Author

Tian Hao Huang

University of TorontoORCID 0009-0004-6506-3384Unclaimed 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· 3 Organism:human· 2 Assay:proteomics· 2 Approach:statistical model· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

Alan M MosesiD· 2 shared Julie Deborah Forman-KayiD· 2 shared Zi Hao LiuiD· 2 shared Akhil Gargey Iragavarapu· 1 shared Ami G. SangsteriD· 1 shared Brian TsangiD· 1 shared Eileigh Kadijk· 1 shared Halil AydiniD· 1 shared

Activity by Year

2026-2026 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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2 shared papersCell Biology

Alan M MosesORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Pericentrin contains internal adaptor-like sequences that activate dynein directly

Wenzhu Zhang, Ami G. Sangster, Thao T. Nguyen, John P. Gillies, Samantha Melancon, Jia-Lin Shiu, Tian Hao Huang, Akhil Gargey Iragavarapu, Xueer Jiang, Jennielee Mia, Halil Aydin, Morgan E. DeSantis, Alan M Moses, Li-En Jao

The paper shows that Pericentrin contains an internal sequence that directly activates dynein for co-translational transport, challenging the notion that dynein relies solely on N-terminal adaptors.

bioRxiv · Oct 15, 2026 · PreprintCell Biology

Competing effects modulate the rate of poly(A) RNA deadenylation in a biomolecular condensate

Rose Irwin, Robert W. Harkness V, Brian Tsang, Zi Hao Liu, Kunyang Sun, Tian Hao Huang, Teresa L. Head-Gordon, Lewis E. Kay, Julie Deborah Forman-Kay

The paper investigates how competing factors in biomolecular condensates modulate the rate of poly(A) RNA deadenylation by CNOT7, revealing concentration-dependent increases and diffusion-related decreases in enzymatic efficiency.

bioRxiv · Jul 6, 2026 · PreprintBiochemistry

PRRC2A, PRRC2B and PRRC2C are Stress Granule Proteins that Promote Translation Through Association with the eIF3 complex

Jie Qi Huang, Eileigh Kadijk, Karl J. Schreiber, Zi Hao Liu, Rachel Chiang, Zhixin Zhang, Kevin M. Guttman, Tian Hao Huang, Sylvia M. T. Almeida, Olena Zhulyn, Alan M Moses, Julie Deborah Forman-Kay, John L. Rubinstein, Ji‐Young Youn

This study identifies PRRC2A, PRRC2B, and PRRC2C as stress granule proteins that regulate translation by interacting with the eIF3 complex and 48S PIC factors.

bioRxiv · Feb 25, 2026 · PreprintCell Biology