ReviewFrontiers in oncology2026
MYO1B in human disease: an actin-based motor linking membrane trafficking to oncogenic signaling, metastasis, and vascular aging.
Review in Frontiers in oncology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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8 authors.
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Abstract
Myosins move along actin filaments by breaking down adenosine triphosphate (ATP) and using the energy it gives out. The superfamily presently has more than 35 classes. Mammals have the most frequent and well-preserved kind of myosin, which is class I (Myo1). People commonly group these isoforms by the morphology of their tails: long-tailed (like MYO1B, C, D), short-tailed, and tail-less. MYO1B is different from the others in that it has a lengthy tail but no second actin-binding domain. MYO1B is not evenly spread out in the body. Instead, it is mostly present near the edges of actin-rich plasma membranes and throughout the endolysosomal system, which includes early endosomes and lysosomes. It is vital for numerous bodily activities because it is located in several places, like the brain, heart, liver, and kidneys. This article brings together recent research on MYO1B's structure, signaling pathways, and disease-causing effects. Its goal is to be a complete source for future study.
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