By Min Kyung-Tai, Karen Chang
Animal experiments have contributed a lot to our figuring out of mechanisms of ailment and are important for making a choice on new remedies. This quantity experiences the newest learn and advancements during this box. * Discusses new discoveries, ways, and ideas * Contributions from top students and specialists * Reference advisor for researchers taken with molecular biology and similar fields
Read or Download Animal Models of Human Disease, Volume 100 (Molecular Biology and Translational Science) PDF
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Extra info for Animal Models of Human Disease, Volume 100 (Molecular Biology and Translational Science)
3). Phosphorylation of the membrane-anchored FRS2a (also known as SNT1 for SUC1-associated neurotrophic factor target proteins) by the FGFR1 kinase recruits and activates the GRB2/SOS1 complex that then interacts with Ras to activate the MAP kinase signaling pathway. In addition, Crk has also been proposed to be a functional 30 FEN WANG FGF FGFR E2Ub Sef FRS2 Grb2 Shc Spry PLC-γ Cbl Gab1 PI3K AKT IP3 Sos DAG Shp2 Ras Ca++ Raf PKC ERK1/2 Signals mTOR PTEN MAP Signals Signals Signals Signals FIG.
High levels of the goblet cell-specific peptide Itf/Tff3 in these transgenic prostates is in accordance with recent microarray studies showing that ITF/TFF3 is upregulated in human prostate cancer. In addition, the PB-RAS prostates have a thickened fibromuscular stroma. Thus, the PB-RAS mouse model can be useful MOUSE MODELS OF HUMAN PROSTATE CANCER 17 for elucidating the early events in prostate carcinogenesis, as well as for studying the mechanisms and potential prostate cancer relevance of intestinal metaplasia.
Many FGF members need to have heparan sulfates (HSs) as cofactors to bind and activate FGFR, which are highly heterogeneous polysaccharide site-chains of proteoglycans on the cell surface. The HS has both FGF- and FGFR-binding motifs that are involved in the determination of ligand-binding and -signaling specificity of FGFR complexes. A HSPG HSPG B 653 654 730 766 Inactive Active FIG. 2. The FGFR signaling axis. (A) Structure domains of the FGF. Boxes indicate the putative structure domains. Empty box, signal peptide; solid box, conserved domain; shaded box, nonconserved sequence.
Animal Models of Human Disease, Volume 100 (Molecular Biology and Translational Science) by Min Kyung-Tai, Karen Chang