JULS
Journal of
Undergraduate
Life Sciences
EDITORIAL REVIEW BOARD MEMBER APPLICATION: 2015 - 2016
Thank you for your interest in joining the Journal of Undergraduate Life Sciences as an editorial review board
member. Together, we will work towards producing a professional journal that showcases some of the finest
research achieved by undergraduate students at the University of Toronto.
There are a total of 8-10 vacancies for this position, and should your application be successful, you will be
required to edit submissions during the months of October and November.
Responsibilities of a Review Board Member
 Provide feedback regarding the scholarly and linguistic merits of a perspective publication, together with
a written basis for the reviewer’s opinion.
 Provide constructive criticism to help the author improve the manuscript
 Maintain confidentiality of the author’s work and any comments
 Adhere to strict deadlines
Application Procedures:
1. Complete this application form with the associated questions by typing in your responses.
2. Submit via email to juls.recruitment@gmail.com. The deadline for completed applications is October 31,
2015 by 11:59PM. In the email subject, please indicate your name and desired position.
3. All applicants will receive notice via email as to whether their application was successful on or before
November 16, 2015.
Name:
Year of Study:
Program(s) of Study:
College Affiliation:
Email:
Phone Number:
Questions:
Please limit your responses to 150 words.
1. Why do you wish to join JULS?
2. Describe why your skillset would distinguish you from other potential candidates.
3. What background do you have in either the life sciences and/or editing (please mention any advanced
instruction in writing)?
4. How much time can you commit to JULS?
5. Correct one of the following abstracts as you see fit. Feel free to use Microsoft Word’s “Track Changes”
feature. Include several comments for the author. Please delete the abstracts that you have not chosen to edit.
Dysferlinopathies are autosomal recessive, progressive muscle dystrophies caused by mutations in
DYSF, leading to a loss or a severe reduction of dysferlin, a key protein in sarcolemmal repair.
Currently, no etiological treatment is available for patients affected with dysferlinopathy. As for
other muscular dystrophies, gene therapy approaches based on recombinant adeno-associated virus
(rAAV) vectors are promising options. However, because dysferlin messenger RNA is far above
the natural packaging size of rAAV, full-length dysferlin gene transfer would be problematic. In a
patient presenting with a late-onset moderate dysferlinopathy, we identified a large homozygous
deletion, leading to the production of a natural “minidysferlin” protein. Using rAAV-mediated gene
transfer into muscle, we demonstrated targeting of the minidysferlin to the muscle membrane and
efficient repair of sarcolemmal lesions in a mouse model of dysferlinopathy. Thus, as previously
demonstrated in the case of dystrophin, a deletion mutant of the dysferlin gene is also functional,
suggesting that dysferlin’s structure is modular. This minidysferlin protein could be used as part of
a therapeutic strategy for patients affected with dysferlinopathies.
Middle cerebral artery occlusion (MCAO) leads to brain cell death. However, quantitation of
injured brain cells and inflammatory cells after MCAO has not been determined in the mouse.
Transient 1 hr MCAO was induced to CD1 male mice with reperfusion at 4 different time groups.
The intraluminal thread occlusion technique with an endovascular approach targeting the MCA
occlusion is more widely used since it does not require complicated intracrainial procedures. The
recent advance of genetically altered mice provides a unique opportunity to see the role of a single
gene products in the pathophysiology of stroke. With the MCAO model in mice there has been
extensive gene manipulation done but not enough work done on control animals to know how the
cells react to this type of injury. The aim of this study was to find a specific cellular populations in
the ischemic and surrounding areas at different reperfused time points when subjected to a one hour
MCAO.
Cytosolic and nuclear iron-sulfur (Fe-S) proteins play key roles in processes such as ribosome
maturation, transcription and DNA repair-replication. For biosynthesis of their Fe-S clusters, a
dedicated cytosolic Fe-S protein assembly (CIA) machinery is required. Here, we identify the
essential flavoprotein Tah18 as a previously unrecognized CIA component and show by cell
biological, biochemical and spectroscopic approaches that the complex of Tah18 and the CIA
protein Dre2 is part of an electron transfer chain functioning in an early step of cytosolic Fe-S
protein biogenesis. Electrons are transferred from NADPH via the FAD- and FMN-containing
Tah18 to the Fe-S clusters of Dre2. This electron transfer chain is required for assembly of target
but not scaffold Fe-S proteins, suggesting a need for reduction in the generation of stably inserted
Fe-S clusters. The pathway is conserved in eukaryotes, as human Ndor1–Ciapin1 proteins can
functionally replace yeast Tah18–Dre2.
Studies on the disposition of labetalol stereoisomers in humans after oral administration of the
racemic labetalol mixture have shown predominance of the (S,S)-stereoisomer in plasma and urine
and small concentrations of the (R,R) and (S,R) stereoisomers in plasma. The proportion of the
(R,S) and (R,R) stereoisomers is respectively 22 and 9% in plasma and 4 and 24% in urine,
respectively, suggesting streoselective renal clearance. Previous experiements observed that the
concentrations in plasma of (R,R)-labetalol was approximately 40% lower than those of the other
stereoisomers, confirming the fact that the kinetic disposition of labetalol is stereoselective.
Concentrations of three of the four stereoisomers of labetalol are higher in women than men.
Concentrations are similar between genders, however, for the b-blocking stereoisomer (R,Rlabetalol), possible explaining the similarity in antihypertensive response to the drug.