Angela S Fleischhacker
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Explore the profile of Angela S Fleischhacker including associated specialties, affiliations and a list of published articles.
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Recent Articles
1.
Zheng K, Rush K, Date S, Johs A, Parks J, Fleischhacker A, et al.
Proc Natl Acad Sci U S A
. 2024 Nov;
121(47):e2408086121.
PMID: 39546574
Mercury (Hg) is a heavy metal that exhibits high biological toxicity. Monomethylmercury and dimethylmercury are neurotoxins and a significant environmental concern as they bioaccumulate and biomagnify within the aquatic food...
2.
Dai Y, Fleischhacker A, Liu L, Fayad S, Gunawan A, Stuehr D, et al.
Biol Chem
. 2022 Oct;
403(11-12):1043-1053.
PMID: 36302634
Heme regulatory motifs (HRMs) are found in a variety of proteins with diverse biological functions. In heme oxygenase-2 (HO2), heme binds to the HRMs and is readily transferred to the...
3.
Hanna D, Moore C, Liu L, Yuan X, Dominic I, Fleischhacker A, et al.
J Biol Chem
. 2022 Jan;
298(2):101549.
PMID: 34973332
Heme oxygenases (HOs) detoxify heme by oxidatively degrading it into carbon monoxide, iron, and biliverdin, which is reduced to bilirubin and excreted. Humans express two isoforms of HO: the inducible...
4.
Fleischhacker A, Sarkar A, Liu L, Ragsdale S
Crit Rev Biochem Mol Biol
. 2021 Sep;
57(1):16-47.
PMID: 34517731
Heme is an essential biomolecule and cofactor involved in a myriad of biological processes. In this review, we focus on how heme binding to heme regulatory motifs (HRMs), catalytic sites,...
5.
Liu L, Dumbrepatil A, Fleischhacker A, Marsh E, Ragsdale S
J Biol Chem
. 2020 Oct;
295(50):17227-17240.
PMID: 33051205
Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Tight regulation of the cellular levels and...
6.
Fleischhacker A, Gunawan A, Kochert B, Liu L, Wales T, Borowy M, et al.
J Biol Chem
. 2020 Mar;
295(16):5177-5191.
PMID: 32152224
Heme-regulatory motifs (HRMs) are present in many proteins that are involved in diverse biological functions. The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues...
7.
Kochert B, Fleischhacker A, Wales T, Becker D, Engen J, Ragsdale S
J Biol Chem
. 2019 Apr;
294(20):8259-8272.
PMID: 30944174
Heme oxygenase (HO) catalyzes heme degradation, a process crucial for regulating cellular levels of this vital, but cytotoxic, cofactor. Two HO isoforms, HO1 and HO2, exhibit similar catalytic mechanisms and...
8.
Fleischhacker A, Ragsdale S
J Biol Chem
. 2018 Sep;
293(37):14569-14570.
PMID: 30217868
Labile heme, as opposed to heme that is tightly bound within proteins, is thought to require a chaperone to be trafficked within the cell due to its cytotoxicity, but the...
9.
Fleischhacker A, Carter E, Ragsdale S
Antioxid Redox Signal
. 2017 Oct;
29(18):1841-1857.
PMID: 28990415
Significance: Heme binds to and serves as a cofactor for a myriad of proteins that are involved in diverse biological processes. Hemoproteins also exhibit varying modes of heme binding, suggesting...
10.
Davydov R, Fleischhacker A, Bagai I, Hoffman B, Ragsdale S
Biochemistry
. 2015 Dec;
55(1):62-8.
PMID: 26652036
The two isoforms of human heme oxygenase (HO1 and HO2) catalyze oxidative degradation of heme to biliverdin, Fe, and CO. Unlike HO1, HO2 contains two C-terminal heme regulatory motifs (HRMs)...