Stephanie Carmicle
About Me
Ubiquitination plays an important role in regulating the intracellular localization and lifetime cellular proteins. As a result, it is an important mechanism by which the cell can regulate many of its processes, e.g. cell cycle progression, activation and cell division. Defects in ubiquitination can result in human disease. The ubiquitination machinary is made of many proteins working in concert to "tag" proteins with ubiquitin. E3 ligases are important because they serve as the part of the machine that recruits protein substrates that will be ubiquitinated. My research interests include characterizing the role of these E3 ligases in cellular processes and understanding the contribution of E3 ligases to both autoimmunity and cancer.
Class Schedule
Fall 2012
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Bio 307 - Cell Biology and Genetics Lab
M 2:30-3:30 T3:30-5 W 1:30-3, , Hederman 202 -
Bio 442,44 - Cancer Immunology Research
T, 10:50AM to 3:30 PM, H200 -
BIO 410/54 - Human Gross Anatomy Lecture and Lab
TR 8-9:25 am and R 1:30-3:30 pm, , H100
Documents
Bio 442,44 Documents
Other Documents
- Exam wrapper
- The characterization of Ring Finger Protein 13 (RNF13) in melanocytes, Molecular Biology Fall 2010, Final Poster