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10.1016/j.molbiopara.2017.02.003 http://scihub22266oqcxt.onion/10.1016/j.molbiopara.2017.02.003 C5388192!5388192 !28223095     free     free     free       Mol+Biochem+Parasitol 2017 ; 213 (?): 16-21 Nephropedia Template TP {{tp|p=28223095 |t=2017. Palmitoylation of Plasmodium alveolins promotes cytoskeletal function |pdf=|usr=}}{{28223095 }} gab.com Text Palmitoylation of Plasmodium alveolins promotes cytoskeletal function JO: Mol Biochem Parasitol http://www.kidney.de/pget.php?&tw=1&pmid=28223095 #FOAvip S-palmitoylation is a post-translational lipid modification that is widespread among Plasmodium proteins and essential for parasite development. Little is known about the contribution of palmitoylation to the function of individual parasite molecules and structures. Alveolins are major components of the subpellicular network (SPN), a cortical cytoskeleton primarily involved in providing mechanical strength to the cell. We show here that the alveolin IMC1c is palmitoylated on a conserved cysteine motif, and that non-palmitoylated IMC1c displays normal expression, stability and trafficking. However, mutant parasites exhibit reduced osmotic stress resistance and tensile strength. These findings support the hypothesis that alveolin palmitoylation enhances cytoskeletal function by strengthening the connection between the SPN and the adjoining inner membrane complex via lipid anchoring. Twit Text FOAVip Palmitoylation of Plasmodium alveolins promotes cytoskeletal function ????Mol Biochem Parasitol http://www.kidney.de/pget.php?&tw=1&pmid=28223095 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28223095 #FOAvip English Wikipedia <ref>{{Cite pmid|28223095 }}</ref> Palmitoylation of Plasmodium alveolins promotes cytoskeletal function #MMPMID28223095 Tremp AZ ; Al-Khattaf FS ; Dessens JT Mol Biochem Parasitol 2017[Apr]; 213 (?): 16-21 PMID28223095 show ga S-palmitoylation is a post-translational lipid modification that is widespread among Plasmodium proteins and essential for parasite development. Little is known about the contribution of palmitoylation to the function of individual parasite molecules and structures. Alveolins are major components of the subpellicular network (SPN), a cortical cytoskeleton primarily involved in providing mechanical strength to the cell. We show here that the alveolin IMC1c is palmitoylated on a conserved cysteine motif, and that non-palmitoylated IMC1c displays normal expression, stability and trafficking. However, mutant parasites exhibit reduced osmotic stress resistance and tensile strength. These findings support the hypothesis that alveolin palmitoylation enhances cytoskeletal function by strengthening the connection between the SPN and the adjoining inner membrane complex via lipid anchoring. |*Protein Processing, Post-Translational [MESH] |Biomechanical Phenomena [MESH] |Lipoylation [MESH] |Metalloendopeptidases/*metabolism [MESH] |Osmotic Pressure [MESH]Palmitoylation of Plasmodium alveolins promotes cytoskeletal function (epmc).pdf DeepDyve Pubget Overpricing