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David E. Kling

Researcher at Harvard University

Publications -  30
Citations -  2639

David E. Kling is an academic researcher from Harvard University. The author has contributed to research in topics: Kinase & Epitope. The author has an hindex of 19, co-authored 29 publications receiving 2065 citations. Previous affiliations of David E. Kling include Brigham and Women's Hospital & United States Department of Veterans Affairs.

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Scaling accurate genetic variant discovery to tens of thousands of samples

TL;DR: A novel assembly-based approach to variant calling, the GATK HaplotypeCaller and Reference Confidence Model, that determines genotype likelihoods independently per-sample but performs joint calling across all samples within a project simultaneously, showing that the accuracy of indel variant calling is superior in comparison to other algorithms.
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The principal fucosylated oligosaccharides of human milk exhibit prebiotic properties on cultured infant microbiota

TL;DR: If these bifidobacteria are representative of pioneering or keystone species for human microbiota, fucosylated HMOS could strongly promote colonization and maintenance of a mutualist symbiotic microbiome.
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The human milk oligosaccharide 2′-fucosyllactose modulates CD14 expression in human enterocytes, thereby attenuating LPS-induced inflammation

TL;DR: In this paper, the authors investigated whether human milk oligosaccharides (HMOSs) influence pathogenic Escherichia coli -induced interleukin (IL)-8 release by intestinal epithelial cells (IECs).
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Large, identical, tandem repeating units in the C protein alpha antigen gene, bca, of group B streptococci.

TL;DR: The C protein alpha antigen structural gene (named bca for group B, C protein, alpha) is cloned into Escherichia coli and demonstrates a regularly laddered pattern of heterogeneous polypeptides.
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Group B streptococci escape host immunity by deletion of tandem repeat elements of the alpha C protein.

TL;DR: Deletions in the repeat region were observed at a much lower frequency and appear to lower the organism's susceptibility to killing by antibody specific to the alpha C protein, suggesting this mechanism of antigenic variation may provide a means whereby GBS evade host immunity.