Brenda Schilke
Affiliations: | 1988-1994 | Bacteriology | University of Wisconsin, Madison, Madison, WI |
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"Brenda Schilke"
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| Ciesielski SJ, Schilke BA, Stolarska M, et al. (2024) Comparative structural and functional analysis of the glycine-rich regions of Class A and B J-domain protein cochaperones of Hsp70. Febs Letters |
| Ziegelhoffer T, Verma AK, Delewski W, et al. (2024) NAC and Zuotin/Hsp70 chaperone systems coexist at the ribosome tunnel exit in vivo. Nucleic Acids Research |
| Jelen M, Grochowina I, Grabinska-Rogala A, et al. (2023) Analysis of reconstituted tripartite complex supports avidity-based recruitment of Hsp70 by substrate bound J-domain protein. Journal of Molecular Biology. 168283 |
| Uzarska MA, Grochowina I, Soldek J, et al. (2022) During FeS cluster biogenesis, ferredoxin and frataxin use overlapping binding sites on yeast cysteine desulfurase Nfs1. The Journal of Biological Chemistry. 298: 101570 |
| Schilke BA, Craig EA. (2021) Essentiality of Sis1, a J-domain protein Hsp70 cochaperone, can be overcome by Tti1, a specialized PIKK chaperone. Molecular Biology of the Cell. mbcE21100493 |
| Tomiczek B, Delewski W, Nierzwicki L, et al. (2020) Two-step mechanism of J-domain action in driving Hsp70 function. Plos Computational Biology. 16: e1007913 |
| Kleczewska M, Grabinska A, Jelen M, et al. (2020) Biochemical Convergence of Mitochondrial Hsp70 System Specialized in Iron-Sulfur Cluster Biogenesis. International Journal of Molecular Sciences. 21 |
| Schilke BA, Ciesielski SJ, Ziegelhoffer T, et al. (2017) Broadening the functionality of a J-protein/Hsp70 molecular chaperone system. Plos Genetics. 13: e1007084 |
| Ting SY, Yan NL, Schilke BA, et al. (2017) Dual interaction of scaffold protein Tim44 of mitochondrial import motor with channel-forming translocase subunit Tim23. Elife. 6 |
| Ciesielski SJ, Schilke B, Marszalek J, et al. (2016) Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe-S cluster biogenesis regulation. Molecular Biology of the Cell. 27: 1060-8 |