Elizabeth Vierling教授学术报告

日期: 2017-11-13 阅读: 来源:

    2017年11月13日马萨诸塞大学杰出教授Elizabeth Vierling前来我校进行学术交流,欢迎广大师生参加。

题  目:Controlling Protein folding and reactive oxygen species: Keys to plant stress tolerance

时  间:2017年11月13日 9:00

地  点:逸夫生物楼301

报告人:伊丽莎白 威尔林(ELIZABETH VIERLING

报告人简介:Elizabeth Vierling,马萨诸塞大学杰出教授,主要从事植物对高温胁迫的耐受机理的研究,在Nature、PNAS、Plant Cell等知名期刊发表植物耐热论文100余篇,对热激蛋白在植物耐热过程中的功能与作用机理有深入系统的研究。

教育背景:

1982-85 博士后, 乔治亚大学;

1982 博士学位, 芝加哥大学;

1979 硕士学位, 芝加哥大学;

1975 学士学位, 密歇根大学。

工作经历:

2013 杰出教授, 马萨诸塞大学

2011 教授,马萨诸塞大学;冠名教授(Regents’ Professor Emerita), 亚利桑那大学

2008 冠名教授(Regents’ Professor), 亚利桑那大学

1996 教授,亚利桑那大学

1991 副教授,亚利桑那大学

1985 助教授,亚利桑那大学

代表论文:

Liyuan Zhang, Xinye Liu, Kishor Gaikwad, Xiaoxia Kou, Fei Wang, Xuejun Tian, Mingming Xin, Zhongfu Ni, Qixin Sun, Huiru Peng, Elizabeth Vierling.  Growth and thermotolerance phenotypes of eIF5B mutants.  The Plant Cell Online Aug 2017, tpc.00808.2016; DOI: 10.1105/tpc.16.00808

McLoughlin F, Basha E, Fowler ME, Kim M, Bordowitz J, Katiyar-Agarwal S, Vierling E. Class I and II Small Heat Shock Proteins Together with HSP101 Protect Protein Translation Factors during Heat Stress. Plant Physiol. 2016 Oct;172(2):1221-1236. PMID: 27474115

Kim, M., U. Lee, I. Small, C. des Francs-Small, E. Vierling. Mutations in a mitochondrial transcription termination factor (mTERF)-related protein enhance thermotolerance in the absence of the major molecular chaperone HSP101. Plant Cell, 24:3349-65 (2012). PMID: 22942382 PMCID: PMC3462636
Basha, E., H. O’Neill, E. Vierling. Small Heat Shock Proteins/α-crystallins:Dynamic proteins with flexible functions. Trends Biochem. Sci. 37:106-117 (2012).
Jaya, N., V. Garcia, E. Vierling. Substrate binding site flexibility of the small heat shock protein molecular chaperones. Proc. Natl. Acad. Sci. 106:15604-15609 (2009)
Cheng, G., E. Basha, V.H. Wysocki, E. Vierling. Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry. J. Biol. Chem., 283:26634-42 (2008) Featured as “Paper of the Week”. PMID: 18621732
Lee, U., C.Wie*, B. O. Fernandez, M. Feelisch, E. Vierling. Modulation of nitrosative stress by S-nitrosoglutathione reductase is critical for thermotolerance and plant growth. Plant Cell 20: 786-802, (2008).
Tonsor, S.J., C. Scott, I. Boumanza*, T.R. Liss, J.L. Brodsky, E. Vierling. Heat shock protein 101 effects in Arabidopsis thaliana: Genetic variation, fitness and pleiotropy in controlled environments. Mol. Ecol., 17: 1614-1626 (2008).
Larkindale, J., E. Vierling. Core genome responses involved in acclimation to high temperature. Plant Physiol. 146: 748-761 (2008).
Schramm, F., J. Larkindale, K. Kiehlmann, G. Arnab, G. Englich, G., E. Vierling, P. von Koskull-Döring. A cascade of transcription factor DREB2A and heat stress transcription factor HsfA3 regulates the heat stress response of Arabidopsis. Plant J. 53: 264-274 (2008).
McClellan, C.A., T.J. Turbeyville, E.M. K. Wijeratne, A. Kerschen, E. Vierling, C. Queitsch, L. Whitesell, A.A. Gunatilaka. A rhizosphere fungus enhances Arabidopsis thermotolerance through production of an Hsp90 inhibitor. Plant Physiol 145: 174-182 (2007). Highlighted in Science Stke http://stke.sciencemag.org/cgi/content/abstract/sigtrans;2007/403/tw333
Lee, U., I. Rioflorido, S-W. Hong, J. Larkindale, E. R.Waters, E.Vierling. The Arabidopsis ClpB/Hsp100 family of proteins: Chaperones for stress and chloroplast development. Plant Journal 49:115-127 (2007).
Giese, K.C., E. Basha, B.Y. Catague, E. Vierling. Evidence for an essential function of the N-terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity. Proc. Natl. Acad. Sci. 102: 18896-18901 (2005).
Larkindale, J. J, D. Hall, M. R. Knight, E. Vierling. Heat stress phenotypes of Arabidopsis mutants implicate multiple signaling pathways in the acquisition of thermotolerance. Plant Physiol., 138:882-97 (2005).
Lee,U., C. Wie*, M. Escobar, B. Williams, S.-W. Hong, E. Vierling. Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the sHsp chaperone system. Plant Cell, 17:559-571 (2005).

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