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10.1042/BCJ20161050 http://scihub22266oqcxt.onion/10.1042/BCJ20161050 C5510646!5510646!28104757     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+J 2017 ; 474 (7): 1093-107 Nephropedia Template TP {{tp|p=28104757|t=2017. Analysis and identification of the Grem2 heparin/heparan sulfate-binding motif |pdf=|usr=}}{{28104757}} gab.com Text Analysis and identification of the Grem2 heparin/heparan sulfate-binding motif JO: Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=28104757 #FOAvip Bone morphogenetic proteins (BMPs) are regulated by extracellular antagonists of the DAN (differential screening-selected gene aberrative in neuroblastoma) family. Similar to the BMP ligands, certain DAN family members have been shown to interact with heparin and heparan sulfate (HS). Structural studies of DAN family members Gremlin-1 and Gremlin-2 (Grem2) have revealed a dimeric growth factor-like fold where a series of lysine residues cluster along one face of the protein. In the present study, we used mutagenesis, heparin-binding measurements, and cell surface-binding analysis to identify lysine residues that are important for heparin/HS binding in Grem2. We determined that residues involved in heparin/HS binding, while not necessary for BMP antagonism, merge with the heparin/HS-binding epitope of BMP2. Furthermore, the Grem2?BMP2 complex has higher affinity for heparin than the individual proteins and this affinity is not abrogated when the heparin/HS-binding epitope of Grem2 is attenuated. Overall, the present study shows that the Grem2 heparin/HS and BMP-binding epitopes are unique and independent, where, interestingly, the Grem2?BMP2 complex exhibits a significant increase in binding affinity toward heparin moieties that appear to be partially independent of the Grem2 heparin/HS-binding epitope. Twit Text FOAVip Analysis and identification of the Grem2 heparin/heparan sulfate-binding motif ????Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=28104757 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28104757 #FOAvip English Wikipedia <ref>{{Cite pmid|28104757}}</ref> Analysis and identification of the Grem2 heparin/heparan sulfate-binding motif #MMPMID28104757 Kattamuri C; Nolan K; Thompson TB Biochem J 2017[Mar]; 474 (7): 1093-107 PMID28104757show ga Bone morphogenetic proteins (BMPs) are regulated by extracellular antagonists of the DAN (differential screening-selected gene aberrative in neuroblastoma) family. Similar to the BMP ligands, certain DAN family members have been shown to interact with heparin and heparan sulfate (HS). Structural studies of DAN family members Gremlin-1 and Gremlin-2 (Grem2) have revealed a dimeric growth factor-like fold where a series of lysine residues cluster along one face of the protein. In the present study, we used mutagenesis, heparin-binding measurements, and cell surface-binding analysis to identify lysine residues that are important for heparin/HS binding in Grem2. We determined that residues involved in heparin/HS binding, while not necessary for BMP antagonism, merge with the heparin/HS-binding epitope of BMP2. Furthermore, the Grem2?BMP2 complex has higher affinity for heparin than the individual proteins and this affinity is not abrogated when the heparin/HS-binding epitope of Grem2 is attenuated. Overall, the present study shows that the Grem2 heparin/HS and BMP-binding epitopes are unique and independent, where, interestingly, the Grem2?BMP2 complex exhibits a significant increase in binding affinity toward heparin moieties that appear to be partially independent of the Grem2 heparin/HS-binding epitope. äAnalysis and identification of the Grem2 heparin/heparan sulfate-bindi(epmc).pdf DeepDyve Pubget Overpricing