Author

A.-P. Zeng

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

Biology Disciplines

Click to filter author papers

Biochemistry· 2 Bioengineering· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Organism:E. coli· 2 Research Focus:cell type annotation· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

W. Wang· 3 shared J. Nie· 2 shared J. Ren· 2 shared Y. Liu· 2 shared C. Ma· 1 shared C. Zhang· 1 shared D. I. Svergun· 1 shared H. Ma· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

W. Wang

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Design, evaluation and implementation of synthetic isopentyldiol pathways in Escherichia coli

Y. Liu, L. Chen, P. Liu, Q. Yuan, C. Ma, W. Wang, C. Zhang, H. Ma, A.-P. Zeng

The paper designs and evaluates synthetic isopentyldiol pathways in E. coli, finding that a computationally designed pathway produces IPDO at 2.2 mg/L from glucose.

bioRxiv · Feb 21, 2023 · PreprintBioengineering

Stand-alone lipoylated H-protein of the glycine cleavage system enables glycine cleavage and the synthesis of glycine from one-carbon compounds in vitro

Y. Xu, Y. Li, H. Zhang, J. Nie, J. Ren, W. Wang, A.-p. Zeng

This paper shows that lipoylated H-protein can catalyze glycine cleavage and synthesis reactions in vitro without the other GCS proteins.

bioRxiv · Mar 28, 2021 · PreprintBiochemistry

A non-structural pure enzyme protein forms an LCST type of stimuli-responsive and reversible hydrogel with novel structure and catalytic activity

J. Nie, X. Zhang, Y. Liu, M. Schroer, W. Wang, J. Ren, D. I. Svergun, A.-P. Zeng

This paper reports a unique enzyme, LplA, that forms a stimuli-responsive and reversible hydrogel with catalytic activity, revealing its structural and functional mechanisms.

bioRxiv · Feb 7, 2021 · PreprintBiochemistry