Structure of the trehalose-6-phosphate phosphatase from Brugia malayi reveals key design principles for anthelmintic drugs. Farelli JD, Galvin BD et al. PLoS Pathog. 2014 Jul 3;10(7):e1004245.
Regulation of the mammalian elongation cycle by subunit rolling: a eukaryotic-specific ribosome rearrangement. Budkevich TV, Giesebrecht J et al. Cell. 2014 Jul 3;158(1):121-31.
Protruding knob-like proteins violate local symmetries in an icosahedral marine virus. Gipson P, Baker ML et al. Nat Commun. 2014 Jul 2;5:4278.
Enhancing UCSF Chimera through web services. Huang CC, Meng EC et al. Nucleic Acids Res. 2014 Jul;42(Web Server issue):W478-84.
Structural rearrangements of a polyketide synthase module during its catalytic cycle. Whicher JR, Dutta S et al. Nature. 2014 Jun 26;510(7506):560-4.(Previously featured citations...)
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Chimera production release 1.8.1 is now available. Changes since 1.8 are mainly to fix problems with Mac OS X 10.9 (Mavericks). See the release notes for further details and for a list of new features since the 1.7 release.(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).
A surface can be colored radially, that is, by distance from a user-specified point. Additional options include coloring by distance from an axis or a plane. Different coloring schemes can be applied.(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...)