What is she best known for?
The fields of study she is best known for:
Helen R. Saibil mostly deals with Protein folding, Biochemistry, Biophysics, Protein structure and Chaperone.
In her research, Cytosol is intimately related to Thermosome, which falls under the overarching field of Protein folding.
Her Biochemistry study frequently involves adjacent topics like In vivo.
Helen R. Saibil studied Biophysics and Membrane that intersect with Cholesterol-dependent cytolysin, Crystallography and Electron microscope.
The concepts of her Protein structure study are interwoven with issues in Cellular compartment, Protein tertiary structure, HSP27 Heat-Shock Proteins and HSP60.
Her Chaperone study combines topics from a wide range of disciplines, such as Nucleotide exchange factor, Structural biology, Hsp33 and Protein aggregation.
Her most cited work include:
- The protofilament structure of insulin amyloid fibrils (691 citations)
- A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. (676 citations)
- Chaperone machines for protein folding, unfolding and disaggregation (545 citations)
What are the main themes of her work throughout her whole career to date?
Her primary areas of investigation include Biophysics, Biochemistry, Chaperonin, Protein folding and Cell biology.
Her Biophysics research integrates issues from Electron microscope, Membrane and Protein structure.
She is studying Fibril, which is a component of Biochemistry.
Her Chaperonin study deals with GroEL intersecting with Crystallography.
Her studies deal with areas such as Plasma protein binding and Chaperone as well as Protein folding.
Her biological study deals with issues like MACPF, which deal with fields such as Transmembrane protein.
She most often published in these fields:
- Biophysics (39.27%)
- Biochemistry (24.61%)
- Chaperonin (20.42%)
What were the highlights of her more recent work (between 2012-2021)?
- Biophysics (39.27%)
- Cell biology (19.90%)
- Chaperone (13.61%)
In recent papers she was focusing on the following fields of study:
Helen R. Saibil mainly focuses on Biophysics, Cell biology, Chaperone, Protein folding and Biological sciences.
The various areas that Helen R. Saibil examines in her Biophysics study include Beta and Cooperativity.
Her work in Cooperativity addresses subjects such as Allosteric regulation, which are connected to disciplines such as ATP hydrolysis and Crystallography.
Her Cell biology study incorporates themes from Perforin, Plasmodium falciparum, Cytoskeleton and Cell membrane.
Chaperone is a subfield of Biochemistry that Helen R. Saibil studies.
Her Protein folding research is multidisciplinary, incorporating elements of Protein structure, Native state and GroEL.
Between 2012 and 2021, her most popular works were:
- Chaperone machines for protein folding, unfolding and disaggregation (545 citations)
- Atomic structure and hierarchical assembly of a cross-β amyloid fibril (340 citations)
- Human Hsp70 Disaggregase Reverses Parkinson’s-Linked α-Synuclein Amyloid Fibrils (186 citations)
In her most recent research, the most cited papers focused on:
Helen R. Saibil focuses on Biophysics, Cell biology, Cell membrane, Chaperone and Biochemistry.
Her Biophysics research includes elements of Huntingtin Protein, Saccharomyces cerevisiae, Bioinformatics, Protein folding and HEK 293 cells.
Her Protein folding study combines topics in areas such as Cooperativity, ATP hydrolysis, Co-chaperone, Structural biology and Protein structure.
Her Cell biology research incorporates themes from Plasmodium falciparum, MACPF, Cytoskeleton and Cholesterol-dependent cytolysin.
The study incorporates disciplines such as Cytotoxic T cell, Exocytosis and Granzyme in addition to Cell membrane.
Her work deals with themes such as Protein aggregation, Fibril, CLPB, Hsp70 and Intracellular, which intersect with Chaperone.
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