Recognition and reprogramming of E3 ubiquitin ligase surfaces by α-helical peptides

Autor: Olena S. Tokareva, Kunhua Li, Tara L. Travaline, Ty M. Thomson, Jean-Marie Swiecicki, Mahmoud Moussa, Jessica D. Ramirez, Sean Litchman, Gregory L. Verdine, John H. McGee

Publikováno v: Nature Communications, Vol 14, Iss 1, Pp 1-19 (2023)

Abstract Molecules that induce novel interactions between proteins hold great promise for the study of biological systems and the development of therapeutics, but their discovery has been limited by the complexities of rationally designing interactio

Externí odkaz: https://doaj.org/article/d47fd7432d3c4f0a95e499dc5d2f9158

Stapled peptide inhibitors of RAB25 target context-specific phenotypes in cancer

Autor: Shreya Mitra, Jeffrey E. Montgomery, Matthew J. Kolar, Gang Li, Kang J. Jeong, Bo Peng, Gregory L. Verdine, Gordon B. Mills, Raymond E. Moellering

Publikováno v: Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)

The Ras-family small GTPase RAB25 can exert both pro- and anti-oncogenic functions. Here, the authors develop all-hydrocarbon stabilized peptides targeting RAB25 and influencing the context-specificity phenotypes in cancer cell lines.

Externí odkaz: https://doaj.org/article/88dae4a0195d4721a84d58ee911ac1ec

Mechanism of DNA Lesion Homing and Recognition by the Uvr Nucleotide Excision Repair System

Autor: Seung-Joo Lee, Rou-Jia Sung, Gregory L. Verdine

Publikováno v: Research, Vol 2019 (2019)

Nucleotide excision repair (NER) is an essential DNA repair system distinguished from other such systems by its extraordinary versatility. NER removes a wide variety of structurally dissimilar lesions having only their bulkiness in common. NER can al

Externí odkaz: https://doaj.org/article/9670cbf2ff2a45388f81484b0ab4a684

De novo mapping of α-helix recognition sites on protein surfaces using unbiased libraries

Autor: Kunhua Li, Olena S. Tokareva, Ty M. Thomson, Sebastian C. T. Wahl, Tara L. Travaline, Jessica D. Ramirez, Santosh K. Choudary, Sorabh Agarwal, Ward G. Walkup, Tivoli J. Olsen, Matthew J. Brennan, Gregory L. Verdine, John H. McGee

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 119(52)

The α-helix is one of the most common protein surface recognition motifs found in nature, and its unique amide-cloaking properties also enable α-helical polypeptide motifs to exist in membranes. Together, these properties have inspired the developm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cd6b9d4ca8e5ed4e4242f16217e6ee7
https://pubmed.ncbi.nlm.nih.gov/36534810

Genomic discovery of an evolutionarily programmed modality for small-molecule targeting of an intractable protein surface

Autor: Dylan T. Stiles, Keith Robison, Alan S. Mann, Brian R. Bowman, Tara Hardy, Michelle L. Stewart, Siavash Mostafavi, Gregory L. Verdine, Seung-Joo Lee, Morgenstern Jay P, Zhigang Weng, Mathew E. Sowa, Sukrat Arya, Andrew M. Fry, Kyle Kenyon, Ende Pan, Richard D. Klausner, Khian Hong Pua, Roy M. Pollock, Sharon A. Townson, Minyun Zhou, Uddhav Kumar Shigdel, Andrew T Rajczewski, Joshua A. V. Blodgett, Daniel W. Udwary, Daniel C. Gray

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, vol 117, iss 29
Proceedings of the National Academy of Sciences of the United States of America

Significance This manuscript reports on a member of the FK506/rapamycin family, WDB002, and the realization that FKBP-mediated recognition is a genetically programmable modality that enables engagement of topologically flat targets. FKBP-mediated rec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3ebc35e6171956666cc689edb272560
https://escholarship.org/uc/item/96w4n83f