Nature Search

A nucleotide code governs Lis1’s ability to relieve dynein autoinhibition

A combination of biochemical, cell biological and electron microscopy analyses reveal a ‘nucleotide code’ that coordinates Lis1–dynein binding stoichiometry, which in turn governs Lis1’s ability to relieve dynein autoinhibition.

Indigo C. Geohring
Pengxin Chai
Steven M. Markus
ResearchOpen Access22 Jan 2026
Nature Chemical Biology

P: 1-14
The mechanochemical cycle of reactive full-length human dynein 1

Chai et al. use cryo-electron microscopy to systematically interrogate the conformational landscape of motor protein dynein. The reported structures reveal intermediate states in the mechanochemical cycle of dynein, the role of adenosine triphosphate and the communication mechanism with microtubules.

Pengxin Chai
Jun Yang
Kai Zhang
Research22 Apr 2025
Nature Structural & Molecular Biology

Volume: 32, P: 1383-1395
Visualizing the translation landscape in human cells at high resolution

Understanding protein synthesis in its cellular context is essential. Here, authors apply in situ cryo-EM to reveal the human ribosome at 2.2 Å resolution, capture 23 states, and uncover drug-specific translation features in native cells.

Wei Zheng
Yuekang Zhang
Yong Xiong
ResearchOpen Access28 Nov 2025
Nature Communications

Volume: 16, P: 1-13
Nde1 promotes Lis1 binding to full-length autoinhibited human dynein 1

Cryo-electron microscopy and biochemical reconstitution analysis reveals that Nde1 enhances Lis1 binding to autoinhibited dynein, promoting formation of a Phi-like–Lis1 intermediate during dynein activation.

Jun Yang
Yuanchang Zhao
Kai Zhang
Research01 Aug 2025
Nature Chemical Biology

Volume: 22, P: 274-283
Author Correction: Cryo-EM structure of an active central apparatus

Long Han
Qinhui Rao
Kai Zhang
Amendments and CorrectionsOpen Access10 Mar 2023
Nature Structural & Molecular Biology

Volume: 30, P: 564
Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism

Outer-arm dyneins (OADs) assemble in large arrays on the ciliary axoneme to drive rhythmic beating. Cryo-EM structures of microtubule-bound Tetrahymena thermophila OAD arrays reveal details of this complex assembly and suggest a model for its mechanism of coordinated action.

Qinhui Rao
Long Han
Kai Zhang
ResearchOpen Access23 Sept 2021
Nature Structural & Molecular Biology

Volume: 28, P: 799-810
Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport

LIS1 is a critical activator of dynein-mediated retrograde transport. Ton et al. reveal that microtubule binding by dynein initiates a cascade of structural changes that trigger LIS1 dissociation from dynein prior to transport, providing insights into dynein activation.

William D. Ton
Yue Wang
Steven M. Markus
Research15 Jun 2023
Nature Structural & Molecular Biology

Volume: 30, P: 1365-1379
Cryo-EM structure of an active central apparatus

Here, authors solve cryo-EM structures of the central apparatus of motile cilia and analyze its dynamic conformations to elucidate the mechanism of ciliary beating.

Long Han
Qinhui Rao
Kai Zhang
ResearchOpen Access16 May 2022
Nature Structural & Molecular Biology

Volume: 29, P: 472-482
High-resolution in situ structures of mammalian respiratory supercomplexes

Mammalian respiratory supercomplexes are imaged in their native membrane environment by in situ cryo-electron microscopy, providing insight into their reactive intermediates and conformational dynamics.

Wan Zheng
Pengxin Chai
Kai Zhang
ResearchOpen Access29 May 2024
Nature

Volume: 631, P: 232-239
Impact of multimorbidity and cognitive impairment on depressive symptoms in community-dwelling older adults and their interaction effects

Pengxin Dong
Haichen Wu
Huiqiao Huang
ResearchOpen Access29 Apr 2025
Scientific Reports

Volume: 15, P: 1-8

Search

Filter By:

Search

Quick links