What is he best known for?
The fields of study he is best known for:
His primary scientific interests are in Cell biology, Biochemistry, Phosphorylation, Tau protein and Molecular biology.
His Cell biology research incorporates elements of Epitope, Neurite and Nervous system.
The Phosphorylation study combines topics in areas such as Tyrosine, Microtubule and Transfection.
As part of his inquiry into Pathology and Alzheimer's disease, Brian H. Anderton is doing Tau protein research.
His studies in Pathology integrate themes in fields like Cytoplasm, Ubiquitin and Neuroscience.
Brian H. Anderton focuses mostly in the field of Molecular biology, narrowing it down to topics relating to Tyrosine phosphorylation and, in certain cases, Receptor tyrosine kinase, PTK2 and Protein tyrosine phosphatase.
His most cited work include:
- Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase. (611 citations)
- Tau phosphorylation: the therapeutic challenge for neurodegenerative disease (599 citations)
- All classes of intermediate filaments share a common antigenic determinant defined by a monoclonal antibody (532 citations)
What are the main themes of his work throughout his whole career to date?
His main research concerns Cell biology, Pathology, Biochemistry, Neurofilament and Phosphorylation.
His work carried out in the field of Cell biology brings together such families of science as Neurodegeneration and Cytoskeleton.
His work is connected to GSK-3, Protein kinase A and Glycogen synthase, as a part of Biochemistry.
His Neurofilament research integrates issues from Protein filament, Immunostaining, Molecular biology and Antibody, Monoclonal antibody.
His Phosphorylation research incorporates themes from Tyrosine, Tau protein and Kinase.
The study incorporates disciplines such as Progressive supranuclear palsy, Tyrosine kinase, Neuroscience, Tauopathy and Gene isoform in addition to Tau protein.
He most often published in these fields:
- Cell biology (32.19%)
- Pathology (23.29%)
- Biochemistry (22.60%)
What were the highlights of his more recent work (between 2003-2016)?
- Cell biology (32.19%)
- Tau protein (16.78%)
- Biochemistry (22.60%)
In recent papers he was focusing on the following fields of study:
Brian H. Anderton mainly focuses on Cell biology, Tau protein, Biochemistry, Phosphorylation and GSK-3.
The various areas that Brian H. Anderton examines in his Cell biology study include Cleavage and Transcription, Gene.
Within the field of Pathology and Alzheimer's disease Brian H. Anderton studies Tau protein.
Brian H. Anderton interconnects Neurofilament and Mass spectrometry in the investigation of issues within Biochemistry.
His Phosphorylation study often links to related topics such as Tyrosine.
His GSK-3 research includes elements of Glycogen synthase and MAP2K7.
Between 2003 and 2016, his most popular works were:
- Tau phosphorylation: the therapeutic challenge for neurodegenerative disease (599 citations)
- Novel Phosphorylation Sites in Tau from Alzheimer Brain Support a Role for Casein Kinase 1 in Disease Pathogenesis (304 citations)
- Glycogen synthase kinase-3 inhibition is integral to long-term potentiation. (272 citations)
In his most recent research, the most cited papers focused on:
His primary areas of investigation include Phosphorylation, Tau protein, Cell biology, Axoplasmic transport and Biochemistry.
His biological study spans a wide range of topics, including Molecular biology and Tyrosine.
His Tau protein research is multidisciplinary, incorporating elements of Genetically modified mouse, Neuroscience and Tauopathy.
His Neuroscience study combines topics from a wide range of disciplines, such as Tau phosphorylation, Tau pathology and Disease, Pathology.
The concepts of his Cell biology study are interwoven with issues in Alzheimer's disease, Neurofilament and Neurodegeneration.
His study in Hippocampal formation is interdisciplinary in nature, drawing from both Glycogen synthase and GSK-3.
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