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Structure of mycobacterial ergothioneine-biosynthesis C-S lyase EgtE

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Cholesterol-activated stress granules reduce the membrane localization of DRD2 and promote prolactinoma dopamine agonists resistance

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Recent advances in the interplay between stress granules and m6A RNA modification

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USP39 phase separates into the nucleolus and drives lung adenocarcinoma progression by promoting GLI1 expression

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Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replicationPreprint

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β-propeller protein-associated neurodegeneration protein WDR45 regulates stress granule disassembly via phase separation with Caprin-1

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Histone Demethylase UTX Suppresses Tumor Cell Proliferation by Regulating Stress Granules

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Caprin1 Bridges PRMT1 to G3BP1 and Spaces Them to Ensure Proper Stress Granule Formation

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Expression of GADD45G and CAPRIN1 in Human Nucleus Pulposus: Implications for Intervertebral Disc Degeneration

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Electrostatics of Salt-Dependent Reentrant Phase Behaviors Highlights Diverse Roles of ATP in Biomolecular CondensatesPreprint

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Maximal inhibitory effect of MOV10 on LINE-1 retrotransposition requires both the MOV10/LINE-1 association and granule formation

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Clues for glues: from serendipity to nature’s blueprints in degrader discovery

Kozicka, Z. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253058 · Cited by 4 · see citing works

Targeted stress granule regulation by engineering a non-catalytic O-GlcNAc transferase

Wang, N., Hou, F., Ma, S., 刘思兰, Wei, H., Fang, W., Zhang, K., & Ge, Y. (2026) · Nature Communications · doi:10.1038/s41467-025-66689-6 · Cited by 3 · see citing works

Two Birds With One Stone: RNA Virus Strategies to Manipulate G3BP1 and Other Stress Granule Components

Firdaus, M. E. R., Dukhno, E., Kapoor, R., & Gerlach, P. (2025) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.70005 · Cited by 3 · see citing works

TDP-43 pathology triggers SRRM4-dependent cryptic splicing of G3BP1 in ALS/FTDPreprint

Fakim, H., Ghosh, A., Amzallag, E., Danino, Y. M., Triassi, V., Brown, A., Pal, N., Deshaies, J.-E., Dubinski, A. F., Lacombe, A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.17.676845 · Cited by 3 · see citing works

Stress Granules Play a Critical Role in Hexavalent Chromium Induced Malignancy in a G3bp1 Dependent Manner

Shaw, B., Thwin, P. H., Jia, N., Weng, H., Ma, C., Zhu, H., & Wang, L. (2024) · Environmental Pollution · doi:10.1016/j.envpol.2024.124997 · Cited by 2 · see citing works

Nanomaterial signatures program biomolecular condensates via triphasic separation for chemoplasticity remodeling

Zheng, L., Yan, Z., Li, X., Chang, J.-J., Tan, X.-Q., Wang, Y., Ding, H., Liu, Q., Ma, Y., & Huo, D. (2025) · Nature Communications · doi:10.1038/s41467-025-64623-4 · Cited by 5 · see citing works

CAPRIN1 specifically mediates m6A modification of RIG-I RNA to inhibit Mycobacterium Tuberculosis infection

Zhou, L., Chen, H., Jiang, D., Xu, X., Li, Z., Zheng, R., Huang, J., Ling, Y., Liao, Y., Wang, H., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08897-w · Cited by 2 · see citing works

RNA binding protein CAPRIN1 suppresses STAT1 translation and interferon signalling to promote HBV replication

Peng, J., Ding, Z., Liu, Q., Zhang, L., Chen, J., Chen, G., Gao, Y., Wang, S., Tian, X., Wei, Y., et al. (2026) · Gut · doi:10.1136/gutjnl-2025-337768 · Cited by 2 · see citing works

Targeting G3BP1-Mediated Stress Granules to Suppress SARS-CoV-2 Replication

Aromokeye, R., Kuang, L., Ackerman-Berrier, M. S., Cardoza, S., Holberg, C., Carver, M., Ma, C., Tharappel, A. M., Li, H., Wang, L., et al. (2026) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.5c01026 · Cited by 2 · see citing works

Enhancement of Stress Granule Formation by a Chiral Compound Targeting G3BP1 via eIF2α Phosphorylation

Park, Y. H., Cho, H. S., Moon, S., Namkoong, S., & Jung, H. S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910571 · Cited by 2 · see citing works

Neurogenetic Disorders and CAPRIN1

Brusco, A., & Pavinato, L. (2024) · Springer eBooks · doi:10.1007/978-3-031-32035-4_70-1 · Cited by 2 · see citing works

Emerging of Ultrafine Membraneless Organelles as the Missing Piece of Nanostress: Mechanism of Biogenesis and Implications at Multilevels

Liu, J., Zheng, L., Li, X., Tang, W., Guo, M., Wang, Y., Tan, X., Chang, J., Zhao, H., Zhu, D., et al. (2025) · ACS Nano · doi:10.1021/acsnano.4c15876 · Cited by 2 · see citing works

Identification and classification of abundant RNA-binding proteins in the mouse lens and interactions of Carhsp1, Igf2bp1/ZBP1, and Ybx1 with crystallin and β-actin mRNAsPreprint

Rayêe, D., Hwang, D.-W., Chang, W. K., Karp, I. N., Zhao, Y., Bowman, T. V., Lachke, S. A., Singer, R. H., Eliscovich, C., & Cvekl, A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.10.632466 · Cited by 2 · see citing works

The important role of stress granules in prostate cancer development, progression, and drug resistance

Xu, Z., You, H., Gu, J., Jiang, J., Yan, Z., & Jin, X. (2025) · Gene · doi:10.1016/j.gene.2025.149776 · Cited by 1 · see citing works

Pharmacological modulation of stress granules via G3BP1/2: A pathway to treat cancer, inflammatory disease, and neurodegeneration

Yang, J., & Gao, F. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1780146 · Cited by 1 · see citing works

Nitrate-responsive Sialin2 couples stress granule assembly and clearance to maintain neuronal homeostasis

Li, X., Cao, Z., Jiang, O., Wu, S., Zhou, B., Feng, Y., Chen, X., Wang, J., Zhou, J., Yan, R., et al. (2026) · Developmental Cell · doi:10.1016/j.devcel.2026.09.001 · Cited by 1 · see citing works

Drosophila and human Headcase define a new family of ribonucleotide granule proteins required for stress response

Ricolo, D., Casanova, J., & Giannios, P. (2025) · Science Advances · doi:10.1126/sciadv.ads2086 · Cited by 1 · see citing works

Defining short linear motif binding determinants by phage-based multiplexed deep mutational scanningPreprint

Benz, C., Maassen, L., Simonetti, L., Mihalič, F., Lindqvist, R., Tsitsa, I., Jemth, P., Överby, A. K., Davey, N. E., & Ivarsson, Y. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.06.606761 · Cited by 1 · see citing works

Structural insights into the Caprin-2 HR1 domain in canonical Wnt signaling

Su, C., Zhong, Y., Zhou, Z., Li, Y., Jia, Y., Xie, S., Zhao, J., Miao, H., Luo, H., Li, Z., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107694

Electrostatics of Salt-Dependent Reentrant Phase Behaviors Highlights Diverse Roles of ATP in Biomolecular CondensatesPreprint

Lin, Y.-H., Kim, T. H., Das, S., Pal, T., Wessén, J., Rangadurai, A., Kay, L. E., Forman-Kay, J. D., & Chan, H. S. (2024) · eLife · doi:10.7554/elife.100284.2

Intrinsic Factors Behind Long COVID: VI. Combined Impact of G3BPs and SARS‐CoV‐2 Nucleocapsid Protein on the Viral Persistence and Long COVID

Eltayeb, A., Rubio‐Casillas, A., Uversky, V. N., & Redwan, E. M. M. M. (2025) · Journal of Cellular Biochemistry · doi:10.1002/jcb.70038

Neurogenetic Disorders and CAPRIN1

Brusco, A., & Pavinato, L. (2025) · Springer eBooks · doi:10.1007/978-3-031-73368-0_70

Antimicrobial Activity Driven by Liquid-Liquid Phase Separation Induced by Bactericidal AgentsPreprint

Yao, K., Ban, Z., Yao, F., Huang, Y., Qiong, S., & Chen, L. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.6117268

CAPRIN1 (Cell Cycle-Associated Protein 1)-Related Neurodevelopmental Disorder: A Novel Mutation With Ataxia

Civan, R. A., Kottmeier, J., & Sidlow, R. (2026) · Cureus · doi:10.7759/cureus.103703

Dual Roles of Ubiquitin-Specific Peptidase 10 (USP10) in Cancer

Zhai, Y., Zhou, L., Zhao, M., & Lin, Q. (2026) · Cells · doi:10.3390/cells15060518

Time-dependent neuroprotective effects of YL-IPA08 in repetitive mild traumatic brain injury associated with changes in Caprin1/SHH signaling

Yu, C., Ye, Q., Song, Z., Li, J., Li, Z., Wang, Z., Wang, J., Li, H., Li, Y., & Ouyang, W. (2026) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2026.178868

Stress granules promote DNA damage repair through the G3BP1/NAT10/ATF3 axis to facilitate nasopharyngeal carcinoma progression

Tian, Y., Yin, H., Yuan, L., Xie, X., Xie, H., Gong, M., Xu, X., Sun, C., Zhang, K., & Liu, J. (2026) · Oncogene · doi:10.1038/s41388-026-03792-y

RNA-binding proteins in the mouse lens: Functional classifications, expression profiling, and interaction studies of Carhsp1 with crystallin mRNAs

Rayêe, D., Hwang, D.-W., Chang, W. K., Karp, I. N., Coomson, S. Y., Zhao, Y., Bowman, T. V., Lachke, S. A., Singer, R. H., Eliscovich, C., et al. (2026) · Developmental Biology · doi:10.1016/j.ydbio.2026.04.017

BOULE is Essential for the Dynamic Disassembly of Heat Shock Granules in Male Germ Cells

Li, X., Zhang, N., Bian, Z., Geng, B., Cao, L., Liu, P., Li, Z., Zhao, Y., & Tan, J. (2026) · Advanced Science · doi:10.1002/advs.77155

The role of cell cycle-associated protein 1 (CAPRIN1) in diseases

Li, C., Tang, P., Fu, Y., & Ji, R. (2026) · PeerJ · doi:10.7717/peerj.21772

G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits

Kedersha, N., Panas, M. D., Achorn, C. A., Lyons, S. M., Tisdale, S., Hickman, T. T., Thomas, M., Lieberman, J., McInerney, G. M., Ivanov, P. V., et al. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201508028 · Cited by 663 · see citing works

Both G3BP1 and G3BP2 contribute to stress granule formation

松木, 秀. (2013) · Medical Entomology and Zoology · Cited by 11 · see citing works

Pharmacological modulation of stress granules via G3BP1/2: A pathway to treat cancer, inflammatory disease, and neurodegeneration

Yang, J., & Gao, F. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1780146 · Cited by 1 · see citing works

Arabidopsis thaliana G3BP Ortholog Rescues Mammalian Stress Granule Phenotype across Kingdoms

Reuper, H., Götte, B., Williams, L., Tan, T. J. C., McInerney, G. M., Panas, M. D., & Krenz, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126287 · Cited by 9 · see citing works

Competing Molecular Interactions Govern the Dynamical Arrest of G3BP1 CondensatesPreprint

Singh, A., Liu, V., Mahendran, T. S., Rizvi, A., Gindra, B. H., Freibaum, B. D., Kim, H. J., Taylor, J. P., Pappu, R. V., & Banerjee, P. R. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.31.741769