Author

Guoliang Lu

Fudan UniversityORCID 0000-0003-1427-8874Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:protein structure prediction· 2 Organism:Arabidopsis· 1 Assay:ChIP-seq· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Approach:genetic perturbation / CRISPR· 1 Organism:human· 1

Frequent Co-Authors

Jinzhong LiniD· 3 shared Aiwu DongiD· 1 shared Bing LiuiD· 1 shared Damu WuiD· 1 shared Guopeng WangiD· 1 shared Jiabing WuiD· 1 shared Jiachen WangiD· 1 shared Jinru ZhangiD· 1 shared

Activity by Year

2022-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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3 shared papersMolecular Biology

Jinzhong LinORCID

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3 papers

Recent·Most cited

Molecular BiologyNature CommunicationsPeer-reviewedOct 29, 2026

Viral tRNA-like structure hijacks host ribosomes for poly(A)-independent translation

Guoliang Lu, Liming Wan, Yuchen Chen…·Jinzhong Lin

This study shows how a viral tRNA-like structure recruits host ribosomes for poly(A)-independent translation by binding to ribosomal subunits and substituting for poly(A) tails.

1 citation

proteomicsexperimental assay

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Plant BiologyStructurePeer-reviewedMay 12, 2025

Structural and functional interrelationship of histone H2A and its variants H2A.Z and H2A.W in Arabidopsis

Youchao Wang, Jiabing Wu, Shuoming Yang…·Aiwu Dong

The paper investigates the structural and functional relationships between histone H2A and its variants H2A.Z and H2A.W in Arabidopsis using CRISPR/Cas9 mutants and cryo-EM, revealing redundancy and substitution capabilities.

6 citations

ArabidopsisChIP-seq

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Molecular BiologybioRxivPreprintMar 10, 2022

Structure and Mechanism of a Structural and Functional Insights into the Action Mode of A Mitochondrial AAA+ DisaggregaseCLPB

Damu Wu, Yan Liu, Yuhao Dai…·Ning Gao

This study reveals the structural and functional mechanism of CLPB, a mitochondrial AAA+ disaggregase, showing its unique assembly and substrate translocation properties.

1 citation

humanprotein structure

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