ArticleMethods in molecular biology (Clifton, N.J.)2026
Structures of Myxobacterial Phytochrome Revealed by Cryo-EM.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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Who cites it
1 citing paper in PubMed.
- A bacteriophytochrome Pr/Pfr heterodimer studied through single-particle time-resolved cryo-electron microscopy.Communications chemistry · 2026Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Phytochromes are red-light photoreceptors first identified in plants, with homologs found in bacteria and fungi that regulate a variety of critical physiological processes. They undergo a reversible photocycle between two distinct states: a red-light-absorbing phytochrome (Pr) form and a far-red light-absorbing phytochrome (Pfr) form. This Pr-to-Pfr photoconversion controls the activity of a C-terminal enzymatic domain, typically a histidine kinase (HK). The molecular mechanisms underlying light-induced regulation of HK activity in bacteria remain poorly understood, as structures of unmodified bacterial phytochromes with HK activity were unknown until recently. Here, we report details of using cryogenic electron microscopy (cryo-EM) to determine the structure of an intact (full-length) bacteriophytochrome.
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