Author

M. J. Eck

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Assay:protein structure· 1

Frequent Co-Authors

E. Park· 2 shared A. Salguero· 1 shared A. Schmoker· 1 shared B.-W. Kim· 1 shared D. E. Heppner· 1 shared H. Arthanari· 1 shared H. Bae· 1 shared H. Jeon· 1 shared

Activity by Year

2022-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiochemistry

E. Park

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Structural analysis of the macrocyclic inhibitor BI-4020 binding to EGFR kinase

T. S. Beyett, J. K. Rana, I. K. Schaeffner, D. E. Heppner, M. J. Eck

The paper analyzes the structural basis of BI-4020's selectivity and potency against mutant EGFR by combining biochemical assays and X-ray crystallography.

bioRxiv · Aug 27, 2022Pharmacology & Toxicology

Cryo-EM structure of a RAS/RAF recruitment complex

M. J. Eck, H. Jeon, E. Park, S. Rawson, A. Schmoker, B.-W. Kim, S. Oh, K. Song

The paper presents cryo-EM structures of a KRAS/BRAF/MEK1/14-3-3 complex, showing KRAS binding to BRAF's Ras-binding domain without activating it, suggesting stabilization of a pre-activation intermediate as a therapeutic target.

bioRxiv · Jul 14, 2022Biochemistry

PH Domain-Mediated Autoinhibition and Oncogenic Activation of Akt

H. Bae, T. Viennet, E. Park, N. Chu, A. Salguero, M. J. Eck, H. Arthanari, P. A. Cole

This study identifies a mutation in the PH domain of Akt that enhances autoinhibition and reveals the molecular mechanism of Akt activation as an oncogenic driver.

bioRxiv · May 25, 2022Biochemistry