| Year |
Citation |
Score |
| 2024 |
Breckel CA, Johnson ZM, Hickey CM, Hochstrasser M. Yeast 26S proteasome nuclear import is coupled to nucleus-specific degradation of the karyopherin adaptor protein Sts1. Scientific Reports. 14: 2048. PMID 38267508 DOI: 10.1038/s41598-024-52352-5 |
0.587 |
|
| 2021 |
Hickey CM, Breckel C, Zhang M, Theune WC, Hochstrasser M. Protein quality control degron-containing substrates are differentially targeted in the cytoplasm and nucleus by ubiquitin ligases. Genetics. 217: 1-19. PMID 33683364 DOI: 10.1093/genetics/iyaa031 |
0.593 |
|
| 2020 |
Budenholzer L, Breckel C, Hickey CM, Hochstrasser M. The Sts1 nuclear import adaptor uses a noncanonical bipartite NLS and is directly degraded by the proteasome. Journal of Cell Science. PMID 32041904 DOI: 10.1242/Jcs.236158 |
0.617 |
|
| 2018 |
Hickey CM, Xie Y, Hochstrasser M. DNA Binding by the MATα2 Transcription Factor Controls its Access to Alternative Ubiquitin-modification Pathways. Molecular Biology of the Cell. PMID 29298839 DOI: 10.1091/Mbc.E17-10-0589 |
0.641 |
|
| 2016 |
Hickey CM. Degradation elements coincide with cofactor binding sites in a short-lived transcription factor. Cellular Logistics. 6: e1157664. PMID 27217978 DOI: 10.1080/21592799.2016.1157664 |
0.394 |
|
| 2016 |
Gillies J, Hickey CM, Su D, Wu Z, Peng J, Hochstrasser M. SUMO Pathway Modulation of Regulatory Protein Binding at the Ribosomal DNA Locus in Saccharomyces cerevisiae. Genetics. PMID 26837752 DOI: 10.1534/Genetics.116.187252 |
0.627 |
|
| 2015 |
Hickey CM, Hochstrasser M. STUbL-mediated degradation of the transcription factor MATα2 requires degradation elements that coincide with corepressor binding sites. Molecular Biology of the Cell. 26: 3401-12. PMID 26246605 DOI: 10.1091/Mbc.E15-06-0436 |
0.528 |
|
| 2012 |
Hickey CM, Wilson NR, Hochstrasser M. Function and regulation of SUMO proteases. Nature Reviews. Molecular Cell Biology. 13: 755-66. PMID 23175280 DOI: 10.1038/Nrm3478 |
0.614 |
|
| 2010 |
Hickey CM, Wickner W. HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly. Molecular Biology of the Cell. 21: 2297-305. PMID 20462954 DOI: 10.1091/Mbc.E10-01-0044 |
0.637 |
|
| 2009 |
Stroupe C, Hickey CM, Mima J, Burfeind AS, Wickner W. Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components. Proceedings of the National Academy of Sciences of the United States of America. 106: 17626-33. PMID 19826089 DOI: 10.1073/Pnas.0903801106 |
0.629 |
|
| 2009 |
Hickey CM, Stroupe C, Wickner W. The major role of the Rab Ypt7p in vacuole fusion is supporting HOPS membrane association. The Journal of Biological Chemistry. 284: 16118-25. PMID 19386605 DOI: 10.1074/Jbc.M109.000737 |
0.648 |
|
| 2008 |
Mima J, Hickey CM, Xu H, Jun Y, Wickner W. Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones. The Embo Journal. 27: 2031-42. PMID 18650938 DOI: 10.1038/Emboj.2008.139 |
0.635 |
|
| 2008 |
Starai VJ, Hickey CM, Wickner W. HOPS proofreads the trans-SNARE complex for yeast vacuole fusion. Molecular Biology of the Cell. 19: 2500-8. PMID 18385512 DOI: 10.1091/Mbc.E08-01-0077 |
0.635 |
|
| 2007 |
Fratti RA, Collins KM, Hickey CM, Wickner W. Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification. The Journal of Biological Chemistry. 282: 14861-7. PMID 17400548 DOI: 10.1074/Jbc.M700971200 |
0.658 |
|
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