Letter to Mary Johns regarding award of a the Lucile Elliott Scholarship, March 2, 1990

A letter from Donna Bennett to Mary Johns accepting the Lucile Elliott Scholarship awarded to her

Concert recording 2014-03-11a

[Track 01]. No. 4 Susse stille from Neun deutsche arien / George Frideric Handel -- [Track 02]. Si mes vers avaient des ailes / Reynaldo Hahn -- La diva de l\u27empire / Erik Satie -- [Track 03]. Er der Herrlichste von allen ; Du Ring an meinem Finger from Frauenliebe und leben / Robert Schumann -- [Track 04]. My name is Barbara ; A big Indian and a little Indian ; I\u27m a person too from I hate music!: A cycle of five kid songs / Leonard Bernstein -- [Track 05]. Deh vieni, non tardar o goija bella from Le Nozze di Figaro / Wolfgang Amadeus Mozart -- Je veux vivre from Romeo et Juliette / Charles Gounod

Exome sequencing identifies a missense variant in EFEMP1 co-segregating in a family with autosomal dominant primary open-angle glaucoma

Primary open-angle glaucoma (POAG) is a clinically important and genetically heterogeneous cause of progressive vision loss as a result of retinal ganglion cell death. Here we have utilized trio-based, whole-exome sequencing to identify the genetic defect underlying an autosomal dominant form of adult-onset POAG segregating in an African-American family. Exome sequencing identified a novel missense variant (c.418C>T, p.Arg140Trp) in exon-5 of the gene coding for epidermal growth factor (EGF) containing fibulin-like extracellular matrix protein 1 (EFEMP1) that co-segregated with disease in the family. Linkage and haplotype analyses with microsatellite markers indicated that the disease interval overlapped a known POAG locus (GLC1H) on chromosome 2p. The p.Arg140Trp substitution was predicted in silico to have damaging effects on protein function and transient expression studies in cultured cells revealed that the Trp140-mutant protein exhibited increased intracellular accumulation compared with wild-type EFEMP1. In situ hybridization of the mouse eye with oligonucleotide probes detected the highest levels of EFEMP1 transcripts in the ciliary body, cornea, inner nuclear layer of the retina, and the optic nerve head. The recent finding that a common variant near EFEMP1 was associated with optic nerve-head morphology supports the possibility that the EFEMP1 variant identified in this POAG family may be pathogenic

Exome sequencing identifies novel and recurrent mutations in GJA8 and CRYGD associated with inherited cataract

BACKGROUND: Inherited cataract is a clinically important and genetically heterogeneous cause of visual impairment. Typically, it presents at an early age with or without other ocular/systemic signs and lacks clear phenotype-genotype correlation rendering both clinical classification and molecular diagnosis challenging. Here we have utilized trio-based whole exome sequencing to discover mutations in candidate genes underlying autosomal dominant cataract segregating in three nuclear families. RESULTS: In family A, we identified a recurrent heterozygous mutation in exon-2 of the gene encoding γD-crystallin (CRYGD; c.70C > A, p.Pro24Thr) that co-segregated with ‘coralliform’ lens opacities. Families B and C were found to harbor different novel variants in exon-2 of the gene coding for gap-junction protein α8 (GJA8; c.20T > C, p.Leu7Pro and c.293A > C, p.His98Pro). Each novel variant co-segregated with disease and was predicted in silico to have damaging effects on protein function. CONCLUSIONS: Exome sequencing facilitates concurrent mutation-profiling of the burgeoning list of candidate genes for inherited cataract, and the results can provide enhanced clinical diagnosis and genetic counseling for affected families. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s40246-014-0019-6) contains supplementary material, which is available to authorized users

Introduction to Environmental Science: 2nd Edition

2nd Edition: Revised by Kalina Manoylov, Allison Rick VandeVoort, Christine Mutiti, Samuel Mutiti and Donna Bennett in 2017. Authors\u27 Description: This course uses the basic principles of biology and earth science as a context for understanding environmental policies and resource management practices. Our planet is facing unprecedented environmental challenges, from oil spills to global climate change. In ENSC 1000, you will learn about the science behind these problems; preparing you to make an informed, invaluable contribution to Earth’s future. I hope that each of you is engaged by the material presented and participates fully in the search for, acquisition of, and sharing of information within our class. Environmental Science Laboratory (ENSC 1000L) is a separate class and you will receive a separate grade for that course. Course Objectives Upon completion of this course, you will be able to: Evaluate the diverse responses of peoples, groups, and cultures to environmental issues, themes and topics. Use critical observation and analysis to predict outcomes associated with environmental modifications. Demonstrate knowledge of the causes & consequences of climate change. Apply quantitative skills to solve environmental science problems. Demonstrate knowledge of environmental law and policy. Design and critically evaluate experiments. Interpret data in figures and graphs. This open textbook for Introduction to Environmental Science was created under a Round Two ALG Textbook Transformation Grant. Accessible files with optical character recognition (OCR) and auto-tagging provided by the Center for Inclusive Design and Innovation.https://oer.galileo.usg.edu/biology-textbooks/1003/thumbnail.jp

Introduction to Environmental Science

This Grants Collection uses the grant-supported open textbook Introduction to Environmental Science from Georgia College and State University: http://oer.galileo.usg.edu/biology-textbooks/4/ This Grants Collection for Introduction to Environmental Science was created under a Round Two 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/biology-collections/1001/thumbnail.jp

Cryopreparation of Tissue for Electron Microscopy

An apparatus able to remove amorphous phase tissue water without recrystallization or rehydration has been produced. Application of this technique to biological samples achieves both the preservation of ultrastructure and the retention of cellular macromolecules and solute without redistribution or modification. Small pieces of fresh tissue were cryofixed by the method of bounce free metal-mirror freezing on polished copper bars at liquid nitrogen temperature. Tissue samples were then placed under liquid nitrogen in a copper sample holder equipped with a thermocouple and feedback controlled heating circuit. Under liquid nitrogen the sample block was placed in a stainless steel sample chamber which was then evacuated to a hydrocarbon-free ultrahigh vacuum (1x10-8mbar). Equilibrium temperature prior to the onset of the drying cycle was -192°C. Tissue was dried by increasing the temperature of the specimen block 1.33°C each hour while monitoring the rate of water removal with a partial pressure analyzer. Results indicate that drying is complete below the devitrification temperature of amorphous phase tissue water. After drying, tissue was fixed with osmium tetroxide vapour, vacuum embedded in low viscosity epoxy resin, sectioned, stained and viewed with the electron microscope. Tissue processed in this manner exhibits excellent morphological preservation with out the need for prefixation or cryoprotective agents. In addition, by avoiding prefixation and solvent contact during resin embedding, this method provides the basis for combining ultrastructural preservation with optimum material for immunocytochemical staining and elecron microprobe analysis