Myoglobin (Mb) is an oxygen-binding muscular hemeprotein regulated via Ca2+-signaling
pathways involving calcineurin (CN), with Mb increases attributed to hypoxia, exercise, and …

Myoglobin (Mb) is a regulator of O2 bioavailability in type I muscle and heart, at least when
tissue O2 levels drop. Mb also plays a role in regulating cellular nitric oxide (NO) pools …

Recent studies of myoglobin (Mb) knockout (myo−/−) mice have extended our
understanding of Mb's diverse functions and have demonstrated a complex array of …

Recent studies have suggested myoglobin (Mb) may have other cellular functions in
addition to storing and transporting O 2. Indeed, NMR experiments have shown that the …

A canonical view of the primary physiological function of myoglobin (Mb) is that it is an
oxygen (O2) storage protein supporting mitochondrial oxidative phosphorylation, especially …

The identification of novel physiological regulators that stimulate energy expenditure
through brown adipose tissue (BAT) activity in substrate catalysis is of utmost importance to …

Myoglobin is an oxygen storage molecule that is selectively expressed in cardiac and slow-
twitch skeletal muscles that have a high oxygen demand. Numerous studies have implicated …

Myoglobin (Mb) regulates O2 bioavailability in muscle and heart as the partial pressure of
O2 (Po2) drops with increased tissue workload. Globin proteins also modulate cellular NO …

Oxygen (O2) transport from air to mitochondria depends on both the mechanisms of
convection and diffusion. In the final step of the O2 cascade, from the capillary to myocyte …

Myoglobin is a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative
skeletal muscle fibers. Myoglobin is a well-characterized protein and numerous studies have …