What is he best known for?
The fields of study he is best known for:
- Enzyme
- Biochemistry
- Amino acid
Anthony L. Fink spends much of his time researching Biochemistry, Biophysics, Protein structure, Fibril and Circular dichroism.
His Biochemistry study frequently draws connections to other fields, such as Alpha-synuclein.
His Biophysics research includes themes of Crystallography, Amyloid fibril, Membrane and Protein folding.
His biological study spans a wide range of topics, including Immunoglobulin light chain, Ionic strength and Amyloidosis.
His work deals with themes such as Plasma protein binding, α synuclein, Human brain, Alzheimer's disease and Amyloid, which intersect with Protein structure.
Anthony L. Fink works mostly in the field of Circular dichroism, limiting it down to topics relating to Native state and, in certain cases, Denaturation, Guanidine, Acid–base titration, Congo red and Protein oligomerization.
His most cited work include:
- Why are "natively unfolded" proteins unstructured under physiologic conditions? (1640 citations)
- Protein aggregation: folding aggregates, inclusion bodies and amyloid (912 citations)
- Chaperone-Mediated Protein Folding (907 citations)
What are the main themes of his work throughout his whole career to date?
Anthony L. Fink focuses on Biochemistry, Crystallography, Biophysics, Circular dichroism and Fibril.
His studies in Biochemistry integrate themes in fields like Substantia nigra and Alpha-synuclein.
His Crystallography research focuses on subjects like Protein secondary structure, which are linked to Protein tertiary structure.
His study looks at the relationship between Biophysics and fields such as Intracellular, as well as how they intersect with chemical problems.
His research in Circular dichroism tackles topics such as Protein structure which are related to areas like Protein folding.
His Fibril research includes elements of Monomer, Oligomer, Immunoglobulin light chain, Amyloid and Amyloidosis.
He most often published in these fields:
- Biochemistry (35.27%)
- Crystallography (28.50%)
- Biophysics (26.57%)
What were the highlights of his more recent work (between 2004-2013)?
- Biochemistry (35.27%)
- Fibril (21.74%)
- Fibrillation (17.39%)
In recent papers he was focusing on the following fields of study:
His primary scientific interests are in Biochemistry, Fibril, Fibrillation, Biophysics and Alpha-synuclein.
Biochemistry is frequently linked to Parkinson's disease in his study.
His Fibril study incorporates themes from Crystallography, Circular dichroism, Thioflavin, Amyloid and Monomer.
Anthony L. Fink interconnects Polymerization and Phosphorylation in the investigation of issues within Biophysics.
His study in Alpha-synuclein is interdisciplinary in nature, drawing from both Nitration and Methionine.
The Protein structure study which covers Protein folding that intersects with Plasma protein binding.
Between 2004 and 2013, his most popular works were:
- Natively unfolded proteins. (621 citations)
- The Aggregation and Fibrillation of α-Synuclein (334 citations)
- The oxidation state of DJ-1 regulates its chaperone activity toward α-synuclein (288 citations)
In his most recent research, the most cited papers focused on:
- Enzyme
- Amino acid
- Biochemistry
His primary areas of investigation include Biochemistry, Fibril, Protein structure, Fibrillation and Oxidative stress.
Biochemistry is closely attributed to Alpha-synuclein in his work.
His Fibril study also includes
- Monomer that intertwine with fields like Oligomer and Amyloid,
- Quenching that connect with fields like Crystallography.
As part of his studies on Protein structure, Anthony L. Fink often connects relevant subjects like Protein folding.
He has included themes like Plasma protein binding, Intrinsically disordered proteins and Thioflavin in his Protein folding study.
His research in Biophysics intersects with topics in Lipid raft, α synuclein and Point mutation.
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