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Oncoprotein HBXIP promotes tumorigenesis through MAPK/ERK pathway activation in non-small cell lung cancer

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Ragopathies and the rising influence of RagGTPases on human diseases

Sambri, I., Ferniani, M., & Ballabio, A. (2024) · Nature Communications · doi:10.1038/s41467-024-50034-4 · Cited by 8

Finding new edges: systems approaches to MTOR signaling

Heberle, A. M., Rehbein, U., Rodríguez-Peiris, M., & Thedieck, K. (2021) · Biochemical Society Transactions · doi:10.1042/bst20190730 · Cited by 8

Peripheral lysosomes recruit PLEKHG3 to focal adhesions and restrain protrusion dynamics

Ettelt, R., Șandru, A.-M., Vucak, G., Didusch, S., Riemelmoser, B., Ehrenreiter, K., Hartl, M., Huber, L. A., & Baccarini, M. (2026) · FEBS Letters · doi:10.1002/1873-3468.70428 · Cited by 8

Codependencies of mTORC1 signaling and endolysosomal actin structures

Priya, A., Antoine‐Bally, S., Macé, A., Monteiro, P., Sabatet, V., Remy, D., Dingli, F., Loew, D., Demetriades, C., Gautreau, A. M., et al. (2023) · Science Advances · doi:10.1126/sciadv.add9084 · Cited by 7

Cryo-EM structure of the BLOC-3 complex provides insights into the pathogenesis of Hermansky-Pudlak syndrome

Yong, X., Jia, G., Yang, Q., Zhou, C., Zhang, S., Deng, H., Billadeau, D. D., Su, Z., & Jia, D. (2025) · Nature Communications · doi:10.1038/s41467-025-58235-1 · Cited by 7

A CRISPR screen in intestinal epithelial cells identifies novel factors for polarity and apical transport

Klee, K. M., Hess, M. W., Lohmüller, M., Herzog, S., Pfaller, K., Müller, T., Vogel, G. F., & Huber, L. A. (2023) · eLife · doi:10.7554/elife.80135 · Cited by 7

Multiomic analysis reveals a key BCAT1 role in mTOR activation by B cell receptor and TLR9

Guo, R., Sun, Y., Lim, M. Y., Shah, H., Paulo, J. A., Ahmed, R. A., Li, W., Zhang, Y., Yang, H., Wang, L. W., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci186258 · Cited by 8

How mTORC1 makes sense of nutrients

Luciani, A., & Stagi, M. (2020) · Kidney International · doi:10.1016/j.kint.2020.07.052 · Cited by 6

CASTOR1 and CASTOR2 respond to different arginine levels to regulate mTORC1 activity.

Liu, C., Zhang, Y., Wang, Y., Wu, M., Li, Y.-C., Wei, J., Shi, J., Wang, R., Su, L., Yang, T., et al. (2026) · Molecules and Cells · doi:10.1016/j.molcel.2025.12.016 · Cited by 6

EGO complex at 20: The Rag GTPase-TORC1 nutrient-sensing blueprint

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Mapping the Interactome of KRAS and Its G12C/D/V Mutants by Integrating TurboID Proximity Labeling with Quantitative Proteomics

Song, J., Wang, B., Zou, M., Zhou, H., Ding, Y., Ren, W., Fang, L., & Zhang, J. (2025) · Biology · doi:10.3390/biology14050477 · Cited by 5

Amino Acid Sensing: Architecture of mTORC1 on the Lysosome Surface

Peng, W., & Jewell, J. L. (2020) · Current Biology · doi:10.1016/j.cub.2019.11.087 · Cited by 5

Understanding P-Rex regulation: structural breakthroughs and emerging perspectives

Jones, G., & Ellisdon, A. M. (2024) · Biochemical Society Transactions · doi:10.1042/bst20231546 · Cited by 5

Crosstalk between dysregulated amino acid sensing and glucose and lipid metabolism in colorectal cancer

Wang, D., Zou, S., Ding, J., Gao, C., Wang, J., & Tang, Z. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1665056 · Cited by 5

Une moisson de nouvelles structures de mTORC1

Nawrotek, A., & Cherfils, J. (2021) · médecine/sciences · doi:10.1051/medsci/2021033 · Cited by 4

GIGYF2: A Multifunctional Regulator at the Crossroads of Gene Expression, mRNA Surveillance, and Human Disease

Zhao, C.-S., Liu, S., Li, Z., Chen, J.-Y., & Xiong, X. (2025) · Cells · doi:10.3390/cells14131032 · Cited by 3

Reversing an agonist into an inhibitor: Development of mTOR degraders

Zhu, L., Fu, S., Ma, L., Chen, Z., Zeng, Q., Li, R., Zhou, Y., Qian, H., Meng, X., & Ge, J. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117774 · Cited by 3

Genetic dissection of Ragulator structure and function in amino acid-dependent regulation of mTORC1.

Nada, S., & Okada, M. (2020) · Journal of Biochemistry (Tokyo) · doi:10.1093/jb/mvaa076 · Cited by 2

Hayatine inhibits amino acid-induced mTORC1 activation as a novel mTOR-Rag A/C interaction disruptor

Lü, M., Yu, L., Yang, Y., Zhu, J., Qiang, S., Wang, X., Wang, J., Tan, X., Wang, W.-F., Zhang, Y., et al. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.10.014 · Cited by 3

Structural Exploration on Palmitoyltransferase DHHC3 from Homo sapiens

Tang, M., Xia, Y., Xiao, T., Cao, R., Cao, Y., & OuYang, B. (2022) · Polymers · doi:10.3390/polym14153013 · Cited by 3

Structure of human mTORC1 components

Ray, L. B. (2017) · Science · doi:10.1126/science.358.6361.316-t

Hybrid Structure of the RagA/C-Ragulator mTORC1 Activation Complex

Su, M.-Y., Morris, K. K., Kim, D. J., Fu, Y., Lawrence, R. E., Stjepanović, G., Zoncu, R., & Hurley, J. H. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.11.193 · Cited by 2

Structural insight into the Ragulator complex which anchors mTORC1 to the lysosomal membrane

Mu, Z., Wang, L., Deng, W., Wang, J., & Wu, G. (2017) · Cell Discovery · doi:10.1038/celldisc.2017.49 · Cited by 63

Structural basis for the assembly of the Ragulator-Rag GTPase complex

Yonehara, R., Nada, S., Nakai, T., Nakai, M., Kitamura, A., Ogawa, A., Nakatsumi, H., Nakayama, K. I., Li, S., Standley, D. M., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01762-3 · Cited by 75

Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1

Zhang, T., Wang, R., Wang, Z., Wang, X., Wang, F., & Ding, J. (2017) · Nature Communications · doi:10.1038/s41467-017-01567-4 · Cited by 72