Author

L. Na

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Microbiology· 3 Plant Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Organism:human· 2 Assay:proteomics· 2 Organism:Arabidopsis· 1 Organism:chicken / avian· 1

Frequent Co-Authors

X. Wang· 3 shared C. Du· 2 shared H. Zhang· 2 shared Y. Wang· 2 shared Z. Zhang· 2 shared C. Liu· 1 shared C. Naumann· 1 shared C. Smith· 1 shared

Activity by Year

2016-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersMicrobiology

X. Wang

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

The SUMO-interacting Motif in NS2 promotes adaptation of avian influenza virus to mammals

L. Sun, H. Kong, M. Yu, Z. Zhang, H. Zhang, L. Na, Y. Qu, Y. Zhang, H. Chen, X. Wang

This study identifies NS2's SUMO-interacting motif as critical for avian influenza virus adaptation to mammals by enhancing vRNP assembly and ANP32A/B interactions.

Science Advances · Jul 14, 2023Peer-reviewedMicrobiology

Keap1 recognizes EIAV early accessory protein Rev to promote antiviral defense

Y. Wang, G. Ma, X.-F. Wang, L. Na, X. Guo, J. Zhang, C. Liu, C. Du, Y. Lin, X. Wang

This study shows the Nrf2/Keap1 axis is activated by EIAV-Rev, leading to antiviral effects through two mechanisms: enhancing antioxidant defenses and inhibiting Rev-mediated RNA transport.

bioRxiv · Sep 29, 2021Microbiology

ANP32A and ANP32B are key factors in the Rev dependent CRM1 pathway for nuclear export of HIV-1 unspliced mRNA

Y. Wang, H. Zhang, L. Na, C. Du, Z. Zhang, Y. Zheng, X. Wang

This study identifies ANP32A and ANP32B as essential host factors that facilitate HIV-1 unspliced RNA export via the Rev-CRM1 pathway.

bioRxiv · Mar 24, 2019Microbiology

Ubiquitylation activates a peptidase that promotes cleavage and destabilization of its activating E3 ligases and diverse growth regulatory proteins to limit cell proliferation in Arabidopsis

H. Dong, J. Dumenil, F.-H. Lu, L. Na, H. Vanhaeren, C. Naumann, M. Klecker, R. Prior, C. Smith, N. McKenzie, G. Saalbach, L. Chen, T. Xia, N. Gonzalez, M. Seguela, , M. W. Bevan

The paper identifies DA1 as a ubiquitin-activated peptidase in Arabidopsis that cleaves and destabilizes E3 ligases and growth regulatory proteins to limit cell proliferation during organ development.

bioRxiv · Nov 30, 2016Plant Biology