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10.1016/j.ceb.2007.09.005 http://scihub22266oqcxt.onion/10.1016/j.ceb.2007.09.005 C4827755!4827755 !17942296     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\17942296 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Curr+Opin+Cell+Biol 2007 ; 19 (5 ): 578-83 Nephropedia Template TP {{tp|p=17942296 |t=2007. Extracellular matrix: from atomic resolution to ultrastructure |pdf=|usr=}}{{17942296 }} gab.com Text Extracellular matrix: from atomic resolution to ultrastructure JO: Curr Opin Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=17942296 #FOAvip The extracellular matrix (ECM) is a highly organized multimolecular structure, essential for life in higher organisms. Although substantial high-resolution structural information is available for relatively small fragments of ECM components, the inherent difficulty in preparing and analyzing samples of large, fibrous polymers impedes structural efforts. Here, we review recent advances in understanding the structure of three important ECM components: collagen, fibrillin and fibronectin. Emphasis is placed on the key role of intermolecular interactions in assembling larger, microm scale, structures. Twit Text FOAVip Extracellular matrix: from atomic resolution to ultrastructure ????Curr Opin Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=17942296 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=17942296 #FOAvip English Wikipedia <ref>{{Cite pmid|17942296 }}</ref> Extracellular matrix: from atomic resolution to ultrastructure #MMPMID17942296 Vakonakis I ; Campbell ID Curr Opin Cell Biol 2007[Oct]; 19 (5 ): 578-83 PMID17942296 show ga The extracellular matrix (ECM) is a highly organized multimolecular structure, essential for life in higher organisms. Although substantial high-resolution structural information is available for relatively small fragments of ECM components, the inherent difficulty in preparing and analyzing samples of large, fibrous polymers impedes structural efforts. Here, we review recent advances in understanding the structure of three important ECM components: collagen, fibrillin and fibronectin. Emphasis is placed on the key role of intermolecular interactions in assembling larger, microm scale, structures. |*Protein Conformation [MESH] |Animals [MESH] |Carbohydrate Conformation [MESH] |Collagen/metabolism/ultrastructure [MESH] |Extracellular Matrix/*chemistry/metabolism/*ultrastructure [MESH] |Fibrillins [MESH] |Fibronectins/metabolism/ultrastructure [MESH] |Microfilament Proteins/metabolism/ultrastructure [MESH] |Models, Molecular [MESH]Extracellular matrix: from atomic resolution to ultrastructure (epmc).pdf DeepDyve Pubget Overpricing