Articolele autorului Cristian Bologa
Link la profilul stiintific al lui Cristian Bologa

Postdoctoral position: Molecular fungal pathogenesis

A postdoctoral fellowship is available at the University of New Mexico Health Science Center and VA Albuquerque Medical Center to study Candida fungal pathogenesis using molecular biology, cell biology, and postgenomic approaches as part of an active mycology research group. Our laboratory is studying the secretion of virulence-associated proteins in C. albicans, identification of novel secretory proteins involved in pathogenesis, biofilm formation

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ONE POSTDOCTORAL POSITION AT THE UNIVERSITY OF NEW MEXICO SCHOOL OF MEDICINE Department of Biochemistry and Molecular Biology One postdoctoral position is immediately available to study vacuolar ATPase proton pumps in Saccharomyces cerevisiae. Applicants would have a PhD in biochemistry, molecular biology, cell biology, genetics, or a related field. Preference will be given to candidates with demonstrated experience in yeast genetics. The ideal candidate

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In vivo effects of a GPR30 antagonist
Virtual and biomolecular screening converge on a selective agonist for GPR30

Estrogen is a hormone critical in the development, normal physiology and pathophysiology of numerous human tissues. The effects of estrogen have traditionally been solely ascribed to estrogen receptor alpha (ERalpha) and more recently ERbeta, members of the soluble, nuclear ligand-activated family of transcription factors. We have recently shown that the seven-transmembrane G protein-coupled receptor GPR30 binds estrogen with high affinity and resides

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Biomolecular screening of formylpeptide receptor ligands with a sensitive, quantitative, high-throughput flow cytometry platform

The formylpeptide receptor (FPR) family of G protein-coupled receptors contributes to the localization and activation of tissue-damaging leukocytes at sites of chronic inflammation. Here we describe a high-throughput flow cytometry screening approach that has successfully identified multiple families of previously unknown FPR ligands. The assay detects active structures that block the binding of a fluorescent ligand to membrane FPR of intact cells,

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