Author

C. M. Noddings

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 Biophysics· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 3 Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:chromatin & epigenetic regulation· 2 Organism:human· 1

Frequent Co-Authors

D. A. Agard· 3 shared J. L. Johnson· 2 shared A. Myasnikov· 1 shared E. Kirschke· 1 shared R. Y.- R. Wang· 1 shared R. Y.-R. Wang· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

6 top collaborators · 11 mutual co-author links

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3 shared papersBiochemistry

D. A. Agard

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3 papers

Recent·Most cited

Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the Glucocorticoid Receptor

C. M. Noddings, J. L. Johnson, D. A. Agard

This paper presents cryo-EM structures of GR:Hsp90:FKBP51 and GR:Hsp90:FKBP52 complexes, revealing their distinct roles in regulating GR activity through different binding interfaces and allosteric mechanisms.

bioRxiv · Jan 10, 2023Biochemistry

GR chaperone cycle mechanism revealed by cryo-EM: inactivation of GR by GR:Hsp90:Hsp70:Hop client-loading complex

R. Y.- R. Wang, C. M. Noddings, E. Kirschke, A. Myasnikov, J. L. Johnson, D. A. Agard

The paper reports the cryo-EM structure of the GR loading complex, revealing the molecular mechanism of GR inactivation and chaperone coordination.

bioRxiv · Nov 5, 2020 · PreprintBiochemistry

GR chaperone cycle mechanism revealed by cryo-EM: reactivation of GR by the GR:Hsp90:p23 client-maturation complex

C. M. Noddings, R. Y.-R. Wang, D. A. Agard

This paper reveals the molecular mechanism of GR activation by Hsp90 through cryo-EM, showing GR ligand binding is restored and stabilized by the Hsp90:p23 complex.

bioRxiv · Sep 12, 2020Biophysics