What is he best known for?
The fields of study he is best known for:
Fabrizio Chiti mainly focuses on Protein folding, Biochemistry, Protein aggregation, Protein structure and Acylphosphatase.
His Protein folding research is multidisciplinary, incorporating elements of Oligomer and Sequence.
He has researched Biochemistry in several fields, including Amyloid disease and Amyloid.
His Protein aggregation research entails a greater understanding of Cell biology.
Fabrizio Chiti usually deals with Protein structure and limits it to topics linked to Biophysics and Hydrogen bond.
Fabrizio Chiti combines subjects such as Protein secondary structure, Mutation, Mutational analysis, Procarboxypeptidase A2 and Phi value analysis with his study of Acylphosphatase.
His most cited work include:
- Protein Misfolding, Functional Amyloid, and Human Disease (4716 citations)
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. (2076 citations)
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. (2076 citations)
What are the main themes of his work throughout his whole career to date?
His scientific interests lie mostly in Biochemistry, Protein folding, Protein aggregation, Biophysics and Amyloid.
In the subject of general Biochemistry, his work in Acylphosphatase, Peptide, Peptide sequence and Enzyme is often linked to Amyloidosis, thereby combining diverse domains of study.
His work deals with themes such as Protein structure, Crystallography, Circular dichroism and Protein secondary structure, which intersect with Protein folding.
His Protein aggregation study is concerned with the larger field of Cell biology.
His Biophysics research includes elements of Mutation, Oligomer, Membrane, Toxicity and Cytotoxicity.
His work on Amyloid disease as part of general Amyloid study is frequently linked to Congo red, bridging the gap between disciplines.
He most often published in these fields:
- Biochemistry (44.67%)
- Protein folding (43.65%)
- Protein aggregation (36.04%)
What were the highlights of his more recent work (between 2015-2021)?
- Biophysics (34.01%)
- Protein aggregation (36.04%)
- Protein folding (43.65%)
In recent papers he was focusing on the following fields of study:
The scientist’s investigation covers issues in Biophysics, Protein aggregation, Protein folding, Amyloid and Biochemistry.
His study in Biophysics is interdisciplinary in nature, drawing from both Oligomer, Membrane, Cell membrane, Toxicity and Cytotoxicity.
Cell biology covers Fabrizio Chiti research in Protein aggregation.
Fabrizio Chiti has included themes like Protein structure, Mutant, Protein secondary structure and Thioflavin in his Protein folding study.
Fabrizio Chiti interconnects Alzheimer's disease, Human disease, Computational biology and Stereochemistry in the investigation of issues within Protein structure.
His Amyloid research is multidisciplinary, relying on both Biomolecule, Peptide sequence and Cell integrity.
Between 2015 and 2021, his most popular works were:
- Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade (873 citations)
- Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers (223 citations)
- A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity. (125 citations)
In his most recent research, the most cited papers focused on:
His main research concerns Protein aggregation, Neurodegeneration, Biochemistry, Cell biology and Protein folding.
His research in Protein aggregation intersects with topics in Biophysics, Alpha-synuclein and Cytotoxicity.
His studies deal with areas such as Inclusion bodies and Cytoplasm, Cytoplasmic inclusion, Cell nucleus as well as Neurodegeneration.
His Biochemistry study frequently draws connections to other fields, such as Amyloid.
His Cell biology research is multidisciplinary, incorporating perspectives in Squalamine and In vivo.
His Protein folding research incorporates themes from Alzheimer's disease, Human disease and Computational biology.
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