Lander, Gabriel C.

A novel cereblon modulator recruits GSPT1 to the CRL4CRBN ubiquitin ligase

Matyskiela, M. E., Lu, G., Ito, T., Pagarigan, B., Lu, C.-C., Miller, K., Fang, W., Wang, N.-Y., Nguyen, D., Houston, J., et al. (2016) · Nature

Protein Degradation and InhibitorsUbiquitin and proteasome pathways

Cited by 701

High-Resolution Microtubule Structures Reveal the Structural Transitions in αβ-Tubulin upon GTP Hydrolysis

Alushin, G. M., Lander, G. C., Kellogg, E. H., Zhang, R., Baker, D., & Nogales, E. (2014) · Cell

Microtubule and mitosis dynamicsCancer Treatment and Pharmacology

Cited by 696

Complete subunit architecture of the proteasome regulatory particle

Lander, G. C., Estrin, E., Matyskiela, M. E., Bashore, C., Nogales, E., & Martin, A. (2012) · Nature

Ubiquitin and proteasome pathwaysEnzyme Structure and Function

Cited by 608

Conformational switching of the 26S proteasome enables substrate degradation

Matyskiela, M. E., Lander, G. C., & Martin, A. (2013) · Nature Structural & Molecular Biology

Ubiquitin and proteasome pathwaysHeat shock proteins research

Cited by 251

Molecular glue CELMoD compounds are regulators of cereblon conformation

Watson, E. R., Novick, S., Matyskiela, M. E., Chamberlain, P. P., H. de la Peña, A., Zhu, J., Tran, E., Griffin, P. R., Wertz, I. E., & Lander, G. C. (2022) · Science

Protein Degradation and InhibitorsUbiquitin and proteasome pathways

Cited by 208

Identification of an allosteric site on the E3 ligase adapter cereblon

Dippon, V. N., Rizvi, Z., Choudhry, A. E., Chung, C.-W., Alkuraya, I. F., Xu, W., Tao, X. B., Jurewicz, A. J., Schneck, J. L., Chen, W., et al. (2026) · Nature

Protein Degradation and InhibitorsUbiquitin and proteasome pathways

Cited by 14

Cellular Function of a Biomolecular Condensate Is Determined by Its Ultrastructure

Scholl, D., Boyd, T., Latham, A. P., Salazar, A., Khan, A., Boeynaems, S., Holehouse, A. S., Lander, G. C., Sali, A., Park, D., et al. (2024) · Nature Structural & Molecular Biology

Protein Structure and DynamicsRNA Research and Splicing

Cited by 14

The filamentous ultrastructure of the PopZ condensate is required for its cellular function

Scholl, D., Boyd, T., Latham, A. P., Salazar, A., Khan, A. M. A. M., Boeynaems, S., Holehouse, A. S., Lander, G. C., Sali, A., Park, D., et al. (2026) · Nature Structural & Molecular Biology

Protein Structure and DynamicsRNA Research and Splicing

Cited by 14