Author

C. J. Howard

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 Evolutionary Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:proteomics· 3 Research Focus:protein folding & dynamics· 2 Research Focus:benchmarking· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:ChIP-seq· 1 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

A. D. Johnson· 1 shared A. Frost· 1 shared A. M. Bardo· 1 shared A. N. Johnson· 1 shared B. A. Osuna· 1 shared B. M. Floyd· 1 shared C. M. Ghent· 1 shared C. P. Hill· 1 shared

Activity by Year

2018-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 8 mutual co-author links

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1 shared paperEvolutionary Biology

A. D. Johnson

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4 papers

Recent·Most cited

Phosphorylation modulates liquid-liquid phase separation of the SARS-CoV-2 N protein

C. R. Carlson, J. B. Asfaha, C. M. Ghent, C. J. Howard, N. Hartooni, D. O. Morgan

This study shows phosphorylation of SARS-CoV-2 N protein modulates its phase separation behavior, forming liquid-like droplets that may support viral genome processing.

bioRxiv · Jun 28, 2020Biochemistry

Solid-Phase Peptide Capture and Release for Bulk and Single-Molecule Proteomics

C. J. Howard, B. M. Floyd, A. M. Bardo, J. Swaminathan, E. M. Marcotte, E. V. Anslyn

This paper introduces a solid-phase peptide capture method for bulk and single-molecule proteomics, demonstrating its effectiveness in isolating and modifying peptides from cell lysates.

bioRxiv · Jan 13, 2020Biochemistry

Intrinsic cooperativity potentiates parallel cis-regulatory evolution

T. R. Sorrells, A. N. Johnson, C. J. Howard, C. S. Britton, K. R. Fowler, J. T. Feigerle, P. A. Weil, A. D. Johnson

The paper shows that intrinsic cooperativity between transcription factors enables parallel cis-regulatory evolution in fungal lineages by channeling mutations into functional sites.

bioRxiv · Apr 14, 2018Evolutionary Biology

Vms1p is a release factor for the Ribosome-associated Quality control Complex

O. Z. Rendon, E. K. Fredrickson, C. J. Howard, J. V. Vranken, S. Fogarty, N. D. Tolley, R. Kalia, B. A. Osuna, P. S. Shen, C. P. Hill, A. Frost, J. Rutter

This study identifies Vms1p as the tRNA hydrolase that releases nascent polypeptides in the RQC pathway for degradation.

bioRxiv · Apr 14, 2018Biochemistry