Author

Liangkun Long

Nanjing Forestry UniversityORCID 0000-0001-7302-6330Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Approach:experimental assay· 1 Organism:fungi (other)· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

Congcong Yuan· 1 shared Shaojun DingiD· 1 shared Yuxing Sun· 1 shared

Activity by Year

2025-2025 · peak 1/yr

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3 top collaborators · 3 mutual co-author links

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1 shared paperBiochemistry

Congcong Yuan

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1 paper

Recent·Most cited

BiochemistrybioRxivPreprintSep 2, 2025

Novel single-domain AA12 pyrroloquinoline quinone-dependent oxidoreductases directly and co-operatively drive lytic polysaccharide monooxygenase activity with AA8 module

Yuxing Sun, Congcong Yuan, Liangkun Long, Shaojun Ding

This study identifies single-domain AA12 oxidoreductases and free AA8 modules as direct and cooperative electron donors to lytic polysaccharide monooxygenase (LPMO) in cellulolytic fungi.

DOI 10.1101/2025.09.02.673750

fungi (other)proteomics

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