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Crystal Structure of Human Profilaggrin S100 Domain and Identification of Target Proteins Annexin II
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Structure and immunogenicity of pre-fusionstabilized human metapneumovirus F glycoprotein
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Crystal structure of human PLD1 provides insight into activation by PI(4,5)P2 and RhoA
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Evolution of protective human antibodies against Plasmodium falciparum circumsporozoite protein repeat motifs
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High resolution X-ray and NMR structural study of human T-cell immunoglobulin and mucin domain containing protein-3
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Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium
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Quantitative time-course metabolomics in human red blood cells reveal the temperature dependence of human metabolic networks
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The genome of a Bacteroidetes inhabitant of the human gut encodes a structurally distinct enoyl-acyl carrier protein reductase (FabI)
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Structural basis for multifunctional roles of human Ints3 C-terminal domain
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Development of a Gut-on-a-Chip Microfluidic Device with Three-Dimensionally Printed Human Intestinal Tissue for Studying Human-Microbe Interactions
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Modeling Human-Technology Interaction as a Sociotechnical System of Systems.
Abstract not provided.
Cryo-EM structure of human adenovirus D26 reveals the conservation of structural organization among human adenoviruses
Abstract not provided
A Global Food Demand Model for the Assessment of Complex Human-Earth Systems
Demand for agricultural products is an important problem in climate change economics. Food consumption will shape and shaped by climate change and emissions mitigation policies through interactions with bioenergy and afforestation, two critical issues in meeting international climate goals such as two-degrees. We develop a model of food demand for staple and nonstaple commodities that evolves with changing incomes and prices. The model addresses a long-standing issue in estimating food demands, the evolution of demand relationships across large changes in income and prices. We discuss the model, some of its properties and limitations. We estimate parameter values using pooled cross-sectional-time-series observations and the Metropolis Monte Carlo method and cross-validate the model by estimating parameters using a subset of the observations and test its ability to project into the unused observations. Finally, we apply bias correction techniques borrowed from the climate-modeling community and report results.
Structural and genetic convergence of HIV-1 neutralizing antibodies in vaccinated non-human primates
A primary goal of HIV-1 vaccine development is the consistent elicitation of protective, neutralizing antibodies. While highly similar neutralizing antibodies (nAbs) have been isolated from multiple HIV-infected individuals, it is unclear whether vaccination can consistently elicit highly similar nAbs in genetically diverse primates. Here, we show in three outbred rhesus macaques that immunization with Env elicits a genotypically and phenotypically conserved nAb response. From these vaccinated macaques, we isolated four antibody lineages that had commonalities in immunoglobulin variable, diversity, and joining gene segment usage. Atomic-level structures of the antigen binding fragments of the two most similar antibodies showed nearly identical paratopes. The Env binding modes of each of the four vaccine-induced nAbs were distinct from previously known monoclonal HIV-1 neutralizing antibodies, but were nearly identical to each other. The similarities of these antibodies show that the immune system in outbred primates can respond to HIV-1 Env vaccination with a similar structural and genotypic solution for recognizing a particular neutralizing epitope. These results support rational vaccine design for HIV-1 that aims to reproducibly elicit, in genetically diverse primates, nAbs with specific paratope structures capable of binding conserved epitopes.