Search Results - "Cunningham, D.D."

Aggregation of the amyloid precursor protein within degenerating neurons and dystrophic neurites in Alzheimer's disease by Cummings, B J, Su, J H, Geddes, J W, Van Nostrand, W E, Wagner, S L, Cunningham, D D, Cotman, C W

“…Using a monoclonal antibody raised against purified, native, human protease nexin-2/amyloid precursor protein, which recognizes an amino terminal epitope on…”
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Thrombin active site regions required for fibroblast receptor binding and initiation of cell division by Glenn, K C, Carney, D H, Fenton, 2nd, J W, Cunningham, D D

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Integration of compressed and composite immobilized enzyme membranes into an injection molded pin format by ultrasonic welding by Cunningham, David D.

“…Enzyme immobilization conditions were optimized using four commercially available pre-activated membranes and glucose oxidase. Compression of the immobilized…”
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Teucrium reidii (Labiatae): a new species from north-western South Australia by Toelken, H.R., Cunningham, D.D.

“…The new species, Teucrium reidii Toelken & D.Dean Cunn., is here described and illustrated, and the generic key for the Flora of South Australia is amended…”
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Regulation of protease nexin-1 synthesis and secretion in cultured brain cells by injury-related factors by VAUGHAN, P. J, CUNNINGHAM, D. D

“…The clotting protease thrombin might contribute to cell damage following brain injury by its ability to retract processes on neurons and astrocytes. Protease…”
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Thrombin receptor activation induces secretion and nonamyloidogenic processing of amyloid beta-protein precursor by J Davis-Salinas, S M Saporito-Irwin, F M Donovan, D D Cunningham, W E Van Nostrand

“…The amyloid beta-protein (A beta) and protease nexin-2/amyloid beta-protein precursor (PN-2/A beta PP) are major constituents of senile plaques and…”
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Regulation of protease nexin-1 target protease specificity by collagen type IV by DONOVAN, F. M, VAUGHAN, P. J, CUNNINGHAM, D. D

“…Recent studies have shown that serine protease inhibitors can be regulated in their activity, specificity, and location by glycoprotein or extracellular matrix…”
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Protease nexin-1, a thrombin inhibitor, is regulated by interleukin-1 and dexamethasone in normal human fibroblasts by Guttridge, D.C., Lau, A.L., Cunningham, D.D.

“…Thrombin participates in several regulatory events following injury as a result of its effects on blood coagulation and cell migration, proliferation, and…”
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Selective radiolabeling of cell surface proteins to a high specific activity by Thompson, James A, Lau, Alice L, Cunningham, Dennis D

“…A procedure was developed for selective radiolabeling of membrane proteins on cells to higher specific activities than possible with available techniques. Cell…”
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Co-distribution of protease nexin-1 and protease nexin-2 in brains of non-human primates by Wagner, S L, Van Nostrand, W E, Lau, A L, Farrow, J S, Suzuki, M, Bartus, R T, Schuppek, R, Nguyen, A, Cotman, C W, Cunningham, D D

“…The protease nexins are protease inhibitors which regulate key blood coagulation proteases and which appear to be involved in certain physiological and…”
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Binding sites for elastase on cultured human fibroblasts that do not mediate internalization by Campbell, C H, Cunningham, D D

“…The proteolytic actions of elastases have been implicated in extracellular matrix damage, which is characteristic of a variety of pathological conditions…”
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A novel method for measuring cell surface-bound thrombin: detection of iodination-induced changes in thrombin-binding affinity by LOW, D. A, CUNNINGHAM, D. D

“…A method is presented for measuring picogram amounts of thrombin bound to the cell surface of normal mouse fibroblasts. After incubation of cells with hirudin,…”
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Glucocorticoids enhance the mitogenic action of insulin in serum-free cultures of chick embryo cells by Baker, J B, Simmer, R L, Glenn, K C, Cunningham, D D

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Transmembrane action of thrombin initiates chick cell division by Carney, D H, Cunningham, D D

“…Thrombin immobilized on polystyrene beads initiates DNA synthesis and cell division in quiescent cultures of chick embryo (CE) cells in serum-free medium…”
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