Results 111 to 120 of about 120,535 (297)

Senotherapeutics for Knee Osteoarthritis

open access: yesMedicinal Research Reviews, EarlyView.
ABSTRACT Osteoarthritis (OA) is a chronic disease that imposes a significant economic burden and deteriorates quality of life. Nevertheless, current therapeutic options for OA are limited to symptomatic remedies. As such, there is a high interest in novel methods for treating or preventing OA.
Ezgi Duman   +6 more
wiley   +1 more source

Post-Mortem Diagnosis of Heme Oxygenase-1 Deficiency by Whole Exome Sequencing in an Iranian Child [PDF]

open access: yesInternational Journal of Molecular and Cellular Medicine, 2019
Heme oxygenase-1 (HO-1) is an inducible enzyme involved in the catalysis of heme conversion into biliverdin. We describe a patient with a novel stop-gain mutation in the HMOX1 coding sequence resulting in HO-1 deficiency.
Fatemeh Tahghighi   +2 more
doaj  

IL-10 provides cardioprotection in diabetic myocardial infarction via upregulation of Heme clearance pathways

open access: yesJCI Insight, 2020
Diabetes is a risk factor for myocardial infarction, and outcomes after myocardial infarction are worse among diabetics compared with nondiabetics. Diabetes is associated with impaired Heme clearance.
Rajesh Gupta   +11 more
doaj   +1 more source

Spectroscopic Studies Reveal That the Heme Regulatory Motifs of Heme Oxygenase‑2 Are Dynamically Disordered and Exhibit Redox- Dependent Interaction with Heme

open access: yes, 2015
: Heme oxygenase (HO) catalyzes a key step ...
Brian M. Hoffman (1270242)   +13 more
core   +1 more source

Capture of long‐missing heme oxygenases that degrade both heme b and heme c

open access: yesmLife, EarlyView.
Abstract Heme serves as a crucial cofactor for hemoproteins and as an iron reservoir; yet, its accumulation is toxic, necessitating efficient degradation pathways. While the catabolism of free heme b is well characterized, the enzymes that disrupt its counterpart covalently tethered to a peptide (heme c) have remained elusive.
Jiyuan Hou   +4 more
wiley   +1 more source

The clinical relevance of heme detoxification by the macrophage heme oxygenase system

open access: yesFrontiers in Immunology
Heme degradation by the heme oxygenase (HMOX) family of enzymes is critical for maintaining homeostasis and limiting heme-induced tissue damage. Macrophages express HMOX1 and 2 and are critical sites of heme degradation in healthy and diseased states ...
Scott Yeudall   +4 more
doaj   +1 more source

Repurposing antimicrobial agents for neuroprotection: Mechanisms, clinical potential, and challenges

open access: yesNeuroprotection, EarlyView.
Antimicrobial agents exert neuroprotective effects through modulation of interconnected pathways. Tetracyclines, macrolides, antimalarial agents, sulfones, and antiparasitic agents suppress neuroinflammation, oxidative stress, and apoptosis while preserving mitochondrial function and neurotransmission.
Mohammad Amin Manavi   +5 more
wiley   +1 more source

Proposed reaction pathway for the formation of biliverdin IXγ from heme by a heme oxygenase-like mechanism.

open access: yes, 2014
Proposed reaction pathway for the formation of biliverdin IXγ from heme by a heme oxygenase-like mechanism.
Ana B. G. Veiga (589839)   +5 more
core   +1 more source

Baicalin Induces Ferroptosis in Breast Cancer Through a Novel STAT3/HO‐1/GPX4 Regulatory Axis

open access: yesPhytotherapy Research, EarlyView.
BA inhibits STAT3 phosphorylation and activation in BC cells, accompanied by decreased expression of HO‐1 and GPX4. Reduced GPX4 activity impairs lipid peroxide clearance, promoting ROS accumulation and lipid peroxidation, which ultimately triggers ferroptosis and inhibits cell proliferation.
Tingting Guo   +11 more
wiley   +1 more source

Expression of inducible heme oxygenase in human endometrium

open access: yes, 2002
Heme oxygenase (HO) was initially described as the regulatory enzyme in the heme degradative pathways. It catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin, which acts as an antioxidant.
Casanas-Roux, Françoise   +3 more
core   +1 more source

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