Author

C. M. Nadel

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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Organism:C. elegans· 1 Research Focus:development & morphogenesis· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

J. E. Gestwicki· 3 shared E. C. Carroll· 2 shared M. D. Callahan· 2 shared A. C. Thwin· 1 shared A. Oehler· 1 shared A. R. Cupo· 1 shared A. R. de Silva· 1 shared A. W. Kao· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiochemistry

J. E. Gestwicki

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3 papers

Recent·Most cited

Phosphorylation of a Cleaved Tau Proteoform at a Single Residue Inhibits Binding to the E3 Ubiquitin Ligase, CHIP

C. M. Nadel, K. Wucherer, A. Oehler, A. C. Thwin, K. Basu, M. D. Callahan, D. R. Southworth, D. A. Mordes, C. S. Craik, J. E. Gestwicki

This study identifies phosphorylation at residue S416 on tauC3 as a mechanism that inhibits its degradation by CHIP, contributing to its accumulation in Alzheimer's disease.

bioRxiv · Aug 16, 2023 · PreprintBiochemistry

Interaction with the membrane-anchored protein CHIC2 constrains the ubiquitin ligase activity of CHIP

M. D. Callahan, M. Hodul, E. C. Carroll, M. Ravalin, C. M. Nadel, A. R. de Silva, A. R. Cupo, L. E. McDermott, J. C. Nix, R. C. Page, A. W. Kao, J. E. Gestwicki

This study identifies CHIC2 as a chaperone-independent regulator of CHIP, showing it attenuates CHIP's ubiquitin ligase activity and contributes to neurodegeneration in C. elegans.

bioRxiv · Jul 17, 2023 · PreprintBiochemistry

Two distinct classes of co-chaperones compete for the EEVD motif in heat shock protein 70 (Hsp70) to tune its activity

O. T. Johnson, C. M. Nadel, E. C. Carroll, T. Arhar, J. E. Gestwicki

The paper identifies two co-chaperones that compete for the EEVD motif of Hsp70, influencing its activity by determining whether bound proteins are folded or degraded.

bioRxiv · Oct 18, 2021 · PreprintBiochemistry