Relevant Degree Programs
Complete these steps before you reach out to a faculty member!
- Familiarize yourself with program requirements. You want to learn as much as possible from the information available to you before you reach out to a faculty member. Be sure to visit the graduate degree program listing and program-specific websites.
- Check whether the program requires you to seek commitment from a supervisor prior to submitting an application. For some programs this is an essential step while others match successful applicants with faculty members within the first year of study. This is either indicated in the program profile under "Requirements" or on the program website.
- Identify specific faculty members who are conducting research in your specific area of interest.
- Establish that your research interests align with the faculty member’s research interests.
- Read up on the faculty members in the program and the research being conducted in the department.
- Familiarize yourself with their work, read their recent publications and past theses/dissertations that they supervised. Be certain that their research is indeed what you are hoping to study.
- Compose an error-free and grammatically correct email addressed to your specifically targeted faculty member, and remember to use their correct titles.
- Do not send non-specific, mass emails to everyone in the department hoping for a match.
- Address the faculty members by name. Your contact should be genuine rather than generic.
- Include a brief outline of your academic background, why you are interested in working with the faculty member, and what experience you could bring to the department. The supervision enquiry form guides you with targeted questions. Ensure to craft compelling answers to these questions.
- Highlight your achievements and why you are a top student. Faculty members receive dozens of requests from prospective students and you may have less than 30 seconds to pique someone’s interest.
- Demonstrate that you are familiar with their research:
- Convey the specific ways you are a good fit for the program.
- Convey the specific ways the program/lab/faculty member is a good fit for the research you are interested in/already conducting.
- Be enthusiastic, but don’t overdo it.
G+PS regularly provides virtual sessions that focus on admission requirements and procedures and tips how to improve your application.
Graduate Student Supervision
Doctoral Student Supervision (Jan 2008 - Nov 2019)
Colorectal cancer (CRC) is the third leading cause of cancer mortality worldwide. The primary cause of treatment failure is the emergence of drug resistance in CRC following chemotherapy. Therefore, understanding the molecular mechanisms underlying chemoresistance in CRC is necessary for the development of effective anti-cancer therapy. We previously identified matricellular protein SPARC as a chemosensitizing agent that promotes apoptosis in CRC chemotherapy. To further understand the mechanisms by which SPARC exerts its chemosensitizing functions in CRC cells, we conducted immunoprecipitation followed by tandem mass spectrometry (MS/MS) analysis and identified GRP78- an endoplasmic reticulum (ER)- resident stress modulator- as a putative binding protein of SPARC. We found that SPARC is able to sensitize CRC cells under chemotherapy to ER stress-associated death by lowering the activation threshold of ER stress signaling via its interaction with GRP78. Notably, it was observed that a relatively higher ratio of GRP78 to SPARC expression correlated to shorter overall survival in patients with CRC, suggesting this finding is relevant clinically. Another SPARC-binding protein identified in the MS/MS analysis was ER-resident protein HSP47. As HSP47 is mostly unexplored in cancer, we focused on understanding the biology behind the role of HSP47 in CRC, especially its effects in relation to the chemotherapeutic response. We found that HSP47 is upregulated in CRC human tissues, and the expression of HSP47 promotes the resistance in CRC cells exposed to 5-fluorouracil (5-FU) by inhibiting apoptosis. In addition, overexpression of HSP47 also enhances Akt signaling in CRC cells exposed to chemotherapy by decreasing the protein stability of the Akt-specific phosphatase PHLPP1. Importantly, this finding was also confirmed in vivo as tumors with HSP47 overexpression were shown to be more resistant to 5-FU exposure and have elevated level of Akt activation. Taken together, our studies suggest a complex protein network surrounding SPARC that modulates the treatment response of CRC following chemotherapy. Therapeutic approaches against HSP47 or targeting GRP78 via SPARC mimetics may improve chemotherapeutic efficacy in CRC.