Author

C. R. Langlois

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· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Assay:proteomics· 2 Organism:yeast· 2 Approach:biophysical modeling· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

D. Sherpa· 2 shared J. Chrustowicz· 2 shared M. Mann· 2 shared O. Karayel· 2 shared A. F. Alpi· 1 shared B. A. Schulman· 1 shared B. Schulman· 1 shared F. M. Hansen· 1 shared

Activity by Year

2021-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 40 mutual co-author links

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2 shared papersCell Biology

D. Sherpa

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2 papers

Recent·Most cited

A GID E3 ligase assembly ubiquitinates an Rsp5 E3 adaptor and regulates plasma membrane transporters

C. R. Langlois, V. Beier, O. Karayel, J. Chrustowicz, D. Sherpa, M. Mann, B. Schulman

The paper shows that the GID E3 ligase system regulates plasma membrane transporters through a stress-specific substrate receptor, Gid10, and ubiquitinates Art2.

bioRxiv · Sep 2, 2021Cell Biology

GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme

D. Sherpa, J. Chrustowicz, S. Qiao, C. R. Langlois, L. A. Hehl, K. V. Gottemukkala, F. M. Hansen, O. Karayel, S. von Gronau, J. R. Prabu, M. Mann, A. F. Alpi, B. A. Schulman

The paper reveals a supramolecular chelate assembly mechanism by which E3 ligases target oligomeric substrates, demonstrating this in yeast and human orthologs.

bioRxiv · Apr 7, 2021Biochemistry