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Katsuyoshi Mihara
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Journal Articles

Fis1 acts as a mitochondrial recruitment factor for TBC1D15 that is involved in regulation of mitochondrial morphology

Kenta Onoue, Akihiro Jofuku, Reiko Ban-Ishihara, Takaya Ishihara, Maki Maeda, Takumi Koshiba, Takashi Itoh, Mitsunori Fukuda, Hidenori Otera, Toshihiko Oka, Hiroyoshi Takano, Noboru Mizushima, Katsuyoshi Mihara, Naotada Ishihara
Journal: Journal of Cell Science
J Cell Sci (2013) 126 (1): 176–185.
https://doi.org/10.1242/jcs.111211
Published: 1 January 2013
View article titled, Fis1 acts as a mitochondrial recruitment factor for TBC1D15 that is involved in regulation of mitochondrial morphology
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Includes: Supplementary data
Journal Articles

KLP6: a newly identified kinesin that regulates the morphology and transport of mitochondria in neuronal cells

Kousuke Tanaka, Yoshimi Sugiura, Ryohei Ichishita, Katsuyoshi Mihara, Toshihiko Oka
Journal: Journal of Cell Science
J Cell Sci (2011) 124 (14): 2457–2465.
https://doi.org/10.1242/jcs.086470
Published: 15 July 2011
View article titled, KLP6: a newly identified kinesin that regulates the morphology and transport of mitochondria in neuronal cells
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Includes: Multimedia, Supplementary data
Journal Articles

Characterization of the mitochondrial protein LETM1, which maintains the mitochondrial tubular shapes and interacts with the AAA-ATPase BCS1L

Shoko Tamai, Hiroshi Iida, Sadaki Yokota, Tomoko Sayano, Shoko Kiguchiya, Naotada Ishihara, Jun-Ichi Hayashi, Katsuyoshi Mihara, Toshihiko Oka
Journal: Journal of Cell Science
J Cell Sci (2008) 121 (15): 2588–2600.
https://doi.org/10.1242/jcs.026625
Published: 1 August 2008
View article titled, Characterization of the mitochondrial protein LETM1, which maintains the mitochondrial tubular shapes and interacts with the AAA-ATPase BCS1L
Open the PDF for Characterization of the mitochondrial protein LETM1, which maintains the mitochondrial tubular shapes and interacts with the AAA-ATPase BCS1L in another window
Includes: Supplementary data
Journal Articles

Identification of a novel protein that regulates mitochondrial fusion by modulating mitofusin (Mfn) protein function

Yuka Eura, Naotada Ishihara, Toshihiko Oka, Katsuyoshi Mihara
Journal: Journal of Cell Science
J Cell Sci (2006) 119 (23): 4913–4925.
https://doi.org/10.1242/jcs.03253
Published: 1 December 2006
View article titled, Identification of a novel protein that regulates mitochondrial fusion by modulating mitofusin (Mfn) protein function
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Journal Articles

Ubiquitin-proteasome-dependent degradation of mammalian ER stearoyl-CoA desaturase

Hiroki Kato, Kenjiro Sakaki, Katsuyoshi Mihara
Journal: Journal of Cell Science
J Cell Sci (2006) 119 (11): 2342–2353.
https://doi.org/10.1242/jcs.02951
Published: 1 June 2006
View article titled, Ubiquitin-proteasome-dependent degradation of mammalian ER stearoyl-CoA desaturase
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Journal Articles

Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity

Naotada Ishihara, Yuka Eura, Katsuyoshi Mihara
Journal: Journal of Cell Science
J Cell Sci (2004) 117 (26): 6535–6546.
https://doi.org/10.1242/jcs.01565
Published: 15 December 2004
View article titled, Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
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Journal Articles

Characterization of rat TOM70 as a receptor of the preprotein translocase of the mitochondrial outer membrane

Hiroyuki Suzuki, Maki Maeda, Katsuyoshi Mihara
Journal: Journal of Cell Science
J Cell Sci (2002) 115 (9): 1895–1905.
https://doi.org/10.1242/jcs.115.9.1895
Published: 1 May 2002
View article titled, Characterization of rat TOM70 as a receptor of the preprotein translocase of the mitochondrial outer membrane
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Journal Articles

Direct targeting of cis-Golgi matrix proteins to the Golgi apparatus

Shin-ichiro Yoshimura, Nobuhiro Nakamura, Francis A. Barr, Yoshio Misumi, Yukio Ikehara, Hiroshi Ohno, Masao Sakaguchi, Katsuyoshi Mihara
Journal: Journal of Cell Science
J Cell Sci (2001) 114 (22): 4105–4115.
https://doi.org/10.1242/jcs.114.22.4105
Published: 15 November 2001
View article titled, Direct targeting of cis-Golgi matrix proteins to the Golgi apparatus
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