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10.1007/s12079-017-0422-6 http://scihub22266oqcxt.onion/10.1007/s12079-017-0422-6 C5842185!5842185 !29086200     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29086200 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\29086200 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Cell+Commun+Signal 2018 ; 12 (1 ): 301-308 Nephropedia Template TP {{tp|p=29086200 |t=2018. Periostin function in communication with extracellular matrices |pdf=|usr=}}{{29086200 }} gab.com Text Periostin function in communication with extracellular matrices JO: J Cell Commun Signal http://www.kidney.de/pget.php?&tw=1&pmid=29086200 #FOAvip Periostin is a secretory protein with a multi-domain structure, comprising an amino-terminal cysteine-rich EMI domain, four internal FAS 1 domains, and a carboxyl-terminal hydrophilic domain. These adjacent domains bind to extracellular matrix proteins (type I collagen, fibronectin, tenascin-C, and laminin ?2), and BMP-1 that catalyzes crosslinking of type I collagen, and proteoglycans, which play a role in cell adhesion. The binding sites on periostin have been demonstrated to contribute to the mechanical strength of connective tissues, enhancing intermolecular interactions in close proximity and their assembly into extracellular matrix architectures, where periostin plays further essential roles in physiological maintenance and pathological progression. Furthermore, periostin also binds to Notch 1 and CCN3, which have functions in maintenance of stemness, thus opening up a new field of periostin action. Twit Text FOAVip Periostin function in communication with extracellular matrices ????J Cell Commun Signal http://www.kidney.de/pget.php?&tw=1&pmid=29086200 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29086200 #FOAvip English Wikipedia <ref>{{Cite pmid|29086200 }}</ref> Periostin function in communication with extracellular matrices #MMPMID29086200 Kudo A ; Kii I J Cell Commun Signal 2018[Mar]; 12 (1 ): 301-308 PMID29086200 show ga Periostin is a secretory protein with a multi-domain structure, comprising an amino-terminal cysteine-rich EMI domain, four internal FAS 1 domains, and a carboxyl-terminal hydrophilic domain. These adjacent domains bind to extracellular matrix proteins (type I collagen, fibronectin, tenascin-C, and laminin ?2), and BMP-1 that catalyzes crosslinking of type I collagen, and proteoglycans, which play a role in cell adhesion. The binding sites on periostin have been demonstrated to contribute to the mechanical strength of connective tissues, enhancing intermolecular interactions in close proximity and their assembly into extracellular matrix architectures, where periostin plays further essential roles in physiological maintenance and pathological progression. Furthermore, periostin also binds to Notch 1 and CCN3, which have functions in maintenance of stemness, thus opening up a new field of periostin action. äPeriostin function in communication with extracellular matrices (epmc).pdf DeepDyve Pubget Overpricing