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Research:

Proteins can be thought of as mini machines or tools that execute the work in the cell. The shape of a protein is a critical factor in determining how well it can perform its tasks. Protein can lose their regular shape (misfold) for many reasons such as activity or cellular stress. In some select cases, proteins can take on alternate shapes that allow them to stack together like building blocks into long fibril structures called amyloids. The buildup of amyloids in cells and tissues is linked to several diseases e.g. Alzheimer’s, Parkinson’s, Huntington’s disease. Our team is trying to understand the biochemical features of proteins that increase their risk of misfolding into amyloids and how this process can be prevented. We also are very interested in understanding our cell’s evolved defense mechanisms against protein misfolding. In particular, we study a group of protective proteins called molecular chaperones that are considered the first line of defense against protein misfolding. We aim to understand how molecular chaperones recognize protein folding problems and why their protection fails when we develop diseases such as Alzheimer’s.

Our team uses biochemical and cellular methods to interrogate tau protein aggregation and aggregate structures associated with neurodegenerative diseases. A main focus in our lab is to develop high-throughput approaches in cloning, protein purification and protein structure and activity assays. Using these novel tools, we aim to systematically define the complex relationships between the factors regulating protein aggregation such as kinetics, phase separation, structure, chaperone recognition, and induced cell stress and damage.

 

Selected Publications:

Sun KT, Mok SA..
Neurotherapeutics (2025) Article in Press, e00512. 

Bravo CP, Giani AM, Perez JM, Zhao Z, Samelson A, Wong MY, Evangelisti A, Fan L, Pozner T, Mercedes M, Ye P, Patel T, Yarahmady A, Carling G, Lee VMY, Sharma M, Mok SA, Luo W, Zhao M, Kampmann M, Gong S, Gan L.
Cell (2024) 187(10):2446-2464

Paul PS, Patel T, Cho J-Y, Yarahmady A, Khalili A, Semencheko V, Wille H, Kulka M, Mok SA, Kar S.
Scientific Reports (2024) 14(1):144.

Sun KT, Patel T, Kang S-G, Yarahmady A, Julien O, Heras J, Mok SA
ACS Chemical Neuroscience (2023) 14(24):4282-4297.

Udeochu J, Amin S, Huang Y, Fan L, Torres E, Liu B, McGurran H, Coronas-Samano G, Kauwe G, Mousa GA, Wong MY, Ye P, Nagiri RK, Lo I, Holtzman J, Corona C, Yarahmady A, Gill M, Raju R, Mok SA, Gong S, Luo W, Tracy TE, Ratan R , Tsai L-H, Sinha S, Gan L.
Nature Neuroscience (2022) 26(5): 737-750.

Sun KT, Patel TS, Kim J, Tang HSH, Eskandari-Sedighi G, Sureshkumar H, Schieve D, Mok SA.
STAR Protocols (2022) 4(1):101930.

Kang SG, Han G, Daude N, McNamara E, Wohlgemuth S, Molina-Porcel L, Safar JG, Mok SA, Westaway D.
BMC Biology (2021) 19(1): 199.

Mok SA, Condello C, Freilich R, Gillies, A, Arhar T, Oroz J, Kadavath H, Julien O, Assimon VA, Rauch JN, Dunyak BM, Lee J, Tsai FTF, Wilson MR, Zweckstetter M, Dickey CA, Gestwicki JE.
Nature Structural and Molecular Biology (2018) 25(5): 384-393.