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10.4049/jimmunol.0900953 http://scihub22266oqcxt.onion/10.4049/jimmunol.0900953 C4053221!4053221!19710472     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Immunol 2009 ; 183 (6): 3690-9 Nephropedia Template TP {{tp|p=19710472|t=2009. XBP-1-deficient plasmablasts show normal protein folding but altered glycosylation and lipid synthesis |pdf=|usr=}}{{19710472}} gab.com Text XBP-1-deficient plasmablasts show normal protein folding but altered glycosylation and lipid synthesis JO: J Immunol http://www.kidney.de/pget.php?&tw=1&pmid=19710472 #FOAvip The accumulation of misfolded secreted IgM in the endoplasmic reticulum (ER) of XBP-1-deficient B cells has been held responsible for the inability of such cells to yield plasma cells, through the failure to mount a proper unfolded protein response. Lipopolysaccharide (LPS)-stimulated B cells incapable of secreting IgM still activate the XBP-1 axis normally: XBP-1 is turned on by cues that trigger differentiation and not in response to accumulation of unfolded IgM, but the impact of XBP-1 deficiency on glycoprotein folding and assembly has not been explored. The lack of XBP-1 compromised neither the formation of functional hen egg lysozyme-specific IgM nor the secretion of free ? chains. Although XBP-1 deficiency affects the synthesis of some ER chaperones, including protein disulfide isomerase, their steady state levels do not drop below the threshold required for proper assembly and maturation of the Ig?/Ig? heterodimer and MHC molecules. Intracellular transport and surface display of integral membrane proteins are unaffected by XBP-1 deficiency. Given the fact that we failed to observe any defects in folding of a variety of glycoproteins, we looked for other means to explain the requirement for XBP-1 in plasma cell development. We observed significantly reduced levels of phosphatidylcholine, sphingomyelin, and phosphatidylinositol in total membranes of XBP-1-deficient B cells, and reduced ER content. Terminal N-linked glycosylation of IgM and class I MHC was altered in these cells. XBP-1 hence has important roles beyond folding proteins in the ER. Twit Text FOAVip XBP-1-deficient plasmablasts show normal protein folding but altered glycosylation and lipid synthesis ????J Immunol http://www.kidney.de/pget.php?&tw=1&pmid=19710472 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19710472 #FOAvip English Wikipedia <ref>{{Cite pmid|19710472}}</ref> XBP-1-deficient plasmablasts show normal protein folding but altered glycosylation and lipid synthesis #MMPMID19710472 McGehee AM; Dougan SK; Klemm EJ; Shui G; Park B; Kim YM; Watson N; Wenk MR; Ploegh HL; Hu CCA J Immunol 2009[Sep]; 183 (6): 3690-9 PMID19710472show ga The accumulation of misfolded secreted IgM in the endoplasmic reticulum (ER) of XBP-1-deficient B cells has been held responsible for the inability of such cells to yield plasma cells, through the failure to mount a proper unfolded protein response. Lipopolysaccharide (LPS)-stimulated B cells incapable of secreting IgM still activate the XBP-1 axis normally: XBP-1 is turned on by cues that trigger differentiation and not in response to accumulation of unfolded IgM, but the impact of XBP-1 deficiency on glycoprotein folding and assembly has not been explored. The lack of XBP-1 compromised neither the formation of functional hen egg lysozyme-specific IgM nor the secretion of free ? chains. Although XBP-1 deficiency affects the synthesis of some ER chaperones, including protein disulfide isomerase, their steady state levels do not drop below the threshold required for proper assembly and maturation of the Ig?/Ig? heterodimer and MHC molecules. Intracellular transport and surface display of integral membrane proteins are unaffected by XBP-1 deficiency. Given the fact that we failed to observe any defects in folding of a variety of glycoproteins, we looked for other means to explain the requirement for XBP-1 in plasma cell development. We observed significantly reduced levels of phosphatidylcholine, sphingomyelin, and phosphatidylinositol in total membranes of XBP-1-deficient B cells, and reduced ER content. Terminal N-linked glycosylation of IgM and class I MHC was altered in these cells. XBP-1 hence has important roles beyond folding proteins in the ER. äXBP-1-deficient plasmablasts show normal protein folding but altered g(epmc).pdf DeepDyve Pubget Overpricing