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Yo-Hei Watanabe

Showing results (11-20 of 16) with videos related to

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Scientific Reports|August 19, 2017
Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregationSayaka Hayashi, Yosuke Nakazaki, Kei Kagii, et al.
The Journal of Biological Chemistry|October 18, 2018
Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregationSaori Sugita, Kumiko Watanabe, Kana Hashimoto, et al.
FEBS Letters|November 21, 2012
Conformational transition of the lid helix covering the protease active site is essential for the ATP-dependent protease activity of FtsHRyoji Suno, Masakazu Shimoyama, Akiko Abe, et al.
Cell|October 22, 2003
The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated stateSukyeong Lee, Mathew E Sowa, Yo-hei Watanabe, et al.
Nature Communications|July 14, 2019
Publisher Correction: Dynamic structural states of ClpB involved in its disaggregation functionTakayuki Uchihashi, Yo-Hei Watanabe, Yosuke Nakazaki, et al.
Nature Communications|June 3, 2018
Dynamic structural states of ClpB involved in its disaggregation functionTakayuki Uchihashi, Yo-Hei Watanabe, Yosuke Nakazaki, et al.
Pageof 2

Showing results (11-20 of 16) with videos related to

Sort By:
Pageof 2
You have reached the last page of results.This site can display upto 16 results.
Scientific Reports|August 19, 2017
Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregationSayaka Hayashi, Yosuke Nakazaki, Kei Kagii, et al.
The Journal of Biological Chemistry|October 18, 2018
Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregationSaori Sugita, Kumiko Watanabe, Kana Hashimoto, et al.
FEBS Letters|November 21, 2012
Conformational transition of the lid helix covering the protease active site is essential for the ATP-dependent protease activity of FtsHRyoji Suno, Masakazu Shimoyama, Akiko Abe, et al.
Cell|October 22, 2003
The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated stateSukyeong Lee, Mathew E Sowa, Yo-hei Watanabe, et al.
Nature Communications|July 14, 2019
Publisher Correction: Dynamic structural states of ClpB involved in its disaggregation functionTakayuki Uchihashi, Yo-Hei Watanabe, Yosuke Nakazaki, et al.
Nature Communications|June 3, 2018
Dynamic structural states of ClpB involved in its disaggregation functionTakayuki Uchihashi, Yo-Hei Watanabe, Yosuke Nakazaki, et al.
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