李文斐
Professor Supervisor of Doctorate Candidates Supervisor of Master's Candidates
Name (Simplified Chinese):李文斐
Name (Pinyin):liwenfei
E-Mail:wenfeili@sdu.edu.cn
Date of Employment:2021-02-01
School/Department:Shandong University, School of Basic Medical Sciences
Administrative Position:Professor
Education Level:Postgraduate (Postdoctoral)
Business Address:School of Basic Medical Sciences， Shandong University
Gender:Female
Contact Information:wenfeili@sdu.edu.cn
Degree:Doctor
Status:Employed
Academic Titles:医学结构生物学中心副主任
Alma Mater:Tsinghua University
Whether on the job:1
Discipline:Biochemistry and Molecular Biology
Cell Biology
Biophysics
Genetics
Academic Honor:
Honors and Titles:
2022-12-22 BMS本科生优秀班主任
2022-06-06 泰山学者青年专家
2021-02-01 齐鲁青年学者（第一层次）
2022-04-01 山东省优秀青年（海外）
2015-07-06 北京市优秀毕业生
2009-12-01 北京市大学生科学研究与创业
2015-07-06 博士生毕业论文奖
2013-03-06 清华大学学生实验室建设贡献二等奖
国家奖学金
Hits:
Journal:Nature Structural&molecular biology
Key Words:The drug-like molecule PF-06446846 (PF846) binds the human ribosome and selectively blocks the translation of a small number of proteins by an unknown mechanism. In structures of PF846-stalled human ribosome nascent chain complexes, PF846 binds in the ribosome exit tunnel in a eukaryotic-specific pocket formed by 28S ribosomal RNA, and alters the path of the nascent polypeptide chain. PF846 arrests the translating ribosome in the rotated state of translocation, in which the peptidyltransfer RNA 3!-CCA end is improperly docked in the peptidyl transferase center. Selections of messenger RNAs from mRNA libraries using translation extracts reveal that PF846 can stall translation elongation, arrest termination or even enhance translation, depending on nascent chain sequence context. These results illuminate how a small molecule selectively targets translation by the human ribosome, and provides a foundation for developing small molecules that modulate the production of proteins of therapeutic interest.
Abstract:The drug-like molecule PF-06446846 (PF846) binds the human ribosome and selectively blocks the translation of a small number
of proteins by an unknown mechanism. In structures of PF846-stalled human ribosome nascent chain complexes, PF846
binds in the ribosome exit tunnel in a eukaryotic-specific pocket formed by 28S ribosomal RNA, and alters the path of the
nascent polypeptide chain. PF846 arrests the translating ribosome in the rotated state of translocation, in which the peptidyltransfer
RNA 3!-CCA end is improperly docked in the peptidyl transferase center. Selections of messenger RNAs from mRNA
libraries using translation extracts reveal that PF846 can stall translation elongation, arrest termination or even enhance translation,
depending on nascent chain sequence context. These results illuminate how a small molecule selectively targets translation
by the human ribosome, and provides a foundation for developing small molecules that modulate the production of proteins
of therapeutic interest.
All the Authors:Ward, K. McClure, S. Chang, E. Montabana, S. Liras, R. Dullea
First Author:Wenfei Li*
Correspondence Author:J. Cate#
Volume:26
Issue:6
Page Number:501-509
Translation or Not:no
Date of Publication:2019-06-01
