quantification. Methods In this study, we characterized inhibitory effect...

10.1186/s13024-023-00613-8 article EN cc-by Molecular Neurodegeneration 2023-04-01

Recent structural studies show distinct morphologies for the fibrils of Aβ(1-42) and Aβ(1-40), which are believed not to co-fibrillize. We describe here a novel, structurally-uniform 1 : mixed fibrillar species, differs from both pure fibrils. It forms preferentially even when Aβ(1-40) peptides in non-stoichiometric ratio.

10.1039/d0cc02463e article EN cc-by-nc Chemical Communications 2020-01-01

The aggregation of Aβ1-40 was monitored by solution NMR, which showed a trend complementary to the one observed ThT-fluorescence. NMR data support kinetic model where initially aggregates with reversible formation oligomeric species, then irreversibly convert into fibrils.

10.1039/c8cc01710g article EN Chemical Communications 2018-01-01

Abstract Many of the effects exerted on protein structure, stability, and dynamics by molecular crowding confinement in cellular environment can be mimicked encapsulation polymeric matrices. We have compared stability unfolding kinetics a highly fluorescent mutant Green Fluorescent Protein, GFPmut2, solution wet, nanoporous silica gels. In absence denaturant, does not induce any observable change circular dichroism fluorescence emission spectra GFPmut2. solution, induced guanidinium chloride...

10.1110/ps.041190805 article EN Protein Science 2005-04-01

α-Synuclein (α-syn) is found to be naturally present in biofluids such as cerebrospinal fluid (CSF) and serum. Human serum albumin (HSA) the most abundant protein these biofluids, which, beyond transporting hormones drugs, also exerts a chaperone-like activity binding other proteins blood inhibiting their aggregation. Contrasting results are reported literature about effects of on α-syn We characterized region HSA by high-field solution NMR spectroscopy effect aggregation thioflavin-T (ThT)...

10.1021/acs.jpcb.9b02381 article EN The Journal of Physical Chemistry B 2019-04-29

We have used a nanosecond pH-jump technique, coupled with simultaneous transient absorption and fluorescence emission detection, to characterize the dynamics of acid-induced spectral changes in GFPmut2 chromophore. Disappearance absorbance at 488 nm green occurs thermally activated, double exponential relaxation. To understand source two transients we introduced mutations amino acid residues that interact chromophore (H148G, T203V, E222Q). Results indicate faster is associated proton binding...

10.1021/ja045400r article EN Journal of the American Chemical Society 2004-12-02

Abstract Polyglutamylation is a reversible posttranslational modification that catalyzed by enzymes of the tubulin tyrosine ligase-like (TTLL) family. Here, we found TTLL11 generates previously unknown type polyglutamylation initiated addition glutamate residue to free C-terminal carboxyl group substrate protein. efficiently polyglutamylates Wnt signaling protein Dishevelled 3 (DVL3), thereby changing interactome DVL3. increases capacity DVL3 get phosphorylated, undergo phase separation, and...

10.1038/s44318-024-00254-7 article EN cc-by The EMBO Journal 2024-09-30

Multi-photon driven photo-switching between dark and bright (fluorescent) states of a green fluorescent protein (GFP) mutant is demonstrated. A single-protein investigation shows the existence two distinct that display sharp two-photon cross-section bands peaked at 780 nm 870 nm. Fluorescence these species can be independently switched on off. These results highlight new photoconversion pathway for photochromic GFPs have significant applications in multi-photon confocal microscopy optical...

10.1103/physreve.70.030901 article EN Physical Review E 2004-09-21

Abstract We report the two‐photon excitation and emission of a recently developed green fluorescent protein (GFP) mutant, E 2 GFP. Two main bands are found at 780 870 nm. Blinking irreversible reversible bleaching were observed. Fluorescence blinking occurs in millisecond range has been ascribed to conversions between neutral, anionic dark zwitterionic states. Bleaching is observed after approximately 10 4000 ms depending on power, it probably due conversion state. The striking feature this...

10.1002/cphc.200400318 article EN ChemPhysChem 2005-02-04

Abstract Green Fluorescent Protein (GFP) mutants are extensively used in optical microscopy studies of vivo biological processes cells. Nonetheless, blinking and bleaching the GFP chromophore at single molecule level greatly limits its usefulness. We have worked out what we think best experimental conditions for use mutant, GFP‐mut2, as a marker two‐photon excitation measurements. measured molecular brightness, excited state lifetime, photo‐bleaching times versus intensity on proteins...

10.1002/jemt.20125 article EN Microscopy Research and Technique 2004-11-01

Abstract Background: Aggregation of α-synuclein (α-syn) is a prominent feature Parkinson’s disease (PD) and other synucleinopathies. In these diseases, the extracellular spreading misfolded α-syn significantly contributes to cell-to-cell propagation misfolding pathology in prion-like fashion. Therefore, aggregates are considered primary targets both for diagnostics novel modifying therapies. Currently, seed amplification assays (SAAs) using cerebrospinal fluid (CSF) represent most promising...

10.21203/rs.3.rs-2001732/v1 preprint EN cc-by Research Square (Research Square) 2022-09-15
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