User:Christopher Berndsen/Labinfo
From Proteopedia
| Line 1: | Line 1: | ||
==The Berndsen Laboratory at James Madison University== | ==The Berndsen Laboratory at James Madison University== | ||
| - | < | + | <Structure load='1WXS' size='350' frame='true' align='right' caption='NMR Structure of the ubiquitin-like protein UFM1' scene='Insert optional scene name here' /> |
The Berndsen Lab is located in the [http://www.jmu.edu/chemistry/ Department of Chemistry and Biochemistry] at [http://www.jmu.edu James Madison University] in Harrisonburg, VA. The primary research focus is the mechanism enzymes involved in the conjugation and processing of ubiquitin and ubiquitin-like proteins. Additionally, the lab is interested in integrating protein structure research and molecular basis for disease into the biochemistry classroom. | The Berndsen Lab is located in the [http://www.jmu.edu/chemistry/ Department of Chemistry and Biochemistry] at [http://www.jmu.edu James Madison University] in Harrisonburg, VA. The primary research focus is the mechanism enzymes involved in the conjugation and processing of ubiquitin and ubiquitin-like proteins. Additionally, the lab is interested in integrating protein structure research and molecular basis for disease into the biochemistry classroom. | ||
== Research Highlights == | == Research Highlights == | ||
| - | Ubiquitin and Ubiquitin-like proteins are linked to many cellular functions included protein degradation and DNA damage repair <ref>PMID:15571809</ref><ref>PMID:24699078</ref>. The Berndsen Lab is interested in the catalytic mechanisms the conjugating enzymes E1, E2, and E3 use to attach ubiquitin/ubiquitin-like proteins to the substrate lysine. We are also interested in the proteases that remove these modifications and the chemical mechanism(s) of catalysis. We are currently focusing on UFM1 | + | Ubiquitin and Ubiquitin-like proteins are linked to many cellular functions included protein degradation and DNA damage repair <ref>PMID:15571809</ref><ref>PMID:24699078</ref>. The Berndsen Lab is interested in the catalytic mechanisms the conjugating enzymes E1, E2, and E3 use to attach ubiquitin/ubiquitin-like proteins to the substrate lysine. We are also interested in the proteases that remove these modifications and the chemical mechanism(s) of catalysis. We are currently focusing on UFM1 and the E1 enzymes associated with UFM1, UBA5[[3H8V]]. |
| - | + | ||
== Disease == | == Disease == | ||
Revision as of 19:59, 1 March 2016
Contents |
The Berndsen Laboratory at James Madison University
|
The Berndsen Lab is located in the Department of Chemistry and Biochemistry at James Madison University in Harrisonburg, VA. The primary research focus is the mechanism enzymes involved in the conjugation and processing of ubiquitin and ubiquitin-like proteins. Additionally, the lab is interested in integrating protein structure research and molecular basis for disease into the biochemistry classroom.
Research Highlights
Ubiquitin and Ubiquitin-like proteins are linked to many cellular functions included protein degradation and DNA damage repair [1][2]. The Berndsen Lab is interested in the catalytic mechanisms the conjugating enzymes E1, E2, and E3 use to attach ubiquitin/ubiquitin-like proteins to the substrate lysine. We are also interested in the proteases that remove these modifications and the chemical mechanism(s) of catalysis. We are currently focusing on UFM1 and the E1 enzymes associated with UFM1, UBA53H8V.
Disease
Relevance
Structural highlights
</StructureSection>
References
- ↑ Pickart CM, Eddins MJ. Ubiquitin: structures, functions, mechanisms. Biochim Biophys Acta. 2004 Nov 29;1695(1-3):55-72. PMID:15571809 doi:http://dx.doi.org/10.1016/j.bbamcr.2004.09.019
- ↑ Berndsen CE, Wolberger C. New insights into ubiquitin E3 ligase mechanism. Nat Struct Mol Biol. 2014 Apr;21(4):301-7. doi: 10.1038/nsmb.2780. PMID:24699078 doi:http://dx.doi.org/10.1038/nsmb.2780
