Yifan Cheng
Researcher Next ID · RN-021625
Researcher · Biochemistry, Genetics and Molecular Biology
University of Science and Technology of China
Hefei, Bangladesh
- Works count
- 353
- Citation count
- 41,762
- H-index
- 86
- i10-index
- 197
Research interests
Publications
Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms
Nature · 2020 · https://doi.org/10.1038/s41586-020-2668-z
Single-particle cryo-EM—How did it get here and where will it go
Science · 2018 · 10.1126/science.aat4346
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Nature Methods · 2017 · https://doi.org/10.1038/nmeth.4193
Cryo-EM structures of the TMEM16A calcium-activated chloride channel
Nature · 2017 · 10.1038/nature25024
Automated structure refinement of macromolecular assemblies from cryo-EM maps using Rosetta
eLife · 2016 · 10.7554/elife.17219
TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action
Nature · 2016 · 10.1038/nature17964
Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement
Nature Methods · 2015 · https://doi.org/10.1038/nmeth.3286
EMRinger: side chain–directed model and map validation for 3D cryo-electron microscopy
Nature Methods · 2015 · https://doi.org/10.1038/nmeth.3541
Glycine receptor mechanism elucidated by electron cryo-microscopy
Nature · 2015 · 10.1038/nature14853
Structure of the TRPA1 ion channel suggests regulatory mechanisms
Nature · 2015 · 10.1038/nature14367
Single-Particle Cryo-EM at Crystallographic Resolution
Cell · 2015 · 10.1016/j.cell.2015.03.049
A Primer to Single-Particle Cryo-Electron Microscopy
Cell · 2015 · 10.1016/j.cell.2015.03.050
Structure of the TRPV1 ion channel determined by electron cryo-microscopy
Nature · 2013 · https://doi.org/10.1038/nature12822
TRPV1 structures in distinct conformations reveal activation mechanisms
Nature · 2013 · https://doi.org/10.1038/nature12823
Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
Nature Methods · 2013 · https://doi.org/10.1038/nmeth.2472
Acetylation-Mediated Proteasomal Degradation of Core Histones during DNA Repair and Spermatogenesis
Cell · 2013 · 10.1016/j.cell.2013.04.032
Direct Membrane Association Drives Mitochondrial Fission by the Parkinson Disease-associated Protein α-Synuclein
Journal of Biological Chemistry · 2011 · 10.1074/jbc.m110.213538
HIV Nef is Secreted in Exosomes and Triggers Apoptosis in Bystander CD4+ T Cells
Traffic · 2009 · 10.1111/j.1600-0854.2009.01006.x
Mechanism of Gate Opening in the 20S Proteasome by the Proteasomal ATPases
Molecular Cell · 2008 · 10.1016/j.molcel.2008.03.004
Docking of the Proteasomal ATPases' Carboxyl Termini in the 20S Proteasome's α Ring Opens the Gate for Substrate Entry
Molecular Cell · 2007 · 10.1016/j.molcel.2007.06.033
Lipid–protein interactions in double-layered two-dimensional AQP0 crystals
Nature · 2005 · 10.1038/nature04321
Aquaporin-0 membrane junctions reveal the structure of a closed water pore
Nature · 2004 · 10.1038/nature02503
Structure of the Human Transferrin Receptor-Transferrin Complex
Cell · 2004 · 10.1016/s0092-8674(04)00130-8
Negative staining and image classification — powerful tools in modern electron microscopy
Biological Procedures Online · 2004 · 10.1251/bpo70
Molecular model for a complete clathrin lattice from electron cryomicroscopy
Nature · 2004 · 10.1038/nature03079
Current projects
No projects listed.