His primary areas of investigation include Serpin, Biochemistry, Protein structure, Antithrombin and Stereochemistry. His Serpin research integrates issues from Cleavage, Protease, Neuroserpin, Familial encephalopathy with neuroserpin inclusion bodies and Conformational change. His Conformational change research incorporates themes from Proteases, Subtilisin and Binding site.
His research in Biochemistry intersects with topics in Plasminogen activator and Fibrinolysis. His work deals with themes such as Coagulopathy, Cohort study and Cohort, which intersect with Antithrombin. His study looks at the relationship between Stereochemistry and topics such as Reactive center, which overlap with Heparin, Protein folding, Chymotrypsin and Guanidinium chloride.
The scientist’s investigation covers issues in Biochemistry, Antithrombin, Serpin, Heparin and Protein structure. His study connects Molecular biology and Biochemistry. In his research on the topic of Antithrombin, Coagulopathy is strongly related with Immunology.
Robin W. Carrell has researched Serpin in several fields, including Cleavage, Biophysics, Conformational change, Stereochemistry and Protease. His studies deal with areas such as Glycosaminoglycan and Binding site as well as Heparin. In his study, which falls under the umbrella issue of Protein structure, Inclusion bodies is strongly linked to Neuroserpin.
His main research concerns Serpin, Biophysics, Renin–angiotensin system, Biochemistry and Endocrinology. His Serpin research focuses on Reactive center in particular. Robin W. Carrell interconnects Protease, Antithrombin and Binding site in the investigation of issues within Biophysics.
His work carried out in the field of Binding site brings together such families of science as Docking and Heparin. His study in Biochemistry is interdisciplinary in nature, drawing from both Alzheimer's disease, Toxicity and Amyloid. His research investigates the link between Peptide and topics such as Stereochemistry that cross with problems in Protein folding, Small molecule and Crystallography.
His scientific interests lie mostly in Biochemistry, Biophysics, Protein structure, Serpin and Plasma protein binding. Specifically, his work in Biochemistry is concerned with the study of Binding site. The Binding site study combines topics in areas such as Reactive center and Allosteric regulation.
Within one scientific family, Robin W. Carrell focuses on topics pertaining to Protease under Protein structure, and may sometimes address concerns connected to Hydrophobic effect. His work in Serpin is not limited to one particular discipline; it also encompasses Cleavage. His research in Plasma protein binding tackles topics such as Conformational change which are related to areas like Proteases, Glycosylation, Globulin and Neutrophil elastase.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
The serpins are an expanding superfamily of structurally similar but functionally diverse proteins - Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
Gary A. Silverman;Phillip I. Bird;Robin W. Carrell;Frank C. Church.
Journal of Biological Chemistry (2001)
Structure of a serpin–protease complex shows inhibition by deformation
James A. Huntington;Randy J. Read;Robin W. Carrell.
Nature (2000)
The mechanism of Z alpha 1-antitrypsin accumulation in the liver.
D A Lomas;D L Evans;J T Finch;R W Carrell.
Nature (1992)
The anticoagulant activation of antithrombin by heparin.
Lei Jin;Jan Pieter Abrahams;Jan Pieter Abrahams;Richard Skinner;Maurice Petitou.
Proceedings of the National Academy of Sciences of the United States of America (1997)
Mutation of antitrypsin to antithrombin. alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder.
Maurice C. Owen;Stephen O. Brennan;Jessica H. Lewis;Robin W. Carrell.
The New England Journal of Medicine (1983)
What do dysfunctional serpins tell us about molecular mobility and disease
Penelope E. Stein;Robin W. Carrell.
Nature Structural & Molecular Biology (1995)
Crystal structure of uncleaved ovalbumin at 1.95 A resolution.
Penelope E. Stein;Andrew G.W. Leslie;John T. Finch;Robin W. Carrell.
Journal of Molecular Biology (1991)
Crystal structure of ovalbumin as a model for the reactive centre of serpins.
Penelope E. Stein;Andrew G. W. Leslie;John T. Finch;William G. Turnell.
Nature (1990)
Alpha1-antitrypsin deficiency--a model for conformational diseases.
Robin W Carrell;David A Lomas.
The New England Journal of Medicine (2002)
Biological implications of a 3 å structure of dimeric antithrombin
Robin W Carrell;Penelope E Stein;Giulio Fermi;Mark R Wardell.
Structure (1994)
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