What is he best known for?
The fields of study he is best known for:
His primary scientific interests are in Protein structure, Biochemistry, Biophysics, Binding site and Stereochemistry.
His Protein structure research integrates issues from Amino acid, Peptide sequence and GTPase, Cell biology.
His work on Maltose, Gene, Trehalose and Enzyme is typically connected to Mycolic acid as part of general Biochemistry study, connecting several disciplines of science.
His Biophysics study integrates concerns from other disciplines, such as Chromatin, DNA, Recombinant DNA and SH3 domain.
His Binding site research focuses on subjects like Plasma protein binding, which are linked to Receptor tyrosine kinase, Receptor and Tyrosine phosphorylation.
His biological study spans a wide range of topics, including Protein tertiary structure, Snake venom and Protein secondary structure.
His most cited work include:
- Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase. (503 citations)
- Solution structure of a DNA-binding domain from HMG1 (226 citations)
- Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 A resolution. (170 citations)
What are the main themes of his work throughout his whole career to date?
Paul C. Driscoll focuses on Protein structure, Biochemistry, Stereochemistry, Crystallography and Binding site.
The concepts of his Protein structure study are interwoven with issues in Protein secondary structure, Biophysics, Structural biology, Peptide sequence and Nuclear magnetic resonance spectroscopy.
His research on Biochemistry often connects related areas such as Cell biology.
His study in the fields of Heteronuclear single quantum coherence spectroscopy under the domain of Stereochemistry overlaps with other disciplines such as Monomer.
His Crystallography study combines topics in areas such as Peptide binding, Protein subunit, Two-dimensional nuclear magnetic resonance spectroscopy and Proto-oncogene tyrosine-protein kinase Src.
His Binding site study incorporates themes from SH2 domain, Tyrosine phosphorylation, Conformational change and Ligand.
He most often published in these fields:
- Protein structure (50.43%)
- Biochemistry (46.96%)
- Stereochemistry (33.04%)
What were the highlights of his more recent work (between 2006-2010)?
- Biochemistry (46.96%)
- Protein structure (50.43%)
- Genetics (16.52%)
In recent papers he was focusing on the following fields of study:
His scientific interests lie mostly in Biochemistry, Protein structure, Genetics, Biophysics and Plasma protein binding.
His research in Protein structure intersects with topics in Glutathione peroxidase, Glutathione, Nuclear magnetic resonance spectroscopy, Dysferlin and Membrane protein.
In general Genetics, his work in Gene and Multiple sequence alignment is often linked to INSRR, Insulin resistance and Insulin-like growth factor 1 receptor linking many areas of study.
He interconnects Heteronuclear single quantum coherence spectroscopy, Nuclear Overhauser effect, Helix, Cell activation and Pichia pastoris in the investigation of issues within Biophysics.
His Plasma protein binding research incorporates elements of Conformational change and Binding site.
His Pleckstrin homology domain research includes themes of GTPase and Phospholipase C.
Between 2006 and 2010, his most popular works were:
- Clustering of Genetically Defined Allele Classes in the Caenorhabditis elegans DAF-2 Insulin/IGF-1 Receptor (73 citations)
- Clustering of Genetically Defined Allele Classes in the Caenorhabditis elegans DAF-2 Insulin/IGF-1 Receptor (73 citations)
- Characterization of phospholipase C gamma enzymes with gain-of-function mutations (47 citations)
In his most recent research, the most cited papers focused on:
Paul C. Driscoll mainly investigates Biochemistry, Mutation, Pleckstrin homology domain, Phospholipase C gamma and Genetics.
Membrane protein, Protein structure, Bacterial outer membrane, Peptide sequence and Structural biology are the subjects of his Biochemistry studies.
His Mutation research includes elements of Isozyme, Enzyme and Phosphorylation.
The various areas that he examines in his Pleckstrin homology domain study include Plasma protein binding, GTPase and Phospholipase C.
His Phospholipase C gamma study deals with the bigger picture of Cell biology.
His Caenorhabditis elegans research is multidisciplinary, relying on both Sequence analysis and Null allele.
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