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.

10.1371/journal.pone.0123277 http://scihub22266oqcxt.onion/10.1371/journal.pone.0123277 C4395375!4395375!25874890     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       PLoS+One 2015 ; 10 (4): ä Nephropedia Template TP {{tp|p=25874890|t=2015. Identification of Critical Residues of Linear B Cell Epitope on Goodpasture Autoantigen |pdf=|usr=}}{{25874890}} gab.com Text Identification of Critical Residues of Linear B Cell Epitope on Goodpasture Autoantigen JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=25874890 #FOAvip Background: The autoantigen of anti-glomerular basement membrane (GBM) disease has been identified as the non-collagenous domain 1 of ?3 chain of type IV collagen, ?3(IV)NC1. Our previous study revealed a peptide on ?3(IV)NC1 as a major linear epitope for B cells and potentially nephrogenic, designated as P14 (?3129-150). This peptide has also been proven to be the epitope of auto-reactive T cells in anti-GBM patients. This study was aimed to further characterize the critical motif of P14. Methods: 16 patients with anti-GBM disease and positive anti-P14 antibodies were enrolled. A set of truncated and alanine substituted peptides derived from P14 were synthesized. Circulating antibodies against the peptides were detected by enzyme linked immunosorbent assay (ELISA). Results: We found that all sera with anti-P14 antibodies reacted with the 13-mer sequence in the C-terminus of P14 (P14c) exclusively. The level of antibodies against P14 was highly correlated with the level of antibodies against P14c (r=0.970, P<0.001). P14c was the core immunogenic region and the amino acid sequence (ISLWKGFSFIMFT) was highly hydrophobic. Each amino acid residue in P14c was sequentially replaced by alanine. Three residues of glycine142, phenylalanine143, and phenylalanine145 were identified crucial for antibody binding based on the remarkable decline (P<0.001) of antibody reaction after each residue replacement. Conclusions: We defined GFxF (?3142, 143,145) as the critical motif of P14. It may provide some clues for understanding the etiology of anti-GBM disease. Twit Text FOAVip Identification of Critical Residues of Linear B Cell Epitope on Goodpasture Autoantigen ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=25874890 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25874890 #FOAvip English Wikipedia <ref>{{Cite pmid|25874890}}</ref> Identification of Critical Residues of Linear B Cell Epitope on Goodpasture Autoantigen #MMPMID25874890 Jia Xy; Cui Z; Li Jn; Hu Sy; Zhao Mh PLoS One 2015[]; 10 (4): ä PMID25874890show ga Background: The autoantigen of anti-glomerular basement membrane (GBM) disease has been identified as the non-collagenous domain 1 of ?3 chain of type IV collagen, ?3(IV)NC1. Our previous study revealed a peptide on ?3(IV)NC1 as a major linear epitope for B cells and potentially nephrogenic, designated as P14 (?3129-150). This peptide has also been proven to be the epitope of auto-reactive T cells in anti-GBM patients. This study was aimed to further characterize the critical motif of P14. Methods: 16 patients with anti-GBM disease and positive anti-P14 antibodies were enrolled. A set of truncated and alanine substituted peptides derived from P14 were synthesized. Circulating antibodies against the peptides were detected by enzyme linked immunosorbent assay (ELISA). Results: We found that all sera with anti-P14 antibodies reacted with the 13-mer sequence in the C-terminus of P14 (P14c) exclusively. The level of antibodies against P14 was highly correlated with the level of antibodies against P14c (r=0.970, P<0.001). P14c was the core immunogenic region and the amino acid sequence (ISLWKGFSFIMFT) was highly hydrophobic. Each amino acid residue in P14c was sequentially replaced by alanine. Three residues of glycine142, phenylalanine143, and phenylalanine145 were identified crucial for antibody binding based on the remarkable decline (P<0.001) of antibody reaction after each residue replacement. Conclusions: We defined GFxF (?3142, 143,145) as the critical motif of P14. It may provide some clues for understanding the etiology of anti-GBM disease. äIdentification of Critical Residues of Linear B Cell Epitope on Goodpa(epmc).pdf DeepDyve Pubget Overpricing