Comparison of topological clustering within protein networks using edge metrics that evaluate full sequence, full structure, and active site microenvironment similarity. Leuthaeuser JB, Knutson ST et al. Protein Sci. 2015 Sep;24(9):1423-39.
Allosteric transcriptional regulation via changes in the overall topology of the core promoter. Philips SJ, Canalizo-Hernandez M et al. Science. 2015 Aug 21;349(6250):877-81.
A putative ATPase mediates RNA transcription and capping in a dsRNA virus. Yu X, Jiang J et al. eLife. 2015 Aug 4;4.
The molecular basis for flexibility in the flexible filamentous plant viruses. DiMaio F, Chen CC et al. Nat Struct Mol Biol. 2015 Aug;22(8):642-4.
Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation. Volkers G, Worrall LJ et al. Nat Struct Mol Biol. 2015 Aug;22(8):627-35.(Previously featured citations...)
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July 23, 2015
Chimera production release 1.10.2 is now available. Fixes include code signing for Mac OS X installation. The 1.10 series will be the last to support OS X 10.6 and 10.7. See the release notes for details.
January 9, 2015
Chimera production release 1.10.1 is now available. 64-bit builds are recommended for all capable platforms, and the 1.10 series will be the last to support OS X 10.6 and 10.7. See the release notes for details.
November 5, 2014
Chimera production release 1.10 is now available. 64-bit builds are recommended for all capable platforms, and v1.10 will be the last to support OS X 10.6 and 10.7. See the release notes for what's new.(Previous news...)
UCSF Chimera is a highly extensible program for interactive visualization and analysis of molecular structures and related data, including density maps, supramolecular assemblies, sequence alignments, docking results, trajectories, and conformational ensembles. High-quality images and animations can be generated. Chimera includes complete documentation and several tutorials, and can be downloaded free of charge for academic, government, non-profit, and personal use. Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics, funded by the National Institutes of Health (NIGMS P41-GM103311).
The default ribbon path is a smooth bspline (semitransparent tan in the figure), which can diverge from the true positions of the backbone atoms (α-carbons shown as gray balls). A cardinal spline allows tracking the backbone more closely. Without smoothing (light blue), it follows the α-carbons exactly, or it can be combined with some “compromise” smoothing of strand and/or coil. Ribbon spline options can be set with the ribspline command or in the molecule model attributes.(More features...)
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...)