Nature Search

Structure and function of a membrane component SecDF that enhances protein export

Tomoya Tsukazaki
Hiroyuki Mori
Osamu Nureki
Research11 May 2011
Nature

Volume: 474, P: 235-238
Incidence of endophthalmitis after intravitreal injection of an anti-VEGF agent with or without topical antibiotics

Masakazu Morioka
Yoshihiro Takamura
Masaru Inatani
ResearchOpen Access17 Dec 2020
Scientific Reports

Volume: 10, P: 1-6
Author Correction: Structural basis for the drug extrusion mechanism by a MATE multidrug transporter

Yoshiki Tanaka
Christopher J. Hipolito
Osamu Nureki
Amendments and Corrections30 Jan 2020
Nature

Volume: 578, P: E19
AFM observation of protein translocation mediated by one unit of SecYEG-SecA complex

Protein translocation across cellular membranes is an essential and nano-scale dynamic process. Here, the authors visualize protein translocation via the SecYEG-SecA complex in a nanodisc by high-speed atomic force microscopy (HS-AFM), shedding light on the structural changes of SecA in this process.

Yui Kanaoka
Takaharu Mori
Tomoya Tsukazaki
ResearchOpen Access08 Jan 2025
Nature Communications

Volume: 16, P: 1-12
Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase

Kaoru Kumazaki
Toshiki Kishimoto
Osamu Nureki
ResearchOpen Access03 Dec 2014
Scientific Reports

Volume: 4, P: 1-6
Conformational transition of Sec machinery inferred from bacterial SecYE structures

A crystal structure of SecY bound to an anti SecY Fab fragment revealing a pre-open state of the channel is presented.

Tomoya Tsukazaki
Hiroyuki Mori
Osamu Nureki
Research16 Oct 2008
Nature

Volume: 455, P: 988-991
Crystal structure of the channelrhodopsin light-gated cation channel

Channelrhodopsins are light-gated cation channels used in optogenetics; here, the high-resolution crystal structure of a channelrhodopsin from Chlamydomonas reinhardtii is determined.

Hideaki E. Kato
Feng Zhang
Osamu Nureki
Research22 Jan 2012
Nature

Volume: 482, P: 369-374
Development of a deep learning method for improving diagnostic accuracy for uterine sarcoma cases

Yusuke Toyohara
Kenbun Sone
Yutaka Osuga
ResearchOpen Access16 Nov 2022
Scientific Reports

Volume: 12, P: 1-11
Structural basis for the drug extrusion mechanism by a MATE multidrug transporter

Several X-ray crystal structures of an H⁺-driven multidrug and toxic compound extrusion (MATE) transporter from Pyrococcus furiosus are presented, whose complex structure with macrocyclic peptides may help facilitate the discovery of efficient inhibitors of MATE transporters.

Yoshiki Tanaka
Christopher J. Hipolito
Osamu Nureki
Research27 Mar 2013
Nature

Volume: 496, P: 247-251
Structural basis of Sec-independent membrane protein insertion by YidC

The crystal structure of the bacterial protein YidC is reported, together with a structure-based functional analysis, providing insight into the role of YidC in inserting single-spanning membrane proteins into the membrane.

Kaoru Kumazaki
Shinobu Chiba
Osamu Nureki
Research16 Apr 2014
Nature

Volume: 509, P: 516-520

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Structure and function of a membrane component SecDF that enhances protein export

Incidence of endophthalmitis after intravitreal injection of an anti-VEGF agent with or without topical antibiotics

Author Correction: Structural basis for the drug extrusion mechanism by a MATE multidrug transporter

AFM observation of protein translocation mediated by one unit of SecYEG-SecA complex

Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase

Conformational transition of Sec machinery inferred from bacterial SecYE structures

Crystal structure of the channelrhodopsin light-gated cation channel

Development of a deep learning method for improving diagnostic accuracy for uterine sarcoma cases

Structural basis for the drug extrusion mechanism by a MATE multidrug transporter

Structural basis of Sec-independent membrane protein insertion by YidC

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