Draft:Todd Yeates
Submission declined on 26 July 2024 by SafariScribe (talk). This submission is not adequately supported by reliable sources. Reliable sources are required so that information can be verified. If you need help with referencing, please see Referencing for beginners and Citing sources. This submission's references do not show that the subject qualifies for a Wikipedia article—that is, they do not show significant coverage (not just passing mentions) about the subject in published, reliable, secondary sources that are independent of the subject (see the guidelines on the notability of people). Before any resubmission, additional references meeting these criteria should be added (see technical help and learn about mistakes to avoid when addressing this issue). If no additional references exist, the subject is not suitable for Wikipedia.
Where to get help
How to improve a draft
You can also browse Wikipedia:Featured articles and Wikipedia:Good articles to find examples of Wikipedia's best writing on topics similar to your proposed article. Improving your odds of a speedy review To improve your odds of a faster review, tag your draft with relevant WikiProject tags using the button below. This will let reviewers know a new draft has been submitted in their area of interest. For instance, if you wrote about a female astronomer, you would want to add the Biography, Astronomy, and Women scientists tags. Editor resources
| ![]() |
Comment: Please cut down the list of 'Published works' significantly – Wikipedia is not intended as a comprehensive catalogue of someone's entire output; focus on the most notable ones only (I'd say ideally fewer than ten). DoubleGrazing (talk) 12:55, 26 July 2024 (UTC)
Todd O. Yeates | |
---|---|
Born | 1961 |
Occupation(s) | American biophysicist and structural biologist |
Todd Owen Yeates (1961 –) Todd Yeates was a Professor at the University of California Los Angeles, from 1990 to 2024. In 2001 his research laboratory invented the field of designed protein cages [1][2][3][4] Designed protein cages are engineered molecular nanoparticles that self-assemble into geometric shapes reminiscent of the Platonic solids (e.g. a cube, tetrahedron, or icosahedron). They have found diverse applications in medicine and biotechnology. Beginning in 2005, his research laboratory elucidated the three-dimensional structures of bacterial microcompartments (known as BMCs or MCPs) [5][6][7][8][9]. Bacterial microcompartments assemble from thousands of hexagonal and pentagonal protein components to form a shell, reminiscent of a large viral capsid, with enzymes encapsulated in the interior and selective pores in the shell that allow passage of enzyme substrates and products. Bacterial microcompartments modify the textbook view of cell biology by highlighting an alternative type of metabolic organelle, one based on a protein shell rather than a lipid membrane, the latter being a defining feature of organelles found in eukaryotic (plant and animal) cells. Yeates’ research led to methodological advances in X-ray crystallography[10][11] and cryo-electron microscopy[12]. From 2019 to 2023 he served as the Director of the US Department of Energy Institute for Genomics and Proteomics.
References/Notes and references
[edit]- ^ Padilla JE, Colovos C, Yeates TO. Nanohedra: using symmetry to design self assembling protein cages, layers, crystals, and filaments. Proc Natl Acad Sci USA. 2001 Feb 27;98(5):2217-21. doi: 10.1073/pnas.041614998.
- ^ Yeates TO, Padilla JE. Designing supramolecular protein assemblies. Curr Opin Struct Biol. 2002 Aug;12(4):464-70. doi: 10.1016/s0959-440x(02)00350-0
- ^ Lai YT, Cascio D, Yeates TO. Structure of a 16-nm cage designed by using protein oligomers. Science. 2012 Jun 1;336(6085):1129. doi:10.1126/science.1219351.
- ^ Yeates TO. Geometric Principles for Designing Highly Symmetric Self-Assembling Protein Nanomaterials. Annu Rev Biophys. 2017 May 22;46:23-42. doi:10.1146/annurev-biophys-070816-033928. .
- ^ Yeates TO, Kerfeld CA, Heinhorst S, Cannon GC, Shively JM. Protein-based organelles in bacteria: carboxysomes and related microcompartments. Nat Rev Microbiol. 2008 Sep;6(9):681-91. doi: 10.1038/nrmicro1913
- ^ Kerfeld CA, Sawaya MR, Tanaka S, Nguyen CV, Phillips M, Beeby M, Yeates TO. Protein structures forming the shell of primitive bacterial organelles. Science. 2005 Aug 5;309(5736):936-8. doi: 10.1126/science.1113397.
- ^ Tsai Y, Sawaya MR, Cannon GC, Cai F, Williams EB, Heinhorst S, Kerfeld CA, Yeates TO. Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysome. PLoS Biol. 2007 Jun;5(6):e144. doi:10.1371/journal.pbio.0050144.
- ^ Tanaka S, Kerfeld CA, Sawaya MR, Cai F, Heinhorst S, Cannon GC, Yeates TO. Atomic-level models of the bacterial carboxysome shell. Science. 2008 Feb 22;319(5866):1083-6. doi: 10.1126/science.1151458.
- ^ Tanaka S, Sawaya MR, Yeates TO. Structure and mechanisms of a protein-based organelle in Escherichia coli. Science. 2010 Jan 1;327(5961):81-4. doi:10.1126/science.1179513
- ^ Padilla JE, Yeates TO. A statistic for local intensity differences: robustness to anisotropy and pseudo-centering and utility for detecting twinning. Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1124-30. doi:10.1107/s0907444903007947
- ^ Yeates TO, Kent SB. Racemic protein crystallography. Annu Rev Biophys. 2012;41:41-61. doi: 10.1146/annurev-biophys-050511-102333
- ^ Castells-Graells R, Meador K, Arbing MA, Sawaya MR, Gee M, Cascio D, Gleave E, Debreczeni JÉ, Breed J, Leopold K, Patel A, Jahagirdar D, Lyons B, Subramaniam S, Phillips C, Yeates TO. Cryo-EM structure determination of small therapeutic protein targets at 3 Å-resolution using a rigid imaging scaffold. Proc Natl Acad Sci U S A. 2023 Sep 12;120(37):e2305494120. doi:10.1073/pnas.2305494120.