Yeast Resource Center | Technology driven by biology.
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Collaborate with the YRC. Click to learn more.

Learn more about the technology being developed by the YRC.

Find software developed by the YRC.

Find research articles published by the YRC.


The YRC is a NIGMS Biomedical Technology Research Center based at the University of Washington in Seattle. Click to learn more about us.


Learn more about the technologies being developed by the YRC and how they are being applied to biomedical problems.


Learn how to collaborate with the YRC–leveraging our technology and expertise in your research.


Active Projects


Collaborators Since 2011


Annual NIH Dollars Impacted


YRC Publications

New Research

We are developing technology to produce biosensors based on a ligand-binding domain (LBD) that may, in principle, be applied to any target molecule. The power of this method is illustrated in this paper by development of biosensors for digoxin and progesterone.

Read more in eLIFE or in PubMed Central.


In this work, we combine the results of protein cross-linking mass spectrometry with iterative structural modelling to determine the molecular architecture of the 10-member Dam1p protein complex in S. cerevisiae. Using this technique, we can model conformational changes resulting from binding with microtubules.

Read more in Nature Communications or in PubMed Central.

Latest Publications

Hsia, Y et al. (2016) Design of a hyperstable 60-subunit protein icosahedron. Nature 535 (7610):136-9. PMID:27309817

Lyon, AS et al. (2016) Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly. Mol. Biol. Cell :. PMID:27226487

Pedros, C et al. (2016) A TRAF-like motif of the inducible costimulator ICOS controls development of germinal center TFH cells via the kinase TBK1. Nat. Immunol. 17 (7):825-33. PMID:27135603

Ma, J et al. (2016) Improved Identification and Analysis of Small Open Reading Frame Encoded Polypeptides. Anal. Chem. 88 (7):3967-75. PMID:27010111

Greenberg, CH et al. (2016) Structure of γ-tubulin small complex based on a cryo-EM map, chemical cross-links, and a remotely related structure. J. Struct. Biol. 194 (3):303-10. PMID:26968363