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Fas apoptotic inhibitory molecule

The protein encoded by this gene protects against death receptor-triggered apoptosis and regulates B-cell signaling and differentiation. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2011] (from NCBI)
Top mentioned proteins: CAN, PrP, caspase-8, OUT, FLIP
Papers on FAIM
Simultaneous FRAP, FLIM and FAIM for measurements of protein mobility and interaction in living cells.
Suhling et al., London, United Kingdom. In Biomed Opt Express, Nov 2015
We present a novel integrated multimodal fluorescence microscopy technique for simultaneous fluorescence recovery after photobleaching (FRAP), fluorescence lifetime imaging (FLIM) and fluorescence anisotropy imaging (FAIM).
Hyperosmotic stress activates the expression of members of the miR-15/107 family and induces downregulation of anti-apoptotic genes in rat liver.
Häussinger et al., Düsseldorf, Germany. In Sci Rep, 2014
It was also identified that hyperosmolarity significantly reduces the expression of anti-apoptotic genes including Bcl2, Ccnd1, Mcl1, Faim, Aatf, Bfar and Ikbkb, which are either validated or predicted targets of these microRNAs.
Amyloid-β reduces the expression of neuronal FAIM-L, thereby shifting the inflammatory response mediated by TNFα from neuronal protection to death.
Comella et al., Barcelona, Spain. In Cell Death Dis, 2014
Here we examined the relevance of the long form of Fas apoptotic inhibitory molecule (FAIM) protein, FAIM-L, in regulating the dual function of TNFα.
Selective inhibition of esophageal cancer cells by combination of HDAC inhibitors and Azacytidine.
Lassmann et al., Freiburg, Germany. In Epigenetics, 2014
RNA transcriptome analyses post MS-275 and/or AZA treatment identified novel regulated candidate genes (up: BCL6, Hes2; down: FAIM, MLKL), which were specifically associated with the treatment responses of esophageal cancer cells.
Structure determination of human Fas apoptosis inhibitory molecule and identification of the critical residues linking the interdomain interaction to the anti-apoptotic activity.
Zheng et al., Beijing, China. In Acta Crystallogr D Biol Crystallogr, 2014
Fas apoptosis inhibitory molecule (FAIM) is a highly conserved anti-apoptotic protein which plays important roles in cells.
FAIM-L is an IAP-binding protein that inhibits XIAP ubiquitinylation and protects from Fas-induced apoptosis.
Comella et al., Lleida, Spain. In J Neurosci, 2014
The neuronal long isoform of Fas Apoptotic Inhibitory Molecule (FAIM-L) protects from death receptor (DR)-induced apoptosis, yet its mechanism of protection remains unknown.
Time-resolved fluorescence anisotropy imaging.
Chung et al., London, United Kingdom. In Methods Mol Biol, 2013
Polarization-resolved fluorescence lifetime imaging-time-resolved fluorescence anisotropy imaging, TR-FAIM-allows mapping of viscosity or binding or of homo-FRET which can indicate dimerization or generally oligomerization.
Lineage-specific duplications of Muroidea Faim and Spag6 genes and atypical accelerated evolution of the parental Spag6 gene.
Wojnowski et al., Mainz, Germany. In J Mol Evol, 2013
Among those nine gene families are Fas apoptosis inhibitory molecule (Faim), implicated in apoptosis, and Sperm antigen 6 (Spag6), implicated in sperm mobility.
Fas apoptosis inhibitory molecule is upregulated by IGF-1 signaling and modulates Akt activation and IRF4 expression in multiple myeloma.
Lam et al., Singapore, Singapore. In Leukemia, 2013
Here, we investigate the role of Fas apoptosis inhibitory molecule (FAIM) in MM.
Expression analysis, single nucleotide polymorphisms and combined genotypes in candidate genes and their associations with growth and carcass traits in Qinchuan cattle.
Chen et al., China. In Mol Biol Rep, 2013
The apolipoprotein E (ApoE) gene is an important component of plasma lipoprotein, and Fas apoptosis inhibitory molecule (FAIM) is a novel anti-apoptotic gene.
TOSO promotes β-cell proliferation and protects from apoptosis.
Maedler et al., Bremen, Germany. In Mol Metab, 2011
Here we show that switching off the Fas pathway using Fas apoptotic inhibitory protein (Faim/TOSO), which regulates apoptosis upstream of caspase 8, blocked β-cell apoptosis and increased proliferation in human islets.
Crystallization and preliminary X-ray crystallographic studies of human FAIM protein.
Zheng et al., Beijing, China. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2010
FAIM (1-90) was crystallized and diffracted to a resolution of 2.5 A; the crystal belonged to space group P3(1), with unit-cell parameters a=b=58.02, c=71.11 A, alpha=beta=90, gamma=120 degrees.
Fas apoptosis inhibitory molecule regulates T cell receptor-mediated apoptosis of thymocytes by modulating Akt activation and Nur77 expression.
Lam et al., Singapore, Singapore. In J Biol Chem, 2010
defined a TCR-induced FAIM/Akt/Nur77 signaling axis that is critical for modulating the apoptosis of developing thymocytes
Fas apoptosis inhibitory molecule expression in B cells is regulated through IRF4 in a feed-forward mechanism.
Rothstein et al., United States. In J Immunol, 2009
FAIM is expressed in germinal center B cells, enhances interferon regulatory factor (IRF)4 expression, and is in turn positively regulated through IRF4 in a positive reinforcing (i.e., feed-forward) system.
Fas apoptosis inhibitory molecule enhances CD40 signaling in B cells and augments the plasma cell compartment.
Rothstein et al., United States. In J Immunol, 2009
FAIM acts to specifically enhance CD40 signaling for NF-kappaB activation, IRF-4 expression, and BCL-6 down-regulation in vitro, but has no effect on its own
Genetic deletion of faim reveals its role in modulating c-FLIP expression during CD95-mediated apoptosis of lymphocytes and hepatocytes.
Lam et al., Singapore, Singapore. In Cell Death Differ, 2009
FAIM plays a novel role in modulating Fas-mediated apoptosis and acts through influencing the expression of c-FLIP and regulating the physical binding of caspase-8 to Fas.
Fluorescence anisotropy imaging microscopy for homo-FRET in living cells.
Coppey-Moisan et al., Paris, France. In Methods Cell Biol, 2007
In this chapter, we present the basic physical principles of the fluorescence anisotropy imaging microscopy (FAIM) and its application to study FP-tagged protein dynamics and interaction in live cells.
Time-resolved fluorescence microscopy.
Phillips et al., London, United Kingdom. In Photochem Photobiol Sci, 2005
Fluorescence lifetime imaging (FLIM) can report on photophysical events that are difficult or impossible to observe by fluorescence intensity imaging, and time-resolved fluorescence anisotropy imaging (TR-FAIM) can measure the rotational mobility of a fluorophore in its environment.
Inducible resistance to Fas-mediated apoptosis in B cells.
Rothstein, Boston, United States. In Cell Res, 2000
Terminal effectors of B cell Fas-resistance include the known anti-apoptotic gene products, Bcl-xL and FLIP, and a novel anti-apoptotic gene that encodes FAIM (Fas Apoptosis Inhibitory Molecule).
Receptor-specific regulation of B-cell susceptibility to Fas-mediated apoptosis and a novel Fas apoptosis inhibitory molecule.
Schneider et al., Boston, United States. In Immunol Rev, 2000
Proximate mediators for Fas resistance include the known anti-apoptotic gene products Bcl-xL and FLIP (but not Btk), and a novel anti-apoptotic gene that encodes Fas apoptosis inhibitory molecule (FAIM).
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