What is he best known for?
The fields of study he is best known for:
His primary areas of investigation include Biochemistry, Circular dichroism, Thioflavin, Analytical chemistry and Ultracentrifuge.
His Biochemistry study frequently draws connections between adjacent fields such as Biophysics.
His work deals with themes such as Phospholipid and Tetramer, which intersect with Circular dichroism.
The study incorporates disciplines such as Analytical Ultracentrifugation, Lamm equation, Sedimentation coefficient, Sedimentation equilibrium and Crystallography in addition to Analytical chemistry.
The Ultracentrifuge study which covers Size-exclusion chromatography that intersects with Chromatography, Sephadex, Epidermal growth factor receptor and Fluorescence anisotropy.
His research in Protein structure intersects with topics in Nuclear localization sequence and NLS.
His most cited work include:
- Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. (570 citations)
- Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II. (217 citations)
- C-Terminal Domain of the Membrane Copper Transporter Ctr1 from Saccharomyces cerevisiae Binds Four Cu(I) Ions as a Cuprous-Thiolate Polynuclear Cluster: Sub-femtomolar Cu(I) Affinity of Three Proteins Involved in Copper Trafficking (201 citations)
What are the main themes of his work throughout his whole career to date?
His primary scientific interests are in Biochemistry, Fibril, Protein structure, Biophysics and Crystallography.
His work in the fields of Apolipoprotein C-II, Apolipoprotein B, Phospholipid and Ultracentrifuge overlaps with other areas such as Micelle.
His work on Fibrillogenesis is typically connected to Thioflavin as part of general Fibril study, connecting several disciplines of science.
His Protein structure study combines topics from a wide range of disciplines, such as Protein aggregation, Protein secondary structure, Circular dichroism, Peptide and Amyloidosis.
His Biophysics research is multidisciplinary, incorporating perspectives in Macromolecule and Tetramer.
He focuses mostly in the field of Crystallography, narrowing it down to topics relating to Sedimentation equilibrium and, in certain cases, Binding site.
He most often published in these fields:
- Biochemistry (43.75%)
- Fibril (27.50%)
- Protein structure (25.00%)
What were the highlights of his more recent work (between 2009-2019)?
- Fibril (27.50%)
- Protein structure (25.00%)
- Biochemistry (43.75%)
In recent papers he was focusing on the following fields of study:
His primary areas of study are Fibril, Protein structure, Biochemistry, Protein folding and Biophysics.
He has researched Fibril in several fields, including Phospholipid, Nucleation, Crystallography, Molecular dynamics and Stereochemistry.
His Protein structure research is multidisciplinary, relying on both Protein aggregation, Tetramer, Protein secondary structure and Circular dichroism.
A large part of his Biochemistry studies is devoted to Apolipoprotein B.
His Protein folding study combines topics from a wide range of disciplines, such as Lamm equation, Worm-like chain, Ultracentrifuge and Dissociation constant.
His Biophysics study integrates concerns from other disciplines, such as Macromolecule, Apolipoprotein C-II and Bovine serum albumin.
Between 2009 and 2019, his most popular works were:
- Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I (76 citations)
- Apolipoproteins and amyloid fibril formation in atherosclerosis (50 citations)
- PcoE--a metal sponge expressed to the periplasm of copper resistance Escherichia coli. Implication of its function role in copper resistance. (46 citations)
In his most recent research, the most cited papers focused on:
Biochemistry, Fibril, Protein structure, Protein folding and P3 peptide are his primary areas of study.
Geoffrey J. Howlett combines Biochemistry and Thioflavin in his research.
His work deals with themes such as Crystallography, Circular dichroism, Protein aggregation and Protein secondary structure, which intersect with Protein structure.
The study incorporates disciplines such as Denticity, Periplasmic space, Escherichia coli and Metal ions in aqueous solution in addition to Crystallography.
His Protein aggregation study combines topics in areas such as Ultracentrifuge and Fluorophore.
His Protein folding research incorporates elements of Heat shock protein, Plasma protein binding, Biophysics, Apolipoprotein C2 and Amyloidosis.
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