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Rudolf Lucas

Researcher at Georgia Regents University

Publications -  165
Citations -  5725

Rudolf Lucas is an academic researcher from Georgia Regents University. The author has contributed to research in topics: Tumor necrosis factor alpha & Lung injury. The author has an hindex of 39, co-authored 153 publications receiving 5036 citations. Previous affiliations of Rudolf Lucas include Weizmann Institute of Science & Innogenetics.

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Cytokine production after intravenous or peritoneal gram-negative bacterial challenge in mice. Comparative protective efficacy of antibodies to tumor necrosis factor-alpha and to lipopolysaccharide.

TL;DR: The striking differences between cytokine profiles as well as the divergent efficacy of anti-TNF-alpha antibody after i.p.v. challenges suggest that TNF- alpha may not be as important in the pathogenesis of lethal peritonitis than after lethal acute bacteremia.
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Multiple Forms of Angiostatin Induce Apoptosis in Endothelial Cells

TL;DR: In vitro findings point to endothelial cell apoptosis as a mechanism for the antiangiogenic effect of angiostatin in vivo.
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Circulating endothelial cells and angiogenic serum factors during neoadjuvant chemotherapy of primary breast cancer

TL;DR: The data suggest that chemotherapy can only reduce the amounts of mature CEC, probably reflecting detached cells from tumour vessels, whereas the EPC and their progenitors are mobilised by chemotherapy.
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Regulators of endothelial and epithelial barrier integrity and function in acute lung injury

TL;DR: An overview of recently identified substances that inhibit and/or reverse endothelial barrier disruption and permeability or alveolar epithelial dysfunction is presented, which could contribute to the development of novel therapeutic strategies to combat permeability edema.
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Mapping the lectin-like activity of tumor necrosis factor.

TL;DR: Tumor necrosis factor (TNF), but not lymphotoxin (LT), is directly trypanolytic for salivarian trypanosomes, probably with lectin-like affinity, which is functionally and spatially distinct from the mammalian TNF receptor binding sites.