What is he best known for?
The fields of study he is best known for:
Robert B. Freedman spends much of his time researching Biochemistry, Protein disulfide-isomerase, Stereochemistry, Enzyme and Isomerase.
Biochemistry connects with themes related to Molecular biology in his study.
His studies deal with areas such as Protein structure, Thioredoxin, Protein folding and Active site as well as Protein disulfide-isomerase.
His research in Stereochemistry intersects with topics in Matrix metalloproteinase, Catalysis and Binding site.
In his research on the topic of Enzyme, Protein disulphide-isomerase and Disulphide bond formation is strongly related with Secretory protein.
His Isomerase course of study focuses on Substrate and Heptane, Thioredoxin fold, Wild type, Heteronuclear single quantum coherence spectroscopy and Enzyme assay.
His most cited work include:
- Protein disulphide isomerase: building bridges in protein folding (633 citations)
- Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteins (417 citations)
- Genomic Dissection of Bipolar Disorder and Schizophrenia, Including 28 Subphenotypes (328 citations)
What are the main themes of his work throughout his whole career to date?
Robert B. Freedman mainly focuses on Biochemistry, Protein disulfide-isomerase, Protein folding, Endoplasmic reticulum and Enzyme.
Many of his studies on Biochemistry involve topics that are commonly interrelated, such as Molecular biology.
His Protein disulfide-isomerase research includes themes of Thioredoxin, Glutathione, Stereochemistry and Active site.
His work in Protein folding covers topics such as In vitro which are related to areas like Protein biosynthesis.
His research investigates the connection between Microsome and topics such as Chromatography that intersect with issues in Isoelectric focusing and Microemulsion.
His study in Recombinant DNA is interdisciplinary in nature, drawing from both Cell culture and Yeast.
He most often published in these fields:
- Biochemistry (59.35%)
- Protein disulfide-isomerase (24.39%)
- Protein folding (16.26%)
What were the highlights of his more recent work (between 2007-2019)?
- Biochemistry (59.35%)
- Protein folding (16.26%)
- Protein disulfide-isomerase (24.39%)
In recent papers he was focusing on the following fields of study:
His main research concerns Biochemistry, Protein folding, Protein disulfide-isomerase, Crystallography and Folding.
Biochemistry is a component of his Periplasmic space, Twin-arginine translocation pathway, Enzyme, Cofactor and Tryptophan studies.
Robert B. Freedman interconnects Protein structure, Thioredoxin, Stereochemistry and Protein–protein interaction in the investigation of issues within Protein folding.
Robert B. Freedman has researched Protein structure in several fields, including Isomerase, Hydrophobic effect and Binding site.
His Protein disulfide-isomerase research is classified as research in Endoplasmic reticulum.
As a part of the same scientific family, he mostly works in the field of Crystallography, focusing on Thioredoxin fold and, on occasion, Heteronuclear single quantum coherence spectroscopy, Wild type and Substrate.
Between 2007 and 2019, his most popular works were:
- Genomic Dissection of Bipolar Disorder and Schizophrenia, Including 28 Subphenotypes (328 citations)
- Genomic Relationships, Novel Loci, and Pleiotropic Mechanisms across Eight Psychiatric Disorders (242 citations)
- Reconstitution of human Ero1-L alpha/protein-disulfide isomerase oxidative folding pathway in vitro: position-dependent differences in role between the a and a' domains of protein-disulfide isomerase (113 citations)
In his most recent research, the most cited papers focused on:
Biochemistry, Protein folding, Protein disulfide-isomerase, Protein structure and Crystallography are his primary areas of study.
His works in Signal peptide, Periplasmic space, Twin-arginine translocation pathway, Membrane transport protein and Escherichia coli are all subjects of inquiry into Biochemistry.
The concepts of his Protein disulfide-isomerase study are interwoven with issues in Folding, Protein domain and Biophysics.
His Protein domain course of study focuses on Saccharomyces cerevisiae and Endoplasmic reticulum.
His Protein structure research incorporates themes from Isomerase and Binding site.
Robert B. Freedman focuses mostly in the field of Binding site, narrowing it down to matters related to Stereochemistry and, in some cases, Thioredoxin fold and Substrate.
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