Author

Joshua H. Corbo

Harvard UniversityORCID 0000-0003-3991-3344Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Research Focus:gene regulatory network inference· 1 Research Focus:protein design· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

David J. TurneriD· 2 shared Eugene ValkoviD· 2 shared Aaron C. GoldstrohmiD· 1 shared Amanda J KorteiD· 1 shared Brenna A SaladiniD· 1 shared Cátia IgrejaiD· 1 shared Chen Qiu· 1 shared Elise B. DunsheeiD· 1 shared

Activity by Year

2023-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersMolecular Biology

David J. TurnerORCID

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3 papers

Recent·Most cited

Cell BiologybioRxivPreprintSep 24, 2026

RNF185 destabilizes specific membrane proteins that span all ERAD branches

Haruka Chino, Isabella M Ruiz, Joshua H. Corbo…·Sichen Shao

This study identifies RNF185 as a human ER-resident ubiquitin ligase that destabilizes membrane proteins with distinct aberrancies across all three ERAD branches.

DOI 10.64898/2026.09.23.753758

humanprotein structure

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Molecular BiologyJournal of Biological ChemistryPeer-reviewedFeb 13, 2026

Human Pumilio proteins use fuzzy multivalent hydrophobic interactions to recruit the CCR4-NOT deadenylase complex to repress mRNAs

Elise B. Dunshee, Brenna A Saladin, David J. Turner…·Aaron C. Goldstrohm

The paper identifies how human PUM proteins repress mRNAs by using fuzzy multivalent hydrophobic interactions to recruit the CCR4-NOT deadenylase complex through their intrinsically disordered RD3 domain.

1 citation

humanexperimental assay

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Molecular BiologybioRxivPreprintSep 20, 2023

A paradigm for regulation at the effector interface with RNA-binding proteins

Kriti Shah, Shiyang He, David J. Turner…·Jernej Murn

The paper identifies a multivalent RBP-effector interface that enables RNA recognition accuracy and functional repurposing of effector proteins.

1 citation

statistical model

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