What is he best known for?
The fields of study he is best known for:
- Gene
- Enzyme
- Phosphorylation
His primary scientific interests are in Rho-associated protein kinase, Cell biology, Myosin light-chain kinase, Molecular biology and Myosin.
His Rho-associated protein kinase research incorporates themes from MAP kinase kinase kinase and Mitogen-activated protein kinase kinase.
He combines topics linked to Lysophosphatidic acid with his work on Cell biology.
He is interested in Myosin-light-chain phosphatase, which is a field of Myosin light-chain kinase.
His Molecular biology research is multidisciplinary, incorporating perspectives in RHOA and Protein kinase A.
His Myosin phosphatase activity study, which is part of a larger body of work in Myosin, is frequently linked to Smooth muscle contraction, bridging the gap between disciplines.
His most cited work include:
- Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase) (2500 citations)
- Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). (1726 citations)
- Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase. (1005 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of study are Cell biology, Rho-associated protein kinase, Phosphorylation, Kinase and Protein kinase A.
As a part of the same scientific family, Mutsuki Amano mostly works in the field of Cell biology, focusing on Neurite and, on occasion, Cellular differentiation and Axon.
He has included themes like Molecular biology, Myosin light-chain kinase, Small GTPase and Focal adhesion in his Rho-associated protein kinase study.
His Myosin light-chain kinase study improves the overall literature in Myosin.
The Myosin phosphatase activity research Mutsuki Amano does as part of his general Myosin study is frequently linked to other disciplines of science, such as Myosin ATPase, therefore creating a link between diverse domains of science.
His research integrates issues of Proteomics and Phosphoprotein in his study of Kinase.
He most often published in these fields:
- Cell biology (64.15%)
- Rho-associated protein kinase (50.00%)
- Phosphorylation (32.08%)
What were the highlights of his more recent work (between 2017-2021)?
- Cell biology (64.15%)
- Phosphorylation (32.08%)
- Kinase (27.36%)
In recent papers he was focusing on the following fields of study:
His primary areas of investigation include Cell biology, Phosphorylation, Kinase, MAPK/ERK pathway and Medium spiny neuron.
His Cell biology research incorporates elements of Neurite, Dopamine and Transcription factor.
His Phosphorylation research focuses on Protein phosphorylation in particular.
His research investigates the link between Kinase and topics such as Signal transduction that cross with problems in Phosphorylation sites, Intrinsically disordered proteins, Phosphoprotein and Neural development.
The study incorporates disciplines such as Dopamine receptor, Dopaminergic and Related gene in addition to MAPK/ERK pathway.
His study in Medium spiny neuron is interdisciplinary in nature, drawing from both Rap1 and CREB.
Between 2017 and 2021, his most popular works were:
- Pathological Progression Induced by the Frontotemporal Dementia-Associated R406W Tau Mutation in Patient-Derived iPSCs (16 citations)
- Targeting Tyro3 ameliorates a model of PGRN-mutant FTLD-TDP via tau-mediated synaptic pathology. (11 citations)
- Phosphorylation of Npas4 by MAPK Regulates Reward-Related Gene Expression and Behaviors. (9 citations)
In his most recent research, the most cited papers focused on:
- Gene
- Enzyme
- Phosphorylation
Mutsuki Amano focuses on Cell biology, Medium spiny neuron, Missense mutation, Cancer research and Tau protein.
In his articles, he combines various disciplines, including Cell biology and Eticlopride.
He combines subjects such as Adenosine, CREB, Cyclic AMP Response Element-Binding Protein and MAPK/ERK pathway with his study of Medium spiny neuron.
His research in Missense mutation intersects with topics in Calpain and Mutant.
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