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10.1016/j.semcdb.2020.09.013 http://scihub22266oqcxt.onion/10.1016/j.semcdb.2020.09.013 33092958!7572318!33092958     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Semin+Cell+Dev+Biol 2021 ; 111 (ä): 76-85 Nephropedia Template TP {{tp|p=33092958|t=2021. Substrate recognition by TRIM and TRIM-like proteins in innate immunity |pdf=|usr=}}{{33092958}} gab.com Text Substrate recognition by TRIM and TRIM-like proteins in innate immunity JO: Semin Cell Dev Biol http://www.kidney.de/pget.php?&tw=1&pmid=33092958 #FOAvip TRIM (Tripartite motif) and TRIM-like proteins have emerged as an important class of E3 ligases in innate immunity. Their functions range from activation or regulation of innate immune signaling pathway to direct detection and restriction of pathogens. Despite the importance, molecular mechanisms for many TRIM/TRIM-like proteins remain poorly characterized, in part due to challenges of identifying their substrates. In this review, we discuss several TRIM/TRIM-like proteins in RNA sensing pathways and viral restriction functions. We focus on those containing PRY-SPRY, the domain most frequently used for substrate recognition, and discuss emerging mechanisms that are commonly utilized by several TRIM/TRIM-like proteins to tightly control their interaction with the substrates. Twit Text FOAVip Substrate recognition by TRIM and TRIM-like proteins in innate immunity ????Semin Cell Dev Biol http://www.kidney.de/pget.php?&tw=1&pmid=33092958 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33092958 #FOAvip English Wikipedia <ref>{{Cite pmid|33092958}}</ref> Substrate recognition by TRIM and TRIM-like proteins in innate immunity #MMPMID33092958 Wang HT; Hur S Semin Cell Dev Biol 2021[Mar]; 111 (ä): 76-85 PMID33092958show ga TRIM (Tripartite motif) and TRIM-like proteins have emerged as an important class of E3 ligases in innate immunity. Their functions range from activation or regulation of innate immune signaling pathway to direct detection and restriction of pathogens. Despite the importance, molecular mechanisms for many TRIM/TRIM-like proteins remain poorly characterized, in part due to challenges of identifying their substrates. In this review, we discuss several TRIM/TRIM-like proteins in RNA sensing pathways and viral restriction functions. We focus on those containing PRY-SPRY, the domain most frequently used for substrate recognition, and discuss emerging mechanisms that are commonly utilized by several TRIM/TRIM-like proteins to tightly control their interaction with the substrates. |*Immunity, Innate[MESH] |Adaptor Proteins, Signal Transducing/genetics/immunology[MESH] |B30.2-SPRY Domain/*genetics[MESH] |DEAD Box Protein 58/*genetics/immunology[MESH] |Gene Expression Regulation[MESH] |Humans[MESH] |Interferon Regulatory Factor-3/genetics/immunology[MESH] |Interferon-Induced Helicase, IFIH1/*genetics/immunology[MESH] |Intracellular Signaling Peptides and Proteins/genetics/immunology[MESH] |Multigene Family[MESH] |Receptors, Immunologic/*genetics/immunology[MESH] |Signal Transduction[MESH] |Substrate Specificity[MESH] |Tripartite Motif Proteins/chemistry/classification/*genetics/immunology[MESH]Substrate recognition by TRIM and TRIM-like proteins in innate immunit(epmc).pdf DeepDyve Pubget Overpricing