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Institution

University of Alberta

EducationEdmonton, Alberta, Canada
About: University of Alberta is a education organization based out in Edmonton, Alberta, Canada. It is known for research contribution in the topics: Population & Health care. The organization has 65403 authors who have published 154847 publications receiving 5358338 citations. The organization is also known as: Ualberta & UAlberta.


Papers
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Journal ArticleDOI
12 Nov 2013-ACS Nano
TL;DR: It is demonstrated that peat moss, a wild plant that covers 3% of the earth's surface, serves as an ideal precursor to create sodium ion battery anodes with some of the most attractive electrochemical properties ever reported for carbonaceous materials.
Abstract: We demonstrate that peat moss, a wild plant that covers 3% of the earth’s surface, serves as an ideal precursor to create sodium ion battery (NIB) anodes with some of the most attractive electrochemical properties ever reported for carbonaceous materials. By inheriting the unique cellular structure of peat moss leaves, the resultant materials are composed of three-dimensional macroporous interconnected networks of carbon nanosheets (as thin as 60 nm). The peat moss tissue is highly cross-linked, being rich in lignin and hemicellulose, suppressing the nucleation of equilibrium graphite even at 1100 °C. Rather, the carbons form highly ordered pseudographitic arrays with substantially larger intergraphene spacing (0.388 nm) than graphite (c/2 = 0.3354 nm). XRD analysis demonstrates that this allows for significant Na intercalation to occur even below 0.2 V vs Na/Na+. By also incorporating a mild (300 °C) air activation step, we introduce hierarchical micro- and mesoporosity that tremendously improves the hig...

784 citations

Journal ArticleDOI
TL;DR: In this paper, remote sensing data indicate that contemporary climate warming has already resulted in increased productivity and increased productivity in the tundra biome (Tundra Tundra Bi biome).
Abstract: Temperature is increasing at unprecedented rates across most of the tundra biome(1). Remote-sensing data indicate that contemporary climate warming has already resulted in increased productivity ov ...

782 citations

Journal ArticleDOI
22 Apr 1993-Nature
TL;DR: In contrast, 69% of Wilms' tumours not undergoing loss of heterozygosity at lip showed biallelic expression of one or both genes, suggesting that relaxation or loss of imprinting could represent a new epigenetic mutational mechanism in carcinogenesis.
Abstract: GENOMIC imprinting, or parental allele-specific expression of genes, has been demonstrated at the molecular level in insects and mice1,2 but not in man. Imprinting as a potential mechanism of human disease is suggested by paternal uniparental disomy of 11 p15 in Beckwith–Wiedemann syndrome3 and by maternal uniparental disomy of 15ql1–12 in Prader–Willi syndrome4. Beckwith–Wiedemann syndrome is characterized by multiorgan overgrowth and predisposition to embryonal tumours such as Wilms9 tumour of the kidney5. A loss of heterozygosity of 11 p15 is also frequently found in a wide variety of tumours, including Wilms' tumour and lung, bladder, ovarian, liver and breast cancers6–11; 11pl5 also directly suppresses tumour growth in vitro12. Two genes in this band, H19 and insulin-like growth factor-II (IGF2) undergo reciprocal imprinting in the mouse, with maternal expression of H19 (ref. 13) and paternal expression of IGF2 (ref. 14). Here we find that both of these genes show monoallelic expression in human tissues and, as in mouse, H19 is expressed from the maternal allele and IGF2 from the paternal allele. In contrast, 69% of Wilms' tumours not undergoing loss of heterozygosity at lip showed biallelic expression of one or both genes, suggesting that relaxation or loss of imprinting could represent a new epigenetic mutational mechanism in carcinogenesis.

782 citations

Journal ArticleDOI
TL;DR: VADAR (Volume Area Dihedral Angle Reporter) is a comprehensive web server for quantitative protein structure evaluation that calculates, identifies, graphs, reports and/or evaluates a large number of key structural parameters both for individual residues and for the entire protein.
Abstract: VADAR (Volume Area Dihedral Angle Reporter) is a comprehensive web server for quantitative protein structure evaluation. It accepts Protein Data Bank (PDB) formatted files or PDB accession numbers as input and calculates, identifies, graphs, reports and/or evaluates a large number (>30) of key structural parameters both for individual residues and for the entire protein. These include excluded volume, accessible surface area, backbone and side chain dihedral angles, secondary structure, hydrogen bonding partners, hydrogen bond energies, steric quality, solvation free energy as well as local and overall fold quality. These derived parameters can be used to rapidly identify both general and residue-specific problems within newly determined protein structures. The VADAR web server is freely accessible at http://redpoll.pharmacy.ualberta.ca/vadar.

780 citations


Authors

Showing all 66027 results

NameH-indexPapersCitations
Salim Yusuf2311439252912
Yi Chen2174342293080
Robert M. Califf1961561167961
Douglas R. Green182661145944
Russel J. Reiter1691646121010
Jiawei Han1681233143427
Jaakko Kaprio1631532126320
Tobin J. Marks1591621111604
Josef M. Penninger154700107295
Subir Sarkar1491542144614
Gerald M. Edelman14754569091
Rinaldo Bellomo1471714120052
P. Sinervo138151699215
David A. Jackson136109568352
Andreas Warburton135157897496
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20241
2023234
20221,084
20219,315
20208,831
20198,177