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Publisher Correction: Dynamic structural states of ClpB involved in its disaggregation function

Takayuki Uchihashi
Yo-hei Watanabe
Toshio Ando
Amendments and CorrectionsOpen Access12 Jul 2019
Nature Communications

Volume: 10, P: 1
Biased Brownian stepping rotation of F_oF₁-ATP synthase driven by proton motive force

The visualization of ion-motive-force driven conformational dynamics of membrane proteins is hampered by technical difficulties. Here, the authors develop an experimental platform to visualize the rotary dynamics of ATP synthase driven by proton-motive-force.

Rikiya Watanabe
Kazuhito V. Tabata
Hiroyuki Noji
Research27 Mar 2013
Nature Communications

Volume: 4, P: 1-6
Rational engineering of DNA-nanoparticle motor with high speed and processivity comparable to motor proteins

DNA-based artificial molecular motors have flexibility in design, but exhibit lower speed and shorter run-length than motor proteins. Here, authors rationally engineered an artificial DNA-nanoparticle motor with high speed and long run-length which is comparable to motor proteins.

Takanori Harashima
Akihiro Otomo
Ryota Iino
ResearchOpen Access16 Jan 2025
Nature Communications

Volume: 16, P: 1-17
Impact of Hypertension and Hypertension-Related Vascular Lesions in IgA Nephropathy

Ryota Ikee
Shuzo Kobayashi
Soichiro Miura
Research01 Jan 2006
Hypertension Research

Volume: 29, P: 15-22
Dynamic structural states of ClpB involved in its disaggregation function

The bacterial protein disaggregation machine ClpB uses ATP to generate mechanical force to unfold and thread its protein substrates. Here authors visualize the ClpB ring using high-speed atomic force microscopy and capture conformational changes of the hexameric ring during the ATPase reaction.

Takayuki Uchihashi
Yo-hei Watanabe
Toshio Ando
ResearchOpen Access01 Jun 2018
Nature Communications

Volume: 9, P: 1-12
Capacitance enhancement by ion-laminated borophene-like layered materials

Liquid crystals with a single-layered boron network and interlayer alkali cations have been developed to enhance capacity between electrodes. Their switching functionality via phase transitions has also been demonstrated.

Tetsuya Kambe
Masahiro Katakura
Kimihisa Yamamoto
ResearchOpen Access27 Jan 2025
Nature Communications

Volume: 16, P: 1-8
Na⁺-V-ATPase inhibitor curbs VRE growth and unveils Na⁺ pathway structure

The authors identify V-161, a compound that inhibits enterococcal Na⁺-V-ATPase and reduces VRE colonization in mice. The high-resolution structure of V-161 reveals its action on the Na+ transport pathway, offering new therapeutic insights.

Kano Suzuki
Yoshiyuki Goto
Takeshi Murata
Research21 Nov 2024
Nature Structural & Molecular Biology

Volume: 32, P: 450-458
Direct observation of intermediate states during the stepping motion of kinesin-1

Laser-based dark field microscopy imaging of a gold-labeled kinesin head during microtubule movement reveals a rightward displacement of unbound kinesin mediated by increased tension in the neck linker.

Hiroshi Isojima
Ryota Iino
Michio Tomishige
Research29 Feb 2016
Nature Chemical Biology

Volume: 12, P: 290-297
Processive chitinase is Brownian monorail operated by fast catalysis after peeling rail from crystalline chitin

Processive chitinase is a linear molecular motor which moves on the surface of crystalline chitin. Here authors use single-molecule imaging, X-ray crystallography and simulations on chitinase A (SmChiA) and show that Brownian motion along the single chitin chain is rectified forward by substrate-assisted catalysis.

Akihiko Nakamura
Kei-ichi Okazaki
Ryota Iino
ResearchOpen Access19 Sept 2018
Nature Communications

Volume: 9, P: 1-12
Design of allosteric sites into rotary motor V₁-ATPase by restoring lost function of pseudo-active sites

Allostery produces concerted functions of protein complexes by orchestrating the cooperative work between the constituent subunits. By restoring functions of pseudo-active sites that have been lost through evolution, allosteric sites have now been designed into a rotary molecular motor, V₁-ATPase, resulting in its rotation being boosted allosterically.

Takahiro Kosugi
Tatsuya Iida
Nobuyasu Koga
ResearchOpen Access06 Jul 2023
Nature Chemistry

Volume: 15, P: 1591-1598
Phosphate release in F₁-ATPase catalytic cycle follows ADP release

A magnetic tweezer system that arrests the rotary ATP synthase F1 at the ATP-hydrolysis step provides an order of events to the chemomechanical cycle involving ADP release before phosphate release upon F1 rotation in ATP-hydrolysis mode.

Rikiya Watanabe
Ryota Iino
Hiroyuki Noji
Research26 Sept 2010
Nature Chemical Biology

Volume: 6, P: 814-820
Mechanical modulation of catalytic power on F₁-ATPase

Single-molecule studies on a molecular motor F₁-ATPase provide evidence that energy from catalysis is gradually converted to mechanical rotation, explaining the high efficiency of energy conversion and the mechanism for positive cooperativity among subunits during ATP hydrolysis.

Rikiya Watanabe
Daichi Okuno
Hiroyuki Noji
Research20 Nov 2011
Nature Chemical Biology

Volume: 8, P: 86-92
Accumulation of anchored proteins forms membrane diffusion barriers during neuronal polarization

Chieko Nakada
Kenneth Ritchie
Akihiro Kusumi
Research22 Jun 2003
Nature Cell Biology

Volume: 5, P: 626-632
Small stepping motion of processive dynein revealed by load-free high-speed single-particle tracking

Jun Ando
Tomohiro Shima
Ryota Iino
ResearchOpen Access23 Jan 2020
Scientific Reports

Volume: 10, P: 1-11
Six states of Enterococcus hirae V-type ATPase reveals non-uniform rotor rotation during turnover

Cryo-electron microscopy is used to trap six intermediate conformations of the active rotary vacuolar-type ATPase from Enterococcus hirae, revealing a non-uniform rotor rotation

Raymond N. Burton-Smith
Chihong Song
Kazuyoshi Murata
ResearchOpen Access28 Jul 2023
Communications Biology

Volume: 6, P: 1-13
Off-axis rotor in Enterococcus hirae V-ATPase visualized by Zernike phase plate single-particle cryo-electron microscopy

Jun Tsunoda
Chihong Song
Kazuyoshi Murata
ResearchOpen Access23 Oct 2018
Scientific Reports

Volume: 8, P: 1-10

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Publisher Correction: Dynamic structural states of ClpB involved in its disaggregation function

Biased Brownian stepping rotation of F_oF₁-ATP synthase driven by proton motive force

Rational engineering of DNA-nanoparticle motor with high speed and processivity comparable to motor proteins

Impact of Hypertension and Hypertension-Related Vascular Lesions in IgA Nephropathy

Dynamic structural states of ClpB involved in its disaggregation function

Capacitance enhancement by ion-laminated borophene-like layered materials

Na⁺-V-ATPase inhibitor curbs VRE growth and unveils Na⁺ pathway structure

Direct observation of intermediate states during the stepping motion of kinesin-1

Processive chitinase is Brownian monorail operated by fast catalysis after peeling rail from crystalline chitin

Design of allosteric sites into rotary motor V₁-ATPase by restoring lost function of pseudo-active sites

Phosphate release in F₁-ATPase catalytic cycle follows ADP release

Mechanical modulation of catalytic power on F₁-ATPase

Accumulation of anchored proteins forms membrane diffusion barriers during neuronal polarization

Small stepping motion of processive dynein revealed by load-free high-speed single-particle tracking

Six states of Enterococcus hirae V-type ATPase reveals non-uniform rotor rotation during turnover

Off-axis rotor in Enterococcus hirae V-ATPase visualized by Zernike phase plate single-particle cryo-electron microscopy

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