Xueliang Ge
Forskare vid Institutionen för cell- och molekylärbiologi; Molekylärbiologi
- E-post:
- xueliang.ge@icm.uu.se
- Besöksadress:
- Husargatan 3
752 37 Uppsala - Postadress:
- Box 596
751 24 Uppsala
Mer information visas för dig som medarbetare om du loggar in.
Kort presentation
Denna text finns inte på svenska, därför visas den engelska versionen.
Senior Researcher of Molecular Biology. My research is focused on protein synthesis in bacteria include translation initiation, regulation of elongation and termination.
Biografi
20 14 to now Senior researcher, In Dept. of Cell & Molecular biology, BMC Uppsala University, Sweden
20 10 to 2014 Post doc. In Dept. of Cell & Molecular biology, BMC Uppsala University, Sweden
2007 to 2010 Ph.D. in Molecular Cell Biology , Northeast Forestry University, PR China
2004 to 2007 Master in Molecular Cell Biology , Northeast Forestry University PRChina
Forskning
My research studies mechanisms of protein synthesis in bacteria and the effect of antibiotics on protein translation. I am particularly interested in the research project below.
- The molecular mechanisms of protein synthesis in E. coli and M. smegmatis .
- Design and application of high throughput in vitro reconstituted protein translation system to low molecular weight compound screening.
- Mechanism of ribosome assembly in E. coli .
- Characterization of ribosomal stalk bL12 on protein translation and the development of anti-L12 drug.
- The mechanism of methylation and phosphorylation of translation factor on the regulation of translation in bacteria.
- The mechanism of bacterial environmental stress factors on the regulation of protein translation.
Publikationer
Senaste publikationer
- Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome (2023)
- Phytochemicals with activity against methicillin-resistant Staphylococcus aureus (2022)
- Uncovering translation roadblocks during the development of a synthetic tRNA (2022)
- GGQ methylation enhances both speed and accuracy of stop codon recognition by bacterial class-I release factors (2021)
- Collateral toxicity limits the evolution of bacterial Release Factor 2 towards total omnipotence (2020)
Alla publikationer
Artiklar
- Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome (2023)
- Phytochemicals with activity against methicillin-resistant Staphylococcus aureus (2022)
- Uncovering translation roadblocks during the development of a synthetic tRNA (2022)
- GGQ methylation enhances both speed and accuracy of stop codon recognition by bacterial class-I release factors (2021)
- Collateral toxicity limits the evolution of bacterial Release Factor 2 towards total omnipotence (2020)
- Selective translation by alternative bacterial ribosomes (2020)
- Loss of a single methylation in 23S rRNA delays 50S assembly at multiple late stages and impairs translation initiation and elongation (2020)
- Inhibition of translation termination by small molecules targeting ribosomal release factors (2019)
- Complementary charge-based interaction between the ribosomal-stalk protein L7/12 and IF2 is the key to rapid subunit association (2018)
- Cryo-EM structure of Mycobacterium smegmatis ribosome reveals two unidentified ribosomal proteins close to the functional centers (2018)
- Experimental Evolution of Escherichia coli Harboring an Ancient Translation Protein (2017)
- Spatial Distribution and Ribosome-Binding Dynamics of EF-P in Live Escherichia coli (2017)
- New melanocortin-like peptide of E. coli can suppress inflammation via the mammalian melanocortin-1 receptor (MC1R) (2017)
- Micrococcin P1-A bactericidal thiopeptide active against Mycobacterium tuberculosis (2016)
- Organization of Ribosomes and Nucleoids in Escherichia coli Cells during Growth and in Quiescence (2014)
- Bacterial ribosome requires multiple L12 dimers for efficient initiation and elongation of protein synthesis involving IF2 and EF-G (2012)
- The extended substrate recognition profile of the dog mast cell chymase reveals similarities and differences to the human chymase (2010)
- Structural mechanism of FusB-mediated rescue from fusidic acid inhibition of protein synthesis
- An extended C-terminal tail of the ribosomal protein S13 modulates the speed of ribosomal translocation.