Studies on the Epstein-Barr virus genome [Ph.D. thesis].
In PLoS ONE, 1983
... Chloramphenicol (Cm; 10 µg/ml; Roth, Karlsruhe, Germany), erythromycin (Em; 10 µg/ml; Merck, Darmstadt, Germany), spectinomycin (Spc; 150 µg/ml; Sigma Aldrich, München, Germany), tetracycline (Tc; ...
SURFACTANT PROTEINS IN SMOKING-RELATED LUNG DISEASE.
Athens, Greece. In Curr Top Med Chem, Oct 2015
The protein part of surfactant constitutes two hydrophilic proteins (SP-A and SP-D) that regulate surfactant metabolism and have immunologic functions, and two hydrophobic proteins (SP-B and SP-C), which play a direct role in the organization of the surfactant structure in the interphase and in the stabilization of the lipid layers during the respiratory cycle.
Lost after translation: insights from pulmonary surfactant for understanding the role of alveolar epithelial dysfunction and cellular quality control in fibrotic lung disease.
Ōita, Japan. In Am J Physiol Lung Cell Mol Physiol, Oct 2015
Drawing on data generated from a variety of model systems expressing disease-related surfactant component mutations [surfactant proteins A and C (SP-A and SP-C); the lipid transporter ABCA3], this review will examine the concept of epithelial dysfunction in fibrotic lung disease, provide an update on AT2 cell and surfactant biology, summarize cellular responses to mutant surfactant components [including endoplasmic reticulum (ER) stress, mitochondrial dysfunction, and intrinsic apoptosis], and examine quality control pathways (unfolded protein response, the ubiquitin-proteasome system, macroautophagy) that can be utilized to restore AT2 homeostasis.
Sphingosylphosphorylcholine in cancer progress.
Jinan, China. In Int J Clin Exp Med, 2014
Sphingosylphosphorylcholine (SPC) is a naturally occurring bioactive sphingolipid in blood plasma, metabolizing from the hydrolysis of the membrane sphingolipid.
Biomimicry of surfactant protein C.
Evanston, United States. In Acc Chem Res, 2008
This is largely because the previous synthetic formulations lacked analogues of the hydrophobic proteins of the lung surfactant system, SP-B and SP-C, which are critical functional constituents.