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Shuwen Zhang
Institutions:
Mayo Clinic,
Peking University,
State Key Laboratory of Artificial Microstructure and Mesoscopic Physics
Observed institutions:
Mayo Clinic,
Peking University,
Center for Life Sciences,
State Key Laboratory of Artificial Microstructure and Mesoscopic Physics
ORCID:
0000-0002-5352-409X
Observed ORCIDs:
0000-0002-5352-409X,
0009-0006-0136-8503
OpenAlex ID:
A5008645266
Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome
2018
·
Yuanchen Dong
, Shuwen Zhang
, et al.
·
Nature
·
328
PDF
USP14-regulated allostery of the human proteasome by time-resolved cryo-EM
2022
·
Shuwen Zhang
, Shitao Zou
, et al.
·
Nature
·
109
PDF
AAA+ ATPases in Protein Degradation: Structures, Functions and Mechanisms
2020
·
Shuwen Zhang
, Youdong Mao
·
Biomolecules
·
61
PDF
Visualizing Conformational Space of Functional Biomolecular Complexes by Deep Manifold Learning
2022
·
Zhaolong Wu
, Enbo Chen
, et al.
·
International Journal of Molecular Sciences
·
29
PDF
Rapaprotin, an Endopeptidase‐Activated Proteasome Inhibitor that Induces 26S Disassembly
2025
·
Hanjing Peng
, Zufeng Guo
, et al.
·
Angewandte Chemie International Edition
·
2
Rapaprotin is Activated by an Endopeptidase to Disassemble 26S Proteasome
2025
·
Hanjing Peng
, Zufeng Guo
, et al.
·
bioRxiv (Cold Spring Harbor Laboratory)
·
2
UBE3C retrofits the proteasome to enforce degradation of ultra-stable folds
2026
·
Shitao Zou
, Deyao Yin
, et al.
·
bioRxiv (Cold Spring Harbor Laboratory)
A split biotin ligase approach reveals proteins associated with oligomeric alpha-synuclein during aggregation
2026
·
Analiese R. Fernandes
, Abigail P. Owen
, et al.
·
Scientific Reports
Rapaprotin, an Endopeptidase‐Activated Proteasome Inhibitor that Induces 26S Disassembly
2025
·
Hanjing Peng
, Zufeng Guo
, et al.
·
Angewandte Chemie
Molecular Mechanism of AAA-ATPase Motor in the 26S Proteasome
2023
·
Shuwen Zhang
, Youdong Mao
·
CRC Press eBooks
Cryo-electron microscopy revolutionizes molecular biophysics
2017
·
Yanan Zhu
, Shuwen Zhang
, et al.
·
Wuli
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Works count:
11
Citation count:
531
H-index:
4
I10-index:
4
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