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Douglas R. Keene

Researcher at Shriners Hospitals for Children - Portland

Publications -  245
Citations -  22468

Douglas R. Keene is an academic researcher from Shriners Hospitals for Children - Portland. The author has contributed to research in topics: Extracellular matrix & Fibrillin. The author has an hindex of 82, co-authored 237 publications receiving 20507 citations. Previous affiliations of Douglas R. Keene include Medical College of Wisconsin & University of Southern California.

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Journal ArticleDOI

Type 2 alveolar cells are stem cells in adult lung

TL;DR: A combination of in vivo clonal lineage analysis, different injury/repair systems, and in vitro culture of purified cell populations is used to obtain new information about the contribution of AEC2s to alveolar maintenance and repair.
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Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils.

TL;DR: Investigation of the connective tissue matrices of skin, lung, kidney, vasculature, cartilage, tendon, muscle, cornea, and ciliary zonule demonstrated its widespread distribution, and immunolocalization suggested that fibrillin is arrayed periodically along the individual microfibril and that individualmicrofibrils may be aligned within bundles.
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Type VII collagen is a major structural component of anchoring fibrils.

TL;DR: The construction and characterization of a murine monoclonal antibody specific for type VII collagen is reported, which demonstrates metal deposition upon anchoring fibrils at both ends of these structures, as predicted by the location of the epitope ontype VII collagen.
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Latent Transforming Growth Factor β-binding Protein 1 Interacts with Fibrillin and Is a Microfibril-associated Protein

TL;DR: Immunolocalization data were consistent with the hypothesis that LTBP-1 is a fibrillin-associated protein present in certain tissues but not in others, and a model depicting the relationship between LT BP-1 and fibrillins microfibrils is proposed.
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Hfq: a bacterial Sm-like protein that mediates RNA-RNA interaction.

TL;DR: The bacterial Hfq protein this article belongs to the large family of Sm and Sm-like proteins: it contains a conserved sequence motif known as the Sm1 motif, forms a doughnut-shaped structure, and has RNA binding specificity very similar to the Sm proteins.