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.

10.1016/j.matbio.2015.01.021 http://scihub22266oqcxt.onion/10.1016/j.matbio.2015.01.021 C4446149!4446149 !25661773     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25661773 &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 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 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 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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25661773 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Matrix+Biol 2015 ; 43 (ä): 97-108 Nephropedia Template TP {{tp|p=25661773 |t=2015. A novel intracellular fibulin-1D variant binds to the cytoplasmic domain of integrin beta 1 subunit |pdf=|usr=}}{{25661773 }} gab.com Text A novel intracellular fibulin-1D variant binds to the cytoplasmic domain of integrin beta 1 subunit JO: Matrix Biol http://www.kidney.de/pget.php?&tw=1&pmid=25661773 #FOAvip Fibulin-1 is a member of a growing family of proteins that includes eight members and is involved in cellular functions such as adhesion, migration and differentiation. Fibulin-1 has also been implicated in embryonic development of the heart and neural crest-derived structures. It is an integral part of the extracellular matrix (ECM) and has been shown to bind to a multitude of ECM proteins. However, fibulin-1 was first identified as a protein purified from placental extracts that binds to the cytoplasmic domain of integrin ?1. Human fibulin-1 is alternatively spliced into four different isoforms namely A-D. These isoforms share a common N-terminus sequence that contains a secretion sequence but differ in their carboxy-terminal fibulin-1 module. In this report we identify a new splice variant of fibulin-1 that differs from all other fibulin-1 variants in the N-terminus sequence and has a similar carboxy-terminus sequence as fibulin-1D. This variant that we named fibulin-1D prime (fibulin-1D') lacks a secretion sequence and the anaphlatoxin region of fibulin-1 variants. The protein has an apparent molecular weight of 70.5kDa. Herein we show that fibulin-1D' binds to the intracellular domain of integrin ?1 as well as to integrin ?5?1. The protein was localized intracellularly in CHO cells transfected with a pEF4 plasmid containing full-length coding sequence of fibulin-1D'. We also localized the protein in human placenta. We propose that the fibulin-1D' variant might play a role in early embryo development as well as in modulating integrin ?1 functions including adhesion and motility. Twit Text FOAVip A novel intracellular fibulin-1D variant binds to the cytoplasmic domain of integrin beta 1 subunit ????Matrix Biol http://www.kidney.de/pget.php?&tw=1&pmid=25661773 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25661773 #FOAvip English Wikipedia <ref>{{Cite pmid|25661773 }}</ref> A novel intracellular fibulin-1D variant binds to the cytoplasmic domain of integrin beta 1 subunit #MMPMID25661773 Twal WO ; Hammad SM ; Guffy SL ; Argraves WS Matrix Biol 2015[Apr]; 43 (ä): 97-108 PMID25661773 show ga Fibulin-1 is a member of a growing family of proteins that includes eight members and is involved in cellular functions such as adhesion, migration and differentiation. Fibulin-1 has also been implicated in embryonic development of the heart and neural crest-derived structures. It is an integral part of the extracellular matrix (ECM) and has been shown to bind to a multitude of ECM proteins. However, fibulin-1 was first identified as a protein purified from placental extracts that binds to the cytoplasmic domain of integrin ?1. Human fibulin-1 is alternatively spliced into four different isoforms namely A-D. These isoforms share a common N-terminus sequence that contains a secretion sequence but differ in their carboxy-terminal fibulin-1 module. In this report we identify a new splice variant of fibulin-1 that differs from all other fibulin-1 variants in the N-terminus sequence and has a similar carboxy-terminus sequence as fibulin-1D. This variant that we named fibulin-1D prime (fibulin-1D') lacks a secretion sequence and the anaphlatoxin region of fibulin-1 variants. The protein has an apparent molecular weight of 70.5kDa. Herein we show that fibulin-1D' binds to the intracellular domain of integrin ?1 as well as to integrin ?5?1. The protein was localized intracellularly in CHO cells transfected with a pEF4 plasmid containing full-length coding sequence of fibulin-1D'. We also localized the protein in human placenta. We propose that the fibulin-1D' variant might play a role in early embryo development as well as in modulating integrin ?1 functions including adhesion and motility. |*Alternative Splicing [MESH] |Animals [MESH] |CHO Cells [MESH] |Calcium-Binding Proteins/chemistry/*genetics/*metabolism [MESH] |Cells, Cultured [MESH] |Cricetulus [MESH] |Female [MESH] |Humans [MESH] |Integrin alpha5beta1/metabolism [MESH] |Integrin beta1/chemistry/*metabolism [MESH] |Placenta/*metabolism [MESH] |Pregnancy [MESH]A novel intracellular fibulin-1D variant binds to the cytoplasmic doma(epmc).pdf DeepDyve Pubget Overpricing