Author

H. Higgs

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 Cell Biology· 2 Pathology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 5 Approach:experimental assay· 5 Assay:proteomics· 3 Research Focus:cell type annotation· 2 Organism:mouse· 2 Research Focus:development & morphogenesis· 1 Research Focus:differential expression· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

R. Chakrabarti· 3 shared T. S. Fung· 3 shared A. L. Hatch· 1 shared A. Liu· 1 shared A. N. Kettenbach· 1 shared A. Suomalainen· 1 shared B. K. Subramanian· 1 shared C. Perez· 1 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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3 shared papersCell Biology

R. Chakrabarti

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Author profile →

5 papers

Recent·Most cited

Effects of phosphorylation on Drp1 activation by its receptors, actin, and cardiolipin

A. Liu, A. L. Hatch, H. Higgs

This study investigates how phosphorylation at S579 and S600 affects Drp1 GTPase activity, showing that S579 phosphorylation reduces actin and cardiolipin stimulation while S600 phosphorylation inhibits these effects.

bioRxiv · Aug 20, 2023Biochemistry

Mitochondrial dysfunction triggers actin polymerization necessary for rapid glycolytic activation

R. Chakrabarti, T. S. Fung, T. Kang, P. W. Pallijeff, A. Suomalainen, E. J. Usherwood, H. Higgs

This study shows mitochondrial dysfunction triggers actin polymerization (ADA) to enable rapid glycolytic activation in multiple cell types.

bioRxiv · Jun 3, 2022Cell Biology

Two distinct actin filament populations have effects on mitochondria, with differences in stimuli and assembly factors

T. S. Fung, W. Ji, H. Higgs, R. Chakrabarti

The paper identifies two distinct actin filament populations with different assembly factors and effects on mitochondrial dynamics in response to calcium and depolarization.

Journal of Cell Science · Sep 23, 2019Peer-reviewedCell Biology

Proteolytic program-dependent functions are impaired in INF2-mediated focal segmental glomerulosclerosis.

B. K. Subramanian, J. Chun, C. Perez, P. Yan, I. Stillman, H. Higgs, S. Alper, J. Schlondorff, M. Pollak

This study identifies a proteolytic cleavage mechanism in INF2 that affects its function in podocytes, leading to impaired localization and contributing to FSGS.

bioRxiv · Jan 26, 2019 · PreprintPathology

A complex containing lysine-acetylated actin inhibits the formin INF2

M. A, T. S. Fung, A. N. Kettenbach, R. Chakrabarti, H. Higgs

The paper identifies a complex of lysine-acetylated actin and CAP as an inhibitor of INF2, revealing a novel mechanism of facilitated auto-inhibition linked to disease.

bioRxiv · Dec 31, 2018Biochemistry