2015.9-至今：中国科学院生物与化学交叉研究中心，研究员、课题组长
2015-2015：普罗简那有限公司，研究员
2013-2015：耶鲁大学医学院，副研究科学家
2009-2012：美国国立卫生研究院，博士后
2004-2009：中国科学院生物物理研究所，生物化学博士
2000-2004：山东大学生命科学学院，学士
主要研究细胞内蛋白质降解（protein degradation）的各种机制、以及内质网维持其蛋白质及膜组分稳态平衡的分子机理。目标是理解有错误折叠倾向的蛋白在细胞内沉积的机制，了解它们为何持续存留在老化的细胞内，并且发展出有效的策略来减轻错误折叠蛋白对细胞或机体组织造成的负担或损伤。我们将综合应用生物化学、细胞生物学、生物物理学，并结合蛋白质组学和高分辨率成像等技术，研究以下基本问题：
1. 错误折叠的跨膜蛋白被质量控制系统识别(recognition)、分选(triage)、泛素化修饰 (ubiquitination)、并传递到蛋白酶体(proteasome)或溶酶体(lysosome)进行降解 (degradation)的分子机制。
2. 内质网与细胞核进行有效的信息交流从而使细胞能够对抗蛋白质错误折叠或聚集的分子机制。
3. O-联接糖基化 (O-GlcNAc glycosylation) 等翻译后修饰方式对内质网蛋白质稳态的调控机制及其与机体寿命的关系。
1. Plumb R*, Zhang ZR*, Appathurai S, &Mariappan M. (2015) A functional link between the co-translational protein translocation pathway and the UPR. eLife 4: e07426 (*Co-first authors)
2. Park SY, Waheed AA, Zhang ZR, Freed EO, & Bonifacino JS.(2014) HIV-1 Vpu accessory protein induces caspase-mediated cleavage of IRF3 transcription factor.J. Biol. Chem. 289, 35102-35110
3. Zhang ZR*, Bonifacino JS, &Hegde RS*. (2013) Deubiquitinases Sharpen Substrate Discrimination during Membrane Protein Degradation from the ER. Cell 154, 609-622 (* Co-corresponding authors)
4. Moran C, Kinsella GK, Zhang ZR, Perrett S, & Jones GW. (2013) Mutational Analysis of Sse1 (Hsp110) Suggests an Integral Role for this Chaperone in Yeast Prion Propagation In Vivo. G3: Genes, Genomes, Genetics 3, 1409-1418
5. Emerman AB, Zhang ZR,Chakrabarti O, &Hegde RS. (2010). Compartment-restricted biotinylation reveals novel features of prion protein metabolism in vivo. Mol. Biol. Cell 21, 4325-4337
6. Zhang C, Jackson A, Zhang ZR, Han Y, Yu S, He RQ, and Perrett S. (2010). Amyloid-Like aggregates of the yeast prion protein Ure2 enter vertebrate cells by specific endocytotic pathways and induce apoptosis. PLoS One 5, e12529
7. Zhang ZR, and Perrett S. (2009). Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils. J. Biol. Chem.284, 14058-14067
8. Wang XY, Zhang ZR, and Perrett S. (2009). Characterization of the activity and folding of the glutathione transferase from Escherichia coli and the roles of residues Cys10 and His106. Biochem. J.417, 55-64
9. Zhang ZR, Bai M, Wang XY, Zhou JM & Perrett S. (2008). "Restoration" of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2. J. Mol. Biol. 384, 641-651
10. Lian HY, Zhang H, Zhang ZR, Loovers HM, Jones GW, Rowling PJ, Itzhaki LS, Zhou JM & Perrett S. (2007). Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils. J. Biol. Chem. 282, 11931-11940
