CIMR-Xiao Yan

Research Group

Xiao Yan

yanxiao(at)cimrbj.ac.cn

Assistant Investigator

Liquid-Liquid Phase Separation, Protein Aggregation, ALS/FTD, AI-Guided Molecular Therapeutics, Neurodegeneration

yanxiao(at)cimrbj.ac.cn

B.S. in Bioengineering, Zhejiang University, China

M.S. in Biochemical Engineering, Zhejiang University, China

Ph.D. in Biochemistry, Max Planck Institute of Biochemistry, Germany

Work Experience

2026.07-Present

Assistant Investigator, Chinese Institute for Medical Physiology, Chinese Institutes for Medical Research, Beijing, China

2019-2026

Postdoctoral Researcher, Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany

Honors and Awards

2024

Science Fund Program for Excellent Young Scientists (Overseas)

2019

Summa Cum Laude

Research Interests

The Yan laboratory studies biomolecular condensates — dynamic, liquid-like assemblies that cells use to organize RNA and proteins — and how their breakdown drives amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), two devastating neurodegenerative diseases. We are building a condensate-centric framework for these diseases around four connected questions:

1. Aggregation mechanism. We view protein aggregation not as an isolated event, but as a network-driven process triggered when condensates fail under stress, transitioning from functional assemblies into pathological aggregates.

2. Structural landscapes. We map the structural routes proteins take as they aggregate inside condensates, tracking how disordered and structured regions change conformation en route to pathological states.

3. Condensate pathology. We dissect how this condensate dysfunction mechanistically drives disease onset.

4. Diagnostics and therapeutics. Building on these mechanistic and structural insights, we apply AI-guided protein design toward early diagnosis and therapeutic intervention.

Major Contributions

1. Linked condensate biophysics to ALS/FTD. We discovered intra-condensate demixing as a novel mechanism driving TDP-43 aggregation, revealing a fundamental link between condensate physics and neurodegenerative disease (Cell, 2025).

2. Revealed phase separation as an organelle-building principle. We showed liquid-liquid phase separation drives de novo assembly of β-carboxysomes (Nature, 2019).

3. Defined chaperone mechanisms in protein folding. We uncovered the ring separation mechanism of the GroEL/GroES chaperonin system, a key step in protein folding (Cell, 2018).

Representative Publications *：Co-first author; #：Co-corresponding author

Yan X, Kuster D, Mohanty P, et al. Intra-condensate demixing of TDP-43 inside stress granules generates pathological aggregates. Cell, 2025, 188: 1-18. DOI: 10.1016/j.cell.2025.04.039

Yin HH, Han YL, Yan X^#, Guan YX^#. Hematoxylin modulates tau-RD protein fibrillization and ameliorates Alzheimer's disease-like symptoms in a yeast model. International Journal of Biological Macromolecules, 2023, 250: 126-140. DOI: 10.1016/j.ijbiomac.2023.126140

Yin HH, Han YL, Yan X^#, Guan YX^#. Proanthocyanidins prevent tau protein aggregation and disintegrate tau filaments. Chinese Journal of Chemical Engineering, 2023, 57: 63-71. DOI: 10.1016/j.cjche.2022.09.013

Wang H*, Yan X*, Aigner H, et al. Rubisco condensate formation by CcmM in β-carboxysome biogenesis. Nature, 2019, 566: 131-135. DOI: 10.1038/s41586-019-0880-5

Yan X, Shi Q, Bracher A, et al. GroEL Ring Separation and Exchange in the Chaperonin Reaction. Cell, 2018, 172: 605-617. DOI: 10.1016/j.cell.2017.12.010

Yan X, Hu S, Guan YX, Yao SJ. Coexpression of chaperonin GroEL/GroES markedly enhanced soluble and functional expression of recombinant human interferon-gamma in Escherichia coli. Applied Microbiology and Biotechnology, 2012, 93: 1065-1074. DOI: 10.1007/s00253-011-3599-2

Full List of Publications Can Be Found here