Editorial Review Board Application Personal Information Name: Phone Number: Email: College/Campus Affiliation: Year of Study: Program(s) of Study: Resume Please upload your curriculum vitae (CV) as a PDF, DOC, or DOCX, outlining academic, research and other co-curricular experiences and skills. Questions 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? Passages Please choose ONE of the following passages and make some suggestions for improving it. We recommend you copy the text to a Microsoft Word document, and track changes. DO NOT MAKE EDITS DIRECTLY IN THIS APPLICATION FORM. Please upload the edited Word document with your changes. Edited Passage (.doc, .docx, .pdf files are accepted): Passage 1: 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. Passage 2: 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. Passage 3: 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. Passage 4: 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,R-labetalol), possible explaining the similarity in antihypertensive response to the drug. *Note: If you receive error code 2 after submitting, please save your answers in a separate document and re-submit after refreshing the page.