What is she best known for?
The fields of study she is best known for:
Michele Vendruscolo mostly deals with Protein structure, Protein folding, Protein aggregation, Biophysics and Biochemistry.
Her Protein structure study combines topics from a wide range of disciplines, such as Crystallography, Chemical shift, Protein secondary structure and Molecular dynamics.
Her Crystallography research includes themes of Nuclear magnetic resonance spectroscopy and Phi value analysis.
Her Protein folding research integrates issues from Folding, Structural biology, Computational biology and Threading.
The various areas that Michele Vendruscolo examines in her Protein aggregation study include Amyloid fibril, Amyloid, In vitro and Peptide.
Michele Vendruscolo has researched Biophysics in several fields, including Membrane, Lipid bilayer, Plasma protein binding and Nucleation.
Her most cited work include:
- The amyloid state and its association with protein misfolding diseases. (1240 citations)
- An analytical solution to the kinetics of breakable filament assembly (750 citations)
- Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism (727 citations)
What are the main themes of her work throughout her whole career to date?
The scientist’s investigation covers issues in Biophysics, Protein folding, Protein structure, Protein aggregation and Molecular dynamics.
She focuses mostly in the field of Biophysics, narrowing it down to topics relating to Biochemistry and, in certain cases, Alpha-synuclein.
Her Protein folding study integrates concerns from other disciplines, such as Folding, Computational biology, Ribosome and Transition state.
Her work deals with themes such as Computational chemistry and Biological system, which intersect with Protein structure.
The concepts of her Protein aggregation study are interwoven with issues in Proteome, In vitro, Neurodegeneration and Drug discovery.
Her research on Molecular dynamics also deals with topics like
- Chemical physics, which have a strong connection to Molecule,
- Crystallography which connect with Nuclear magnetic resonance spectroscopy.
She most often published in these fields:
- Biophysics (27.65%)
- Protein folding (22.67%)
- Protein structure (19.29%)
What were the highlights of her more recent work (between 2018-2021)?
- Biophysics (27.65%)
- Protein aggregation (19.13%)
- Amyloid (9.81%)
In recent papers she was focusing on the following fields of study:
Her primary areas of study are Biophysics, Protein aggregation, Amyloid, Protein folding and In vitro.
Her Biophysics study combines topics in areas such as Membrane, Lipid bilayer, Small molecule, Peptide and Monomer.
Her Protein aggregation study improves the overall literature in Cell biology.
Her Amyloid research incorporates themes from α synuclein, Kinetics and Nucleation.
Her Protein folding research is multidisciplinary, incorporating elements of Protein structure, Disease and Synucleinopathies.
In vitro is a subfield of Biochemistry that Michele Vendruscolo studies.
Between 2018 and 2021, her most popular works were:
- RNA Granules Hitchhike on Lysosomes for Long-Distance Transport, Using Annexin A11 as a Molecular Tether. (111 citations)
- Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms (96 citations)
- Effects of alpha-tubulin acetylation on microtubule structure and stability. (77 citations)
In her most recent research, the most cited papers focused on:
Protein aggregation, Biophysics, Protein folding, Cell biology and Peptide are her primary areas of study.
Her Protein aggregation research incorporates elements of Proteome, Caenorhabditis elegans, Toxicity and Protein Homeostasis.
She is interested in Fibril, which is a branch of Biophysics.
Her Protein folding study incorporates themes from Protein structure, Epitope and Computational biology.
Her work in Protein structure tackles topics such as Protein sequencing which are related to areas like Plasma protein binding.
Michele Vendruscolo has included themes like Mechanism of action, Oligomer, Small molecule, Structure–activity relationship and Monomer in her Peptide study.
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