Compact Anthology of World Literature II: Volumes 4, 5, and 6

The Compact Anthology of World Literature, Parts 4, 5, and 6 is designed as an e-book to be accessible on a variety of devices: smart phone, tablet, e-reader, laptop, or desktop computer. Students have reported ease of accessibility and readability on all these devices. To access the ePub text on a laptop, desktop, or tablet, you will need to download a program through which you can read the text. We recommend Readium, an application available through Google. If you plan to read the text on an Android device, you will need to download an application called Lithium from the App Store. On an iPhone, the text will open in iBooks. Affordable Learning Georgia has also converted the .epub files to PDF. Because .epub does not easily convert to other formats, the left margin of the .pdf is very narrow. ALG recommends using the .epub version. Although the text is designed to look like an actual book, the Table of Contents is composed of hyperlinks that will take you to each introductory section and then to each text. The three parts of the text are organized into the following units: Part 4—The Seventeenth and Eighteenth Centuries Unit I: The Age of Reason Unit II: The Near East and Asia Part 5—The Long Nineteenth Century Unit I Romanticism Unit II Realism Part 6—The Twentieth Century and Contemporary Literature Unit I Modernism Unit II Postcolonial Literature Unit III Contemporary Literature Texts from a variety of genres and cultures are included in each unit. Additionally, each selection or collection includes a brief introduction about the author and text(s), and each includes 3 – 5 discussion questions. Texts in the public domain--those published or translated before 1923--are replicated here. Texts published or translated after 1923 are not yet available in the public domain. In those cases, we have provided a link to a stable site that includes the text. Thus, in Part 6, most of the texts are accessible in the form of links to outside sites. In every case, we have attempted to connect to the most stable links available. The following texts have been prepared with the assistance of the University of North Georgia Press in its role as Affordable Learning Georgia\u27s Partner Press. Affordable Learning Georgia partners with the University of North Georgia Press to assist grantees with copyright clearance, peer review, production and design, and other tasks required to produce quality Open Educational Resources (OER). The University Press is a peer-reviewed, academic press. Its mission is to produce scholarly work that contributes to the fields of innovative teaching, textbooks, and Open Educational Resources. Affordable Learning Georgia Textbook Transformation Grant funds may be used for services provided by the Press. To determine how the University Press can assist ALG grantees or anyone interested in developing OER with ALG, the University Press will provide advance free consultations. Please contact the Press at 706-864-1556 or [email protected]. “Textbook Transformation Grants” from Affordable Learning Georgia Accessible files with optical character recognition (OCR) and auto-tagging provided by the Center for Inclusive Design and Innovation.https://oer.galileo.usg.edu/english-textbooks/1018/thumbnail.jp

World Literature II (UNG)

This Grants Collection for World Literature II was created under a Round Nine ALG Textbook Transformation Grant. Affordable Learning Georgia Grants Collections are intended to provide faculty with the frameworks to quickly implement or revise the same materials as a Textbook Transformation Grants team, along with the aims and lessons learned from project teams during the implementation process. Documents are in .pdf format, with a separate .docx (Word) version available for download. Each collection contains the following materials: Linked Syllabus Initial Proposal Final Reporthttps://oer.galileo.usg.edu/english-collections/1006/thumbnail.jp

2-(1,3-Benzothia­zol-2-yl)guanidinium chloride

The non-H atoms of the cation of the title salt, C8H9N4S+·Cl−, are approximately co-planar (r.m.s. deviation = 0.037 Å), with one amino group forming an intra­molecular hydrogen bond to the tertiary N atom of the benzothia­zole fused-ring system. The cations and anions are linked by cyclic R 2 1(6) N—H⋯Cl hydrogen-bonding associations, generating helical chains running along the b-axis direction

N-(4,6-Dimethyl­pyrimidin-2-yl)-1,3-benzothia­zol-2-amine

In the title compound, C13H12N4S, an amino N atom is connected to a 1,3-benzothia­zole fused-ring system and a dimethyl-substituted pyrimidine ring, these components being aligned [inter­planar dihedral angle = 1.9 (1)°]. The secondary amino N atom forms an inter­molecular N—H⋯N hydrogen bond to an N atom of the fused ring of an adjacent mol­ecule, generating a centrosymmetric cyclic hydrogen-bonded dimer [graph set R 2 2(8)]

2-(1,3-Benzoxazol-2-yl)guanidinium chloride

The non-H atoms of the cation of the title salt, C8H9N4O+·Cl−, are approximately co-planar (r.m.s. deviation = 0.024 Å) with one amino group forming an intra­molecular hydrogen bond to the tertiary N atom of the benzoxazole fused-ring system. The cations and anions are linked by cyclic R 2 1(6) N—H⋯Cl hydrogen-bonding associations, generating linear chains running along the a-axis direction

Identification by whole-genome resequencing of gene defect responsible for severe hypercholesterolemia

Whole-genome sequencing is a potentially powerful tool for the diagnosis of genetic diseases. Here, we used sequencing-by-ligation to sequence the genome of an 11-month-old breast-fed girl with xanthomas and very high plasma cholesterol levels (1023 mg/dl). Her parents had normal plasma cholesterol levels and reported no family history of hypercholesterolemia, suggesting either an autosomal recessive disorder or a de novo mutation. Known genetic causes of severe hypercholesterolemia were ruled out by sequencing the responsible genes (LDLRAP, LDLR, PCSK9, APOE and APOB), and sitosterolemia was ruled out by documenting a normal plasma sitosterol:cholesterol ratio. Sequencing revealed 3 797 207 deviations from the reference sequence, of which 9726 were nonsynonymous single-nucleotide substitutions. A total of 9027 of the nonsynonymous substitutions were present in dbSNP or in 21 additional individuals from whom complete exonic sequences were available. The 699 novel nonsynonymous substitutions were distributed among 604 genes, 23 of which were single-copy genes that each contained 2 nonsynonymous substitutions consistent with an autosomal recessive model. One gene, ABCG5, had two nonsense mutations (Q16X and R446X). This finding indicated that the infant has sitosterolemia. Thus, whole-genome sequencing led to the diagnosis of a known disease with an atypical presentation. Diagnosis was confirmed by the finding of severe sitosterolemia in a blood sample obtained after the infant had been weaned. These findings demonstrate that whole-genome (or exome) sequencing can be a valuable aid to diagnose genetic diseases, even in individual patients

Food policy council case study describing cross-sector collaboration for food system change in a rural setting

Problem: Food Policy Councils (FPCs) are cross-sector collaborations that bring representatives from across the food system together to identify issues, coordinate programs, and inform policy. Little is known about how rural FPCs operate to influence food access in their communities. Purpose: To explore how a rural FPC facilitates cross-sector partnerships and influences food system change through interviews with eight members of the Adam’s County FPC. Results: Connections developed through the FPC helped council members work more effectively in their home organizations. Four themes were discussed: council dynamics and structure; sharing resources, expertise, and information; promoting healthy food access through programs; and food policy opportunities and challenges. Conclusions: This case study illustrates connections between FPC members in a rural county and identifies how FPCs can facilitate food system change in their communities. Improving our understanding of how rural FPCs function can help to advance the potential public health impact of councils

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

2-Oxoglutarate (2OG)-dependent oxygenases have important roles in the regulation of gene expression via demethylation of N-methylated chromatin components1,2 and in the hydroxylation of transcription factors3 and splicing factor proteins4. Recently, 2OG-dependent oxygenases that catalyse hydroxylation of transfer RNA5,6,7 and ribosomal proteins8 have been shown to be important in translation relating to cellular growth, TH17-cell differentiation and translational accuracy9,10,11,12. The finding that ribosomal oxygenases (ROXs) occur in organisms ranging from prokaryotes to humans8 raises questions as to their structural and evolutionary relationships. In Escherichia coli, YcfD catalyses arginine hydroxylation in the ribosomal protein L16; in humans, MYC-induced nuclear antigen (MINA53; also known as MINA) and nucleolar protein 66 (NO66) catalyse histidine hydroxylation in the ribosomal proteins RPL27A and RPL8, respectively. The functional assignments of ROXs open therapeutic possibilities via either ROX inhibition or targeting of differentially modified ribosomes. Despite differences in the residue and protein selectivities of prokaryotic and eukaryotic ROXs, comparison of the crystal structures of E. coli YcfD and Rhodothermus marinus YcfD with those of human MINA53 and NO66 reveals highly conserved folds and novel dimerization modes defining a new structural subfamily of 2OG-dependent oxygenases. ROX structures with and without their substrates support their functional assignments as hydroxylases but not demethylases, and reveal how the subfamily has evolved to catalyse the hydroxylation of different residue side chains of ribosomal proteins. Comparison of ROX crystal structures with those of other JmjC-domain-containing hydroxylases, including the hypoxia-inducible factor asparaginyl hydroxylase FIH and histone Nε-methyl lysine demethylases, identifies branch points in 2OG-dependent oxygenase evolution and distinguishes between JmjC-containing hydroxylases and demethylases catalysing modifications of translational and transcriptional machinery. The structures reveal that new protein hydroxylation activities can evolve by changing the coordination position from which the iron-bound substrate-oxidizing species reacts. This coordination flexibility has probably contributed to the evolution of the wide range of reactions catalysed by oxygenases