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David M. Rose

Researcher at University of California, San Diego

Publications -  36
Citations -  4887

David M. Rose is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Integrin & Paxillin. The author has an hindex of 28, co-authored 36 publications receiving 4684 citations. Previous affiliations of David M. Rose include Scripps Research Institute & Veterans Health Administration.

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A receptor for phosphatidylserine-specific clearance of apoptotic cells

TL;DR: Using phage display, a gene that appears to recognize phosphatidylserine on apoptotic cells is cloned and shown to be highly homologous to genes of unknown function in Caenorhabditis elegans and Drosophila melanogaster, suggesting that phosphatido-serine recognition on apoptosis cells during their removal by phagocytes is highly conserved throughout phylogeny.
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Innate immunity conferred by Toll-like receptors 2 and 4 and myeloid differentiation factor 88 expression is pivotal to monosodium urate monohydrate crystal-induced inflammation.

TL;DR: The murine host requires TLR-2,TLR-4, and MyD88 for macrophage activation and development of full-blown neutrophilic, air pouch inflammation in response to MSU crystals, which implicate innate immune cellular recognition of naked MSUstals by specific TLRs as a major factor in determining the inflammatory potential of MSU crystal deposits and the course of gouty arthritis.
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Binding of paxillin to α 4 integrins modifies integrin-dependent biological responses

TL;DR: The alpha4 integrins are indispensable for embryogenesis, haematopoiesis, and immune responses, possibly because alpha4 regulates cellular functions differently from other integrin through its cytoplasmic tail.
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Increased filamin binding to beta-integrin cytoplasmic domains inhibits cell migration.

TL;DR: The role of filamin binding in integrin-cytoskeleton connections was explored in this paper, where the authors mapped the filamin-binding site of integrin tails and identified amino acid substitutions that led to selective loss of filamins binding to the beta7 integrin tail and gain of filmin binding to β1A tail.
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Integrin modulation and signaling in leukocyte adhesion and migration

TL;DR: Mechanisms through which α4β1 integrin signaling regulates appropriate Rac activation to drive leukocyte migration are described.