K
Kazuaki Homma
Researcher at Northwestern University
Publications - 52
Citations - 2008
Kazuaki Homma is an academic researcher from Northwestern University. The author has contributed to research in topics: Myosin & Prestin. The author has an hindex of 21, co-authored 46 publications receiving 1768 citations. Previous affiliations of Kazuaki Homma include University of Texas Health Science Center at Tyler & University of Massachusetts Medical School.
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Journal ArticleDOI
Infrared light excites cells by changing their electrical capacitance
Mikhail G. Shapiro,Kazuaki Homma,Sebastian Villarreal,Claus Peter Richter,Francisco Bezanilla +4 more
TL;DR: It is shown that infrared light excites cells through a novel, highly general electrostatic mechanism that reversibly alters the electrical capacitance of the plasma membrane, depolarizing the target cell.
Journal ArticleDOI
Class VI myosin moves processively along actin filaments backward with large steps.
So Nishikawa,Kazuaki Homma,Yasunori Komori,Mitsuhiro Iwaki,Tetsuichi Wazawa,Atsuko Hikikoshi Iwone,Junya Saito,Reiko Ikebe,Eisaku Katayama,Eisaku Katayama,Toshio Yanagida,Mitsuo Ikebe +11 more
TL;DR: It is found by electron microscopy that myosin VI cooperatively binds to an actin filament at approximately 36 nm intervals in the presence of ATP, raising a hypothesis that the binding of myosIn VI evokes "hot spots" on actin filaments that attract myosIN heads, thus producing processive movement with 36 nm steps.
Journal ArticleDOI
The motor domain determines the large step of myosin-V.
Hiroto Tanaka,Kazuaki Homma,Atsuko H. Iwane,Eisaku Katayama,Eisaku Katayama,Reiko Ikebe,Junya Saito,Toshio Yanagida,Mitsuo Ikebe +8 more
TL;DR: The mechanical properties of single molecules of myosin-V truncation mutants with neck domains only one-sixth of the native length are measured and show that the processivity and step distance along actin are both similar to those of full-length myosIn-V.
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cGMP-Dependent Relaxation of Smooth Muscle Is Coupled With the Change in the Phosphorylation of Myosin Phosphatase
TL;DR: Results suggest that the phosphorylation at Ser640 induced by cGMP shifted the equilibrium of the Thr641 phosphorylated toward dephosphorylation, thus increasing MLCP activity, which results in the decrease in MLC phosphorylations and smooth muscle relaxation.
Journal ArticleDOI
Ca2+-dependent Regulation of the Motor Activity of Myosin V
TL;DR: Results indicate that inhibition of the motility is due to conformational changes of cal modulin upon the Ca2+ binding to the high affinity site but is not due to dissociation of calmodulin from the heavy chain.