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Profil bibliographique

Megan J. R. Yeo

Informations fournies par OpenAlex. Research Africa ne déduit ni nationalité, ni poste, ni coordonnées personnelles.

10Publications signalées
238Citations signalées
2Affiliations récentes

Les institutions déclarées

Les domaines associés

Protein Degradation and InhibitorsHistone Deacetylase Inhibitors ResearchRNA and protein synthesis mechanismsUbiquitin and proteasome pathwaysRNA modifications and cancer

Les publications récentes

Accès ouvert 2025 article OpenAlex

UM171 glues asymmetric CRL3–HDAC1/2 assembly to degrade CoREST corepressors

Megan J. R. Yeo, Olivia Zhang, Xiaowen Xie, Eunju Nam et autres

Abstract UM171 is a potent agonist of ex vivo human haematopoietic stem cell self-renewal 1 . By co-opting KBTBD4, a substrate receptor of the CUL3–RING E3 ubiquitin ligase (CRL3) complex, UM171 promotes the degradation of the LSD1–CoREST corepressor complex, thereby limiting haematopoietic …

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54 citations Nature
Accès ouvert 2025 article OpenAlex

Converging mechanism of UM171 and KBTBD4 neomorphic cancer mutations

Xiaowen Xie, Olivia Zhang, Megan J. R. Yeo, Ceejay Lee et autres

Abstract Cancer mutations can create neomorphic protein–protein interactions to drive aberrant function 1,2 . As a substrate receptor of the CULLIN3-RING E3 ubiquitin ligase complex, KBTBD4 is recurrently mutated in medulloblastoma 3 , the most common embryonal brain tumour in children 4 …

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43 citations Nature
Accès ouvert 2024 preprint OpenAlex

Asymmetric Engagement of Dimeric CRL3 KBTBD4 by the Molecular Glue UM171 Licenses Degradation of HDAC1/2 Complexes

Megan J. R. Yeo, Olivia Zhang, Xiaowen Xie, Eunju Nam et autres

UM171 is a potent small molecule agonist of ex vivo human hematopoietic stem cell (HSC) self-renewal, a process that is tightly controlled by epigenetic regulation. By co-opting KBTBD4, a substrate receptor of the CULLIN3-RING E3 ubiquitin ligase complex, UM171 promotes the degradation …

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1 citation bioRxiv (Cold Spring Harbor Laboratory)
Accès ouvert 2024 preprint OpenAlex

KBTBD4 Cancer Hotspot Mutations Drive Neomorphic Degradation of HDAC1/2 Corepressor Complexes

Xiaowen Xie, Olivia Zhang, Megan J. R. Yeo, Ceejay Lee et autres

Abstract Cancer mutations can create neomorphic protein-protein interactions to drive aberrant function 1 . As a substrate receptor of the CULLIN3-RBX1 E3 ubiquitin ligase complex, KBTBD4 is recurrently mutated in medulloblastoma (MB) 2 , the most common embryonal brain tumor in children, …

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5 citations bioRxiv (Cold Spring Harbor Laboratory)
Accès ouvert 2022 article OpenAlex

A Facile Platform to Engineer Escherichia coli Tyrosyl-tRNA Synthetase Adds New Chemistries to the Eukaryotic Genetic Code, Including a Phosphotyrosine Mimic

Katherine T. Grasso, Soumya Jyoti Singha Roy, Arianna O. Osgood, Megan J. R. Yeo et autres

High Resolution Image Download MS PowerPoint Slide The Escherichia coli tyrosyl-tRNA synthetase (EcTyrRS)/tRNA EcTyr pair offers an attractive platform for genetically encoding new noncanonical amino acids (ncAA) in eukaryotes. However, challenges associated with a eukaryotic selection system, which is needed to engineer …

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34 citations ACS Central Science
Accès ouvert 2022 article OpenAlex

Profiling the Landscape of Drug Resistance Mutations in Neosubstrates to Molecular Glue Degraders

Pallavi M. Gosavi, Kevin Chun-Ho Ngan, Megan J. R. Yeo, Cindy Su et autres

Targeted protein degradation (TPD) holds immense promise for drug discovery, but mechanisms of acquired resistance to degraders remain to be fully identified. Here, we used clustered regularly interspaced short palindromic repeats (CRISPR)-suppressor scanning to identify mechanistic classes of drug resistance mutations to …

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59 citations ACS Central Science
Accès ouvert 2021 preprint OpenAlex

Profiling the Landscape of Drug Resistance Mutations in Neosubstrates to Molecular Glue Degraders

Pallavi M. Gosavi, Kevin Chun-Ho Ngan, Megan J. R. Yeo, Cindy Su et autres

Abstract Targeted protein degradation (TPD) holds immense promise for drug discovery but mechanisms of acquired resistance to degraders remain to be fully identified. Here we used CRISPR-suppressor scanning to identify mechanistic classes of drug resistance mutations to molecular glue degraders in GSPT1 …

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5 citations bioRxiv (Cold Spring Harbor Laboratory)
Accès ouvert 2021 preprint OpenAlex

A facile platform to engineer E. coli tyrosyl-tRNA synthetase adds new chemistries to the eukaryotic genetic code, including a phosphotyrosine mimic

Katherine T. Grasso, Soumya Jyoti Singha Roy, Megan J. R. Yeo, Chintan Soni et autres

Abstract The E. coli tyrosyl-tRNA synthetase (EcTyrRS)/tRNA EcTyr pair offers an attractive platform to genetically encode new noncanonical amino acids (ncAA) in eukaryotes. However, challenges associated with a eukaryotic selection system, which is needed for its engineering, has impeded its success in …

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2 citations bioRxiv (Cold Spring Harbor Laboratory)
Accès ouvert 2021 article OpenAlex

Structural Robustness Affects the Engineerability of Aminoacyl-tRNA Synthetases for Genetic Code Expansion

Katherine T. Grasso, Megan J. R. Yeo, Christen M. Hillenbrand, Elise D. Ficaretta et autres

The ability to engineer the substrate specificity of natural aminoacyl-tRNA synthetase/tRNA pairs facilitates the site-specific incorporation of noncanonical amino acids (ncAAs) into proteins. The Methanocaldococcus jannaschii -derived tyrosyl-tRNA synthetase (MjTyrRS)/tRNA pair has been engineered to incorporate numerous ncAAs into protein expressed in …

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31 citations Biochemistry
Accès ouvert 2019 preprint OpenAlex

Structural robustness affects the engineerability of aminoacyl-tRNA synthetases for genetic code expansion

Katherine T. Grasso, Megan J. R. Yeo, Christen M. Hillenbrand, Elise D. Ficaretta et autres

Abstract The ability to engineer the substrate specificity of natural aminoacyl-tRNA synthetase/tRNA pairs facilitates the site-specific incorporation of noncanonical amino acids (ncAAs) into proteins. The Methanocaldococcus jannaschii derived tyrosyl-tRNA synthetase (MjTyrRS)/tRNA pair has been engineered to incorporate numerous ncAAs into protein expressed …

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4 citations bioRxiv (Cold Spring Harbor Laboratory)

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