{"title":"\"Ewondo in the Classes, French for the Masses\"","authors":"Parker Henry","doi":"10.14434/iujur.v4i1.24507","DOIUrl":"https://doi.org/10.14434/iujur.v4i1.24507","url":null,"abstract":"Cameroon is home to over two hundred eighty native languages coming from three language families, making it one of the most linguistically diverse countries on Earth. Despite this, native languages hold very few domains in Cameroonian society. In recent years, several experimental programs have begun to implement native languages in schools, citing that children learn best in their mother tongue. Among these schools is ELAN-Afrique, an initiative put forth by La Francophonie with the main aim of helping students better learn French by way of their mother tongue. This paper seeks to differentiate the benefits prescribed or expected by ELAN leadership from the actual benefits occurring at one Ewondo-medium ELAN school in Yaoundé. The study includes a series of twenty interviews with program leadership, linguists, and NGOs, as well as teachers and parents of students enrolled in the program. Claims made in interviews were then validated or refuted by classroom observation. The program’s main flaw is the assumption that the students’ mother tongue is Ewondo when in reality, due to their urban upbringing, the students’ mother tongue is French. This causes the reality of the program to differ fundamentally from the expectations of La Francophonie as some predicted benefits are negated, some manifest differently than expected, and other benefits appear never having been predicted.","PeriodicalId":92647,"journal":{"name":"Indiana University journal of undergraduate research","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41675595","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Systematic Survey of the Role of IGF in the Link Between Diabetes and Cancer.","authors":"Nirupama Devanathan, Ann C Kimble-Hill","doi":"10.14434/iujur.v4i1.24499","DOIUrl":"https://doi.org/10.14434/iujur.v4i1.24499","url":null,"abstract":"<p><p>Epidemiological studies have proposed a link between type II diabetes and cancer via the IGF/insulin signaling pathway, which includes insulin-like peptides (IGF1, IGF2, and insulin), insulin receptors (IR-A, IR-B, IGF1R, and hybrids), and insulin substrate proteins (IRS1-6). In this study, up- and down-regulation of various components in the IGF/insulin signaling pathway are compared to clinical outcomes for cancer patients; the components include diagnosis age, overall survival, tumor invasion and vascularization, and body mass index. It was found that the up-regulation of insulin growth Factor (IGF)/insulin components was associated with overall survival and tumor invasion and vascularization, while the down-regulation of equivalent components was not associated with clinical outcomes assessed in this study. Particularly, the up-regulation of DOK5, IGF2, and IRS2 in colorectal cancer and IGF1R in liver cancer is associated with significantly decreased overall survival. Functional aberrations in either of the two proteins in co-expression pairs were identified for each cancer and correlated with overall survival and diagnosis age. Specific biomarkers proposed in this study will be further analyzed to fine-tune consistent associations that can be translated to reliable prognostic standards for the roles of IGF/insulin signaling pathway modulations that promote cancer.</p>","PeriodicalId":92647,"journal":{"name":"Indiana University journal of undergraduate research","volume":"4 1","pages":"17-26"},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6425955/pdf/nihms-1008167.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37086381","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Cameron Peck, Piia Virtanen, Derrick Johnson, Ann C Kimble-Hill
{"title":"Using the Predicted Structure of the Amot Coiled Coil Homology Domain to Understand Lipid Binding.","authors":"Cameron Peck, Piia Virtanen, Derrick Johnson, Ann C Kimble-Hill","doi":"10.14434/iujur.v4i1.24528","DOIUrl":"10.14434/iujur.v4i1.24528","url":null,"abstract":"<p><p>Angiomotins (Amots) are a family of adapter proteins that modulate cellular polarity, differentiation, proliferation, and migration. Amot family members have a characteristic lipid-binding domain, the coiled coil homology (ACCH) domain that selectively targets the protein to membranes, which has been directly linked to its regulatory role in the cell. Several spot blot assays were used to validate the regions of the domain that participate in its membrane association, deformation, and vesicle fusion activity, which indicated the need for a structure to define the mechanism. Therefore, we sought to understand the structure-function relationship of this domain in order to find ways to modulate these signaling pathways. After many failed attempts to crystallize the ACCH domain of each Amot family member for structural analysis, we decided to pursue homologous models that could be refined using small angle x-ray scattering data. Theoretical models were produced using the homology software SWISS-MODEL and threading software I-TASSER and LOMETS, followed by comparison to SAXS data for model selection and refinement. We present a theoretical model of the domain that is driven by alpha helices and short random coil regions. These alpha helical regions form a classic dimer interface followed by two wide spread legs that we predict to be the lipid binding interface.</p>","PeriodicalId":92647,"journal":{"name":"Indiana University journal of undergraduate research","volume":"4 1","pages":"27-46"},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6448796/pdf/nihms-1008169.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37291696","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}