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Institution

University of Georgia

EducationAthens, Georgia, United States
About: University of Georgia is a education organization based out in Athens, Georgia, United States. It is known for research contribution in the topics: Population & Gene. The organization has 41934 authors who have published 93622 publications receiving 3713212 citations. The organization is also known as: UGA & Franklin College.


Papers
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Journal ArticleDOI
TL;DR: A draft genome sequence of mungbean is constructed to facilitate genome research into the subgenus Ceratotropis, which includes several important dietary legumes in Asia, and to enable a better understanding of the evolution of leguminous species.
Abstract: Mungbean (Vigna radiata) is a fast-growing, warm-season legume crop that is primarily cultivated in developing countries of Asia. Here we construct a draft genome sequence of mungbean to facilitate genome research into the subgenus Ceratotropis, which includes several important dietary legumes in Asia, and to enable a better understanding of the evolution of leguminous species. Based on the de novo assembly of additional wild mungbean species, the divergence of what was eventually domesticated and the sampled wild mungbean species appears to have predated domestication. Moreover, the de novo assembly of a tetraploid Vigna species (V. reflexo-pilosa var. glabra) provides genomic evidence of a recent allopolyploid event. The species tree is constructed using de novo RNA-seq assemblies of 22 accessions of 18 Vigna species and protein sets of Glycine max. The present assembly of V. radiata var. radiata will facilitate genome research and accelerate molecular breeding of the subgenus Ceratotropis.

397 citations

Journal ArticleDOI
TL;DR: Fifteen pigs from five farms on which there had been a previous clinical and histopathological diagnosis of postweaning multisystemic wasting syndrome (PMWS) were investigated, and lymphoid lesions were suggestive of immunosuppression.

397 citations

Journal ArticleDOI
TL;DR: In this paper, an approximate serpentine-magnetite geothermometer curve was constructed by extrapolation of observed O18 fractionations between coexisting chlorites and Fe-Ti oxides in low-grade pelitic schists whose isotopic temperatures are known from the quartz-muscovite O18 geithermometer.
Abstract: Five lizardite-chrysotile type serpentinites from California, Guatemala and the Dominican Republic show oxygen isotope fractionations of 15.1 to 12.9 per mil between coexisting serpentine and magnetite (δO18 magnetite=−7.6 to −4.6 per mil relative to SMOW). Nine antigorites (mainly from Vermont and S. E. Pennsylvania) show distinctly smaller fractionations of 8.7 to 4.8 per mil (δO18 magnetite=−2.6 to +1.7 per mil). Two lizardite and chrysotile serpentinites dredged from the Mid-Atlantic Ridge exhibit fractionations of 10.0 and 12.4 per mil (δO18 magnetite=−6.8 and −7.9 per mil, respectively), whereas an oceanic antigorite shows a value of 8.2 per mil (δO18 magnetite=−6.2). These data all clearly indicate that the antigorites formed at higher temperatures than the chrysotilelizardites. Electron microprobe analyses of magnetites from the above samples show that they are chemically homogeneous and essentially pure Fe3O2. However, some magnetites from certain other samples that show a wide variation of Cr content also give very erratic oxygen isotopic results, suggesting non-equilibrium. An approximate serpentine-magnetite geothermometer curve was constructed by (1) extrapolation of observed O18 fractionations between coexisting chlorites and Fe-Ti oxides in low-grade pelitic schists whose isotopic temperatures are known from the quartz-muscovite O18 geothermometer, and (2) estimates of the O18 fractionation factor between chlorite and serpentine (assumed to be equal to unity). This serpentine-magnetite geothermometer suggests approximate equilibrium temperatures as follows: continental lizardite-chrysotile, 85° to 115° C; oceanic lizardite and chrysotile, 130° C and 185° C, respectively; oceanic antigorite, 235° C; and continental antigorites, 220° to 460° C.

397 citations

Journal ArticleDOI
TL;DR: The results of this multi-institutional study indicate that MS-based analysis appears as the efficient method for identification and quantitation of oligosaccharides in glycomic studies and endorse the power of MS for glycopeptide characterization with high sensitivity in proteomic programs.
Abstract: Mass spectrometry (MS) of glycoproteins is an emerging field in proteomics, poised to meet the technical demand for elucidation of the structural complexity and functions of the oligosaccharide components of molecules. Considering the divergence of the mass spectrometric methods employed for oligosaccharide analysis in recent publications, it is necessary to establish technical standards and demonstrate capabilities. In the present study of the Human Proteome Organisation (HUPO) Human Disease Glycomics/Proteome Initiative (HGPI), the same samples of transferrin and immunoglobulin-G were analyzed for N-linked oligosaccharides and their relative abundances in 20 laboratories, and the chromatographic and mass spectrometric analysis results were evaluated. In general, matrix-assisted laser desorption/ionization (MALDI) time-of-flight MS of permethylated oligosaccharide mixtures carried out in six laboratories yielded good quantitation, and the results can be correlated to those of chromatography of reductive amination derivatives. For underivatized oligosaccharide alditols, graphitized carbon-liquid chromatography (LC)/electrospray ionization (ESI) MS detecting deprotonated molecules in the negative ion mode provided acceptable quantitation. The variance of the results among these three methods was small. Detailed analyses of tryptic glycopeptides employing either nano LC/ESI MS/MS or MALDI MS demonstrated excellent capability to determine site-specific or subclass-specific glycan profiles in these samples. Taking into account the variety of MS technologies and options for distinct protocols used in this study, the results of this multi-institutional study indicate that MS-based analysis appears as the efficient method for identification and quantitation of oligosaccharides in glycomic studies and endorse the power of MS for glycopeptide characterization with high sensitivity in proteomic programs.

397 citations

Journal ArticleDOI
23 Oct 2020-Science
TL;DR: Targeting the interaction between the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein and the human angiotensin-converting enzyme 2 (ACE2) receptor is a promising therapeutic strategy and small, stable proteins that bind tightly to the spike and block it from binding to ACE2 are designed.
Abstract: Targeting the interaction between the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein and the human angiotensin-converting enzyme 2 (ACE2) receptor is a promising therapeutic strategy. We designed inhibitors using two de novo design approaches. Computer-generated scaffolds were either built around an ACE2 helix that interacts with the spike receptor binding domain (RBD) or docked against the RBD to identify new binding modes, and their amino acid sequences were designed to optimize target binding, folding, and stability. Ten designs bound the RBD, with affinities ranging from 100 picomolar to 10 nanomolar, and blocked SARS-CoV-2 infection of Vero E6 cells with median inhibitory concentration (IC50) values between 24 picomolar and 35 nanomolar. The most potent, with new binding modes, are 56- and 64-residue proteins (IC50 ~ 0.16 nanograms per milliliter). Cryo-electron microscopy structures of these minibinders in complex with the SARS-CoV-2 spike ectodomain trimer with all three RBDs bound are nearly identical to the computational models. These hyperstable minibinders provide starting points for SARS-CoV-2 therapeutics.

397 citations


Authors

Showing all 42268 results

NameH-indexPapersCitations
Rob Knight2011061253207
Feng Zhang1721278181865
Zhenan Bao169865106571
Carl W. Cotman165809105323
Yoshio Bando147123480883
Mark Raymond Adams1471187135038
Han Zhang13097058863
Dmitri Golberg129102461788
Godfrey D. Pearlson12874058845
Douglas E. Soltis12761267161
Richard A. Dixon12660371424
Ajit Varki12454258772
Keith A. Johnson12079851034
Gustavo E. Scuseria12065895195
Julian I. Schroeder12031550323
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
2023125
2022542
20214,670
20204,504
20194,098
20183,994