University College London
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.
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.
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.
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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Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase.
K Salim;M J Bottomley;E Querfurth;M J Zvelebil.
The EMBO Journal (1996)
Solution structure of a DNA-binding domain from HMG1.
Christopher M. Read;Peter D. Cary;Colyn Crane-Robinson;Paul C. Driscoll.
Nucleic Acids Research (1993)
The phosphatidylinositol 3-phosphate-binding FYVE finger
Harald Alfred Stenmark;Rein Aasland;Paul C. Driscoll.
FEBS Letters (2002)
Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 A resolution.
E. Y. Jones;K. Harlos;M. J. Bottomley;R. C. Robinson.
Solution structure and ligand-binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3-kinase
Grant W. Booker;Ivan Gout;A. Kristina^Downing;Paul C. Driscoll.
Structure of domain 1 of rat T lymphocyte CD2 antigen
Paul C. Driscoll;Jason G. Cyster;Iain D. Campbell;Alan F. Williams.
Human epidermal growth factor: High resolution solution structure and comparison with human transforming growth factor α
Ulrich Hommel;Timothy S. Harvey;Paul C. Driscoll;Iain D. Campbell.
Journal of Molecular Biology (1992)
H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein.
Diego Esposito;Arsen Petrovic;Richard Harris;Shusuke Ono.
Journal of Molecular Biology (2002)
Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins.
B Kieffer;P C Driscoll;I D Campbell;A C Willis.
Characterization of a Bicyclic Peptide Neuropilin-1 (NP-1) Antagonist (EG3287) Reveals Importance of Vascular Endothelial Growth Factor Exon 8 for NP-1 Binding and Role of NP-1 in KDR Signaling
Haiyan Jia;Azadeh Bagherzadeh;Basil Hartzoulakis;Ashley Jarvis.
Journal of Biological Chemistry (2006)
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