Data from: Reversible, specific, active aggregates of endogenous proteins assemble upon heat stress

Wallace EWJ, Kear-Scott JL, Pilipenko EV, Schwartz MH, Laskowski PR, Rojek AE, Katanski CD, Riback JA, Dion MF, Franks AM, Airoldi EM, Pan T, Budnik BA, Drummond DA

Date Published: September 11, 2015

DOI: http://dx.doi.org/10.5061/dryad.hn16c

 

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Title S. cerevisiae protein aggregation estimates
Downloaded 49 times
Description Estimates of proportion in 100,000g supernatant (pSup) from S. cerevisiae cells grown in SC-complete media at 30C, transferred from 30C to 46C for 2, 4, and 8 min and to 37C and 42C for 8 min.
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Title S. cerevisiae protein disaggregation and synthesis estimates
Downloaded 17 times
Description Protein disaggregation and new synthesis measured by media-shift SILAC. Cells are grown on a first set of stable-isotope-labeled amino acids, shifted to media containing a second set of labels, then heat shocked at 42C for 10mins and allowed to recover at 30C for 0, 20, 60, or 180 minutes. Upon collection, these cells are mixed with cells from an unshocked (30C) reference sample grown on a third label. Protein in 100,000g supernatant fraction of lysate is measured, intensities and normalized ratios reported.
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Title Wallace2015-yeast-heat-agg-dryad-package
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Description Complete package including processed data, intermediate data, and processing scripts.
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When using this data, please cite the original publication:

Wallace EWJ, Kear-Scott JL, Pilipenko EV, Schwartz MH, Laskowski PR, Rojek AE, Katanski CD, Riback JA, Dion MF, Franks AM, Airoldi EM, Pan T, Budnik BA, Drummond DA (2015) Reversible, specific, active aggregates of endogenous proteins assemble upon heat stress. Cell 162(6): 1286–1298. http://dx.doi.org/10.1016/j.cell.2015.08.041

Additionally, please cite the Dryad data package:

Wallace EWJ, Kear-Scott JL, Pilipenko EV, Schwartz MH, Laskowski PR, Rojek AE, Katanski CD, Riback JA, Dion MF, Franks AM, Airoldi EM, Pan T, Budnik BA, Drummond DA (2015) Data from: Reversible, specific, active aggregates of endogenous proteins assemble upon heat stress. Dryad Digital Repository. http://dx.doi.org/10.5061/dryad.hn16c
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