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10.1007/978-94-024-0945-1_2 http://scihub22266oqcxt.onion/10.1007/978-94-024-0945-1_2 C5493979!5493979 !27830500     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27830500 &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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27830500 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Subcell+Biochem 2016 ; 81 (ä): 21-76 Nephropedia Template TP {{tp|p=27830500 |t=2016. Functions of Intracellular Retinoid Binding-Proteins |pdf=|usr=}}{{27830500 }} gab.com Text Functions of Intracellular Retinoid Binding-Proteins JO: Subcell Biochem http://www.kidney.de/pget.php?&tw=1&pmid=27830500 #FOAvip Multiple binding and transport proteins facilitate many aspects of retinoid biology through effects on retinoid transport, cellular uptake, metabolism, and nuclear delivery. These include the serum retinol binding protein sRBP (aka Rbp4), the plasma membrane sRBP receptor Stra6, and the intracellular retinoid binding-proteins such as cellular retinol-binding proteins (CRBP) and cellular retinoic acid binding-proteins (CRABP). sRBP transports the highly lipophilic retinol through an aqueous medium. The major intracellular retinol-binding protein, CRBP1, likely enhances efficient retinoid use by providing a sink to facilitate retinol uptake from sRBP through the plasma membrane or via Stra6, delivering retinol or retinal to select enzymes that generate retinyl esters or retinoic acid, and protecting retinol/retinal from excess catabolism or opportunistic metabolism. Intracellular retinoic acid binding-proteins (CRABP1 and 2, and FABP5) seem to have more diverse functions distinctive to each, such as directing retinoic acid to catabolism, delivering retinoic acid to specific nuclear receptors, and generating non-canonical actions. Gene ablation of intracellular retinoid binding-proteins does not cause embryonic lethality or gross morphological defects. Metabolic and functional defects manifested in knockouts of CRBP1, CRBP2 and CRBP3, however, illustrate their essentiality to health, and in the case of CRBP2, to survival during limited dietary vitamin A. Future studies should continue to address the specific molecular interactions that occur between retinoid binding-proteins and their targets and their precise physiologic contributions to retinoid homeostasis and function. Twit Text FOAVip Functions of Intracellular Retinoid Binding-Proteins ????Subcell Biochem http://www.kidney.de/pget.php?&tw=1&pmid=27830500 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27830500 #FOAvip English Wikipedia <ref>{{Cite pmid|27830500 }}</ref> Functions of Intracellular Retinoid Binding-Proteins #MMPMID27830500 Napoli JL Subcell Biochem 2016[]; 81 (ä): 21-76 PMID27830500 show ga Multiple binding and transport proteins facilitate many aspects of retinoid biology through effects on retinoid transport, cellular uptake, metabolism, and nuclear delivery. These include the serum retinol binding protein sRBP (aka Rbp4), the plasma membrane sRBP receptor Stra6, and the intracellular retinoid binding-proteins such as cellular retinol-binding proteins (CRBP) and cellular retinoic acid binding-proteins (CRABP). sRBP transports the highly lipophilic retinol through an aqueous medium. The major intracellular retinol-binding protein, CRBP1, likely enhances efficient retinoid use by providing a sink to facilitate retinol uptake from sRBP through the plasma membrane or via Stra6, delivering retinol or retinal to select enzymes that generate retinyl esters or retinoic acid, and protecting retinol/retinal from excess catabolism or opportunistic metabolism. Intracellular retinoic acid binding-proteins (CRABP1 and 2, and FABP5) seem to have more diverse functions distinctive to each, such as directing retinoic acid to catabolism, delivering retinoic acid to specific nuclear receptors, and generating non-canonical actions. Gene ablation of intracellular retinoid binding-proteins does not cause embryonic lethality or gross morphological defects. Metabolic and functional defects manifested in knockouts of CRBP1, CRBP2 and CRBP3, however, illustrate their essentiality to health, and in the case of CRBP2, to survival during limited dietary vitamin A. Future studies should continue to address the specific molecular interactions that occur between retinoid binding-proteins and their targets and their precise physiologic contributions to retinoid homeostasis and function. |Alcohol Oxidoreductases/metabolism [MESH] |Aldehyde Dehydrogenase/metabolism [MESH] |Animals [MESH] |Biological Transport [MESH] |Cell Nucleus/metabolism [MESH] |Eye/metabolism [MESH] |Gene Knockout Techniques [MESH] |Homeostasis [MESH] |Humans [MESH] |Intestinal Mucosa/metabolism [MESH] |Mice [MESH] |Mice, Knockout [MESH] |Models, Molecular [MESH] |Neoplasm Proteins/metabolism [MESH] |Protein Conformation [MESH] |Receptors, Cytoplasmic and Nuclear/metabolism [MESH] |Retinaldehyde/metabolism [MESH] |Retinoids/*physiology [MESH] |Retinol-Binding Proteins, Cellular/chemistry/deficiency/genetics/*physiology [MESH] |Signal Transduction/physiology [MESH] |Tretinoin/metabolism [MESH]Functions of Intracellular Retinoid Binding-Proteins (epmc).pdf DeepDyve Pubget Overpricing