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Polymerase trapping as the mechanism of H5 highly pathogenic avian influenza virus genesis. Funk M, Spronken MI et al. Science. 2026 Mar 12;391(6790):eadr6632.
Identification of an allosteric site on the E3 ligase adapter cereblon. Dippon VN, Rizvi Z et al. Nature. 2026 Mar 12;651(8105):482-490.
Structural remodeling of the mitochondrial protein biogenesis machinery under proteostatic stress. Ehses K, López-Alonso JP et al. Sci Adv. 2026 Mar 6;12(10):eaed3579.
Structures of Ostα/β reveal a unique fold and bile acid transport mechanism. Yang X, Cui N et al. Nature. 2026 Mar 5;651(8104):260–267.
Structure and mechanism of the human bile acid transporter OSTα-OSTβ. Wang K, Fan J et al. Nature. 2026 Mar 5;651(8104):251–259
Previously featured citations...Chimera Search
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December 25, 2025
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September 22, 2025
Mac users may wish to defer upgrading to MacOS Tahoe. Currently on that OS the Chimera graphics window is shifted so that it covers the command and status lines.
March 6, 2025
Chimera production release 1.19 is now available, fixing the ability to fetch structures from the PDB (1.19 release notes).
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UCSF Chimera is a program for the interactive visualization and analysis of molecular structures and related data, including density maps, trajectories, and sequence alignments. It is available free of charge for noncommercial use. Commercial users, please see Chimera commercial licensing.
We encourage Chimera users to try ChimeraX for much better performance with large structures, as well as other major advantages and completely new features in addition to nearly all the capabilities of Chimera (details...).
Chimera is no longer under active development. Chimera development was supported by a grant from the National Institutes of Health (P41-GM103311) that ended in 2018.
Feature Highlight
Protein backbone angles can be shown in a Ramachandran Plot along with probability contours (green lines) from a reference set of well-determined structures. Each amino acid residue is shown as a dot in a graph of φ vs. ψ, more commonly known as a Ramachandran plot or Ramachandran map. Residues are shown as blue dots, or when selected, as red dots. In the example, all helix residues have been selected. Conversely, clicking a dot in the plot will select the corresponding residue in the structure. When the plot has mouse focus, the cursor position (x = φ, y = ψ) is reported under the plot.
(More features...)
Gallery Sample
Mutations that inactivate the tumor suppressor p53 are found in over 50% of human cancers, and most of the cancer-associated mutations are within its DNA-binding domain. The image shows a tetramer of the p53 DNA-binding domain complexed with DNA (Protein Data Bank entry 2ac0). The tetramer subunits are shown as light blue, green, orange, and yellow ribbons, with red spheres marking several major "hot spots" of mutation. The DNA is shown in purple and blue. (More samples...)
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