Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1073/pnas.1517993112 http://scihub22266oqcxt.onion/10.1073/pnas.1517993112 C4672809!4672809!26627256     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2015 ; 112 (48): E6654-62 Nephropedia Template TP {{tp|p=26627256|t=2015. Post-conversion sialylation of prions in lymphoid tissues |pdf=|usr=}}{{26627256}} gab.com Text Post-conversion sialylation of prions in lymphoid tissues JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=26627256 #FOAvip In mammals, sialic acids are the most abundant terminal residues on cell-surface glycans and comprise ?self-associated molecular patterns,? which protect the host from inappropriate activation of multiple immune pathways. In a striking illustration of molecular mimicry, a number of microbial pathogens recruit host sialic acids to decorate their surfaces and hide from the same immune responses. Prions are proteinaceous infectious agents, not conventional pathogens. This study found that sialylation of prions is enhanced upon their colonization of secondary lymphoid organs, via extracellular host sialylation machinery. Thus, prions may use strategies similar to other pathogens to camouflage themselves from the immune system, facilitating host invasion. Twit Text FOAVip Post-conversion sialylation of prions in lymphoid tissues ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=26627256 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26627256 #FOAvip English Wikipedia <ref>{{Cite pmid|26627256}}</ref> Post-conversion sialylation of prions in lymphoid tissues #MMPMID26627256 Srivastava S; Makarava N; Katorcha E; Savtchenko R; Brossmer R; Baskakov IV Proc Natl Acad Sci U S A 2015[Dec]; 112 (48): E6654-62 PMID26627256show ga In mammals, sialic acids are the most abundant terminal residues on cell-surface glycans and comprise ?self-associated molecular patterns,? which protect the host from inappropriate activation of multiple immune pathways. In a striking illustration of molecular mimicry, a number of microbial pathogens recruit host sialic acids to decorate their surfaces and hide from the same immune responses. Prions are proteinaceous infectious agents, not conventional pathogens. This study found that sialylation of prions is enhanced upon their colonization of secondary lymphoid organs, via extracellular host sialylation machinery. Thus, prions may use strategies similar to other pathogens to camouflage themselves from the immune system, facilitating host invasion. äPost-conversion sialylation of prions in lymphoid tissues (epmc).pdf DeepDyve Pubget Overpricing