نتایج جستجو برای: metacaspase

تعداد نتایج: 151  

Journal: :iranian journal of parasitology 0
entsar saheb dept. of biology, college of sciences, university of baghdad, baghdad, iraq. wendy trzyna dept. of biological sciences, marshall university, huntington, west virginia, usa. katherine maringer dept. of biology, college of science and mathematics, university of arkansas at little rock, arkansas, usa. john bush dept. of biology, college of science and mathematics, university of arkansas at little rock, arkansas, usa.

background : acanthamoeba castellanii forms a resistant cyst that protects the para-site against the host’s immune response. acanthamoeba type-i metacaspase (acmcp) is a caspase-like protein that has been found to be expressed during the encysta-tions. dictyostelium discoideum is an organism closely related to acanthamoeba useful for studying the molecular function of this protozoan caspase-lik...

Journal: :Current Biology 2004
Maria F Suarez Lada H Filonova Andrei Smertenko Eugene I Savenkov David H Clapham Sara von Arnold Boris Zhivotovsky Peter V Bozhkov

In plants, as in animals, programmed cell death (PCD) is a key process responsible for the elimination of unneeded structures and for overall shape remodeling during development [1]; however, the molecular mechanisms remain poorly understood. Despite the absence of canonical caspases in plants, dying plant cells show an increased proteolytic caspase-like activity [2]. Moreover, the cell death c...

Journal: :Applied and environmental microbiology 2008
Akira Ohno Naoyuki Kato Ryota Sakamoto Soichiro Kimura Keizo Yamaguchi

We analyzed the effects of temperature on the interaction of Legionella pneumophila with Acanthamoeba castellanii. At <20 degrees C, overexpression of type 1 metacaspase, a stimulator of A. castellanii encystation, was associated with a reduced number of bacteria within amoeba. At low temperatures, A. castellanii seems to eliminate L. pneumophila by encystation and digestion.

Journal: :Molecular & cellular proteomics : MCP 2016
Thibaut Léger Camille Garcia Jean-Michel Camadro

Protein glycolysation is an essential posttranslational modification in eukaryotic cells. In pathogenic yeasts, it is involved in a large number of biological processes, such as protein folding quality control, cell viability and host/pathogen relationships. A link between protein glycosylation and apoptosis was established by the analysis of the phenotypes of oligosaccharyltransferase mutants ...

Journal: :Proceedings of the National Academy of Sciences 2012

Journal: :Bioorganic & Medicinal Chemistry Letters 2010

Journal: :Journal of Biological Chemistry 2012

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید