Institution
Lehigh University
Education•Bethlehem, Pennsylvania, United States•
About: Lehigh University is a education organization based out in Bethlehem, Pennsylvania, United States. It is known for research contribution in the topics: Catalysis & Fracture mechanics. The organization has 12684 authors who have published 26550 publications receiving 770061 citations.
Papers published on a yearly basis
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TL;DR: In this paper, a critical review and analysis of existing fatigue-crack-growth data on high-strength aluminum and titanium alloys and high strength steels has been made.
160 citations
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American Museum of Natural History1, Instituto Butantan2, George Washington University3, Lehigh University4, South Australian Museum5, University of Adelaide6, Moravian College7, Australian National University8, University of Michigan9, Royal Ontario Museum10, University of Mississippi11, Rutgers University12, Florida State University13, University of Paris14, University of São Paulo15
TL;DR: High-throughput sequence data is used from 289 samples covering 75 families of squamates to address phylogenetic affinities, estimate divergence times, and characterize residual topological uncertainty in the presence of genome scale data to address genomic support for traditional taxonomic groupings Scleroglossa and Macrostomata.
Abstract: Genomics is narrowing uncertainty in the phylogenetic structure for many amniote groups. For one of the most diverse and species-rich groups, the squamate reptiles (lizards, snakes, and amphisbaenians), an inverse correlation between the number of taxa and loci sampled still persists across all publications using DNA sequence data and reaching a consensus on the relationships among them has been highly problematic. In this study, we use high-throughput sequence data from 289 samples covering 75 families of squamates to address phylogenetic affinities, estimate divergence times, and characterize residual topological uncertainty in the presence of genome-scale data. Importantly, we address genomic support for the traditional taxonomic groupings Scleroglossa and Macrostomata using novel machine-learning techniques. We interrogate genes using various metrics inherent to these loci, including parsimony-informative sites (PIS), phylogenetic informativeness, length, gaps, number of substitutions, and site concordance to understand why certain loci fail to find previously well-supported molecular clades and how they fail to support species-tree estimates. We show that both incomplete lineage sorting and poor gene-tree estimation (due to a few undesirable gene properties, such as an insufficient number of PIS), may account for most gene and species-tree discordance. We find overwhelming signal for Toxicofera, and also show that none of the loci included in this study supports Scleroglossa or Macrostomata. We comment on the origins and diversification of Squamata throughout the Mesozoic and underscore remaining uncertainties that persist in both deeper parts of the tree (e.g., relationships between Dibamia, Gekkota, and remaining squamates; among the three toxicoferan clades Iguania, Serpentes, and Anguiformes) and within specific clades (e.g., affinities among gekkotan, pleurodont iguanians, and colubroid families).
160 citations
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TL;DR: This work uses single-molecule Förster resonance energy transfer to probe the temperature-induced chain collapse of five unfolded or intrinsically disordered proteins and finds that each of the proteins undergoes a collapse with increasing temperature, with the most hydrophobic one, λ-repressor, undergoing a reexpansion at the highest temperatures.
Abstract: For disordered proteins, the dimensions of the chain are an important property that is sensitive to environmental conditions. We have used single-molecule Forster resonance energy transfer to probe the temperature-induced chain collapse of five unfolded or intrinsically disordered proteins. Because this behavior is sensitive to the details of intrachain and chain–solvent interactions, the collapse allows us to probe the physical interactions governing the dimensions of disordered proteins. We find that each of the proteins undergoes a collapse with increasing temperature, with the most hydrophobic one, λ-repressor, undergoing a reexpansion at the highest temperatures. Although such a collapse might be expected due to the temperature dependence of the classical “hydrophobic effect,” remarkably we find that the largest collapse occurs for the most hydrophilic, charged sequences. Using a combination of theory and simulation, we show that this result can be rationalized in terms of the temperature-dependent solvation free energies of the constituent amino acids, with the solvation properties of the most hydrophilic residues playing a large part in determining the collapse.
159 citations
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TL;DR: In this article, the transport of zero-valent iron (nZVI) particles stabilized by three polyelectrolytes: polyvinyl alcohol, co-vinyl acetate-co-itaconic acid (PV3A), poly(acrylic acid) (PAA), and soy proteins was investigated.
159 citations
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TL;DR: In this article, the authors used transmission electron microscopy to characterize the dispersions of CuO, ZnO, and Cr/sub 2/O/sub 3/ in methanol synthesis catalysts.
159 citations
Authors
Showing all 12785 results
Name | H-index | Papers | Citations |
---|---|---|---|
Yang Yang | 171 | 2644 | 153049 |
Gang Chen | 167 | 3372 | 149819 |
Yi Yang | 143 | 2456 | 92268 |
Mark D. Griffiths | 124 | 1238 | 61335 |
Michael Gill | 121 | 810 | 86338 |
Masaki Mori | 110 | 2200 | 66676 |
Kai Nan An | 109 | 953 | 51638 |
James R. Rice | 108 | 278 | 68943 |
Vinayak P. Dravid | 103 | 817 | 43612 |
Andrew M. Jones | 103 | 764 | 37253 |
Israel E. Wachs | 103 | 427 | 32029 |
Demetrios N. Christodoulides | 100 | 704 | 51093 |
Bert M. Weckhuysen | 100 | 767 | 40945 |
José Luis García Fierro | 100 | 1027 | 47228 |
Mordechai Segev | 99 | 729 | 40073 |