Author

A. S. Fleischhacker

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 type annotation· 2 Approach:experimental assay· 2 Organism:human· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

L. Liu· 2 shared S. W. Ragsdale· 2 shared A. B. Dumbrepatil· 1 shared A. R. Reddi· 1 shared C. M. Moore· 1 shared D. A. Hanna· 1 shared E. N. G. Marsh· 1 shared I. Hamza· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

9 top collaborators · 26 mutual co-author links

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2 shared papersCell Biology

L. Liu

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2 papers

Recent·Most cited

Heme oxygenase-2 (HO-2) binds and buffers labile heme, which is largely oxidized, in human embryonic kidney cells

D. A. Hanna, C. M. Moore, L. Liu, X. Yuan, A. S. Fleischhacker, I. Hamza, S. W. Ragsdale, A. R. Reddi

This study shows HO-2 binds and buffers oxidized labile heme in HEK293 cells, regulating heme homeostasis by controlling bioavailability rather than degrading heme under non-stress conditions.

bioRxiv · Jun 6, 2021Cell Biology

Absence of heme at the catalytic site of heme oxygenase-2 triggers its lysosomal degradation

L. Liu, A. B. Dumbrepatil, A. S. Fleischhacker, E. N. G. Marsh, S. W. Ragsdale

This study identifies that heme absence at the catalytic site of HO2 triggers its lysosomal degradation, distinct from other HRM-containing proteins and HO1.

bioRxiv · Jun 21, 2020 · PreprintBiochemistry