What is he best known for?
The fields of study he is best known for:
His primary areas of investigation include Flagellum, Crystallography, Cell biology, Biophysics and Protein filament.
His work carried out in the field of Flagellum brings together such families of science as ATPase, Protein subunit, Chemiosmosis and Cytoplasm.
His Crystallography research is multidisciplinary, incorporating perspectives in Fiber diffraction, Flagellar filament, Core and Cryo-electron microscopy.
Keiichi Namba has included themes like Type three secretion system, Virulence and Flik in his Cell biology study.
His Biophysics study combines topics from a wide range of disciplines, such as Mechanism, Protein structure, Biochemistry, Stator and Rotor.
His biological study spans a wide range of topics, including DNA, Antiparallel and Flagellin.
His most cited work include:
- Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. (599 citations)
- Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. (407 citations)
- Visualization of protein-nucleic acid interactions in a virus. Refined structure of intact tobacco mosaic virus at 2.9 A resolution by X-ray fiber diffraction. (371 citations)
What are the main themes of his work throughout his whole career to date?
The scientist’s investigation covers issues in Biophysics, Flagellum, Cell biology, Crystallography and Protein filament.
In Biophysics, he works on issues like Stator, which are connected to Rotor and Torque.
The Flagellum study combines topics in areas such as Transport protein, Cytoplasm and Protein structure.
His Cell biology research includes themes of ATPase, Mutant, Flagellar protein and Salmonella.
His Crystallography research is multidisciplinary, incorporating elements of Fiber diffraction, X-ray crystallography and Crystallization.
His studies deal with areas such as Protein subunit, Hook and Flagellin as well as Protein filament.
He most often published in these fields:
- Biophysics (40.42%)
- Flagellum (33.92%)
- Cell biology (29.70%)
What were the highlights of his more recent work (between 2016-2021)?
- Biophysics (40.42%)
- Flagellum (33.92%)
- Protein filament (19.33%)
In recent papers he was focusing on the following fields of study:
His primary scientific interests are in Biophysics, Flagellum, Protein filament, Cytoplasm and Cell biology.
He works in the field of Biophysics, focusing on Cryo-electron microscopy in particular.
Keiichi Namba has researched Flagellum in several fields, including Transport protein, Type three secretion system, Flagellin and Organelle.
Keiichi Namba combines subjects such as Protein structure and Plasma protein binding with his study of Transport protein.
The various areas that Keiichi Namba examines in his Protein filament study include Hook, Protein subunit, Motor protein, Resolution and Actin.
His research integrates issues of ATPase, Mutant, Transmembrane protein, Chemiosmosis and Conformational change in his study of Cytoplasm.
Between 2016 and 2021, his most popular works were:
- Bacterial flagella grow through an injection-diffusion mechanism. (44 citations)
- Bacterial flagella grow through an injection-diffusion mechanism. (44 citations)
- Identical folds used for distinct mechanical functions of the bacterial flagellar rod and hook (41 citations)
In his most recent research, the most cited papers focused on:
His main research concerns Biophysics, Flagellum, Protein filament, Cytoplasm and Basal body.
His Biophysics research is multidisciplinary, incorporating perspectives in Flexibility, Microbiology, Transmembrane protein, Universal joint and Stator.
His Flagellum research incorporates elements of Transport protein and Flagellin.
The various areas that he examines in his Protein filament study include Motor protein, Organelle, Muscle contraction and Hook.
His Cytoplasm study integrates concerns from other disciplines, such as Periplasmic space, ATPase and Mutant.
Keiichi Namba combines subjects such as Chemiosmosis and Cell biology with his study of ATPase.
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