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10.1007/s00441-015-2216-6 http://scihub22266oqcxt.onion/10.1007/s00441-015-2216-6 C4452579!4452579 !26017636     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 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\26017636 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Tissue+Res 2015 ; 360 (3 ): 529-44 Nephropedia Template TP {{tp|p=26017636 |t=2015. Molecular architecture and function of the hemidesmosome |pdf=|usr=}}{{26017636 }} gab.com Text Molecular architecture and function of the hemidesmosome JO: Cell Tissue Res http://www.kidney.de/pget.php?&tw=1&pmid=26017636 #FOAvip Hemidesmosomes are multiprotein complexes that facilitate the stable adhesion of basal epithelial cells to the underlying basement membrane. The mechanical stability of hemidesmosomes relies on multiple interactions of a few protein components that form a membrane-embedded tightly-ordered complex. The core of this complex is provided by integrin ?6?4 and P1a, an isoform of the cytoskeletal linker protein plectin that is specifically associated with hemidesmosomes. Integrin ?6?4 binds to the extracellular matrix protein laminin-332, whereas P1a forms a bridge to the cytoplasmic keratin intermediate filament network. Other important components are BPAG1e, the epithelial isoform of bullous pemphigoid antigen 1, BPAG2, a collagen-type transmembrane protein and CD151. Inherited or acquired diseases in which essential components of the hemidesmosome are missing or structurally altered result in tissue fragility and blistering. Modulation of hemidesmosome function is of crucial importance for a variety of biological processes, such as terminal differentiation of basal keratinocytes and keratinocyte migration during wound healing and carcinoma invasion. Here, we review the molecular characteristics of the proteins that make up the hemidesmosome core structure and summarize the current knowledge about how their assembly and turnover are regulated by transcriptional and post-translational mechanisms. Twit Text FOAVip Molecular architecture and function of the hemidesmosome ????Cell Tissue Res http://www.kidney.de/pget.php?&tw=1&pmid=26017636 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26017636 #FOAvip English Wikipedia <ref>{{Cite pmid|26017636 }}</ref> Molecular architecture and function of the hemidesmosome #MMPMID26017636 Walko G ; Castañón MJ ; Wiche G Cell Tissue Res 2015[Jun]; 360 (3 ): 529-44 PMID26017636 show ga Hemidesmosomes are multiprotein complexes that facilitate the stable adhesion of basal epithelial cells to the underlying basement membrane. The mechanical stability of hemidesmosomes relies on multiple interactions of a few protein components that form a membrane-embedded tightly-ordered complex. The core of this complex is provided by integrin ?6?4 and P1a, an isoform of the cytoskeletal linker protein plectin that is specifically associated with hemidesmosomes. Integrin ?6?4 binds to the extracellular matrix protein laminin-332, whereas P1a forms a bridge to the cytoplasmic keratin intermediate filament network. Other important components are BPAG1e, the epithelial isoform of bullous pemphigoid antigen 1, BPAG2, a collagen-type transmembrane protein and CD151. Inherited or acquired diseases in which essential components of the hemidesmosome are missing or structurally altered result in tissue fragility and blistering. Modulation of hemidesmosome function is of crucial importance for a variety of biological processes, such as terminal differentiation of basal keratinocytes and keratinocyte migration during wound healing and carcinoma invasion. Here, we review the molecular characteristics of the proteins that make up the hemidesmosome core structure and summarize the current knowledge about how their assembly and turnover are regulated by transcriptional and post-translational mechanisms. |Animals [MESH] |Basement Membrane/metabolism [MESH] |Hemidesmosomes/*metabolism [MESH] |Humans [MESH] |Intermediate Filaments/metabolism [MESH] |Models, Biological [MESH] |Protein Binding [MESH]Molecular architecture and function of the hemidesmosome (epmc).pdf DeepDyve Pubget Overpricing