Author

Masihuz Zaman

St. Jude Children's Research HospitalORCID 0000-0002-3610-929XUnclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:mouse· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Research Focus:database / resource· 1 Research Focus:differential expression· 1 Research Focus:gene regulatory network inference· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

Danting LiuiD· 2 shared Gang YuiD· 2 shared Jay M. YarbroiD· 2 shared Junmin PengiD· 2 shared Ping‐Chung CheniD· 2 shared Xusheng WangiD· 2 shared Yun JiaoiD· 2 shared Zhiping WuiD· 2 shared

Activity by Year

2025-2025 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 44 mutual co-author links

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2 shared papersBiochemistry

Danting LiuORCID

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Author profile →

2 papers

Recent·Most cited

Midkine Attenuates Aβ Fibril Assembly and Amyloid Plaque Formation

Masihuz Zaman, Shu Yang, Ya Huang, Jay M. Yarbro, Yanhong Hao, Zhen Wang, Danting Liu, Kiara E. Harper, Hadeer Soliman, Alex Hemphill, Sarah Harvey, Shondra M. Pruett‐Miller, Valerie Stewart, Ajay Singh Tanwar, Ravi Kalathur, , Junmin Peng

This study shows that midkine reduces Aβ fibril formation and amyloid plaque development in Alzheimer's disease models.

bioRxiv · Mar 20, 2025 · PreprintBiochemistry

Human-mouse proteomics reveals the shared pathways in Alzheimer's disease and delayed protein turnover in the amyloidome

Jay M. Yarbro, Xian Han, Abhijit Dasgupta, Ka Yang, Danting Liu, Him K. Shrestha, Masihuz Zaman, Zhen Wang, Kaiwen Yu, Dong Geun Lee, David Vanderwall, Mingming Niu, Huan Sun, Boer Xie, Ping‐Chung Chen, , Junmin Peng

Alzheimer's mouse model proteomes capture 30% (amyloid-only models) to 42% (adding tau and splicing models) of consensus human AD protein changes; in 5xFAD, plaques slow degradation of plaque-associated proteins.

Nature Communications · Feb 11, 2025Peer-reviewedBiochemistry✦ In-depth digest