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10.1128/MCB.00202-14 http://scihub22266oqcxt.onion/10.1128/MCB.00202-14 C4295385!4295385!25368379     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mol+Cell+Biol 2015 ; 35 (1): 277-87 Nephropedia Template TP {{tp|p=25368379|t=2015. The RASSF1A Tumor Suppressor Regulates XPA-Mediated DNA Repair |pdf=|usr=}}{{25368379}} gab.com Text The RASSF1A Tumor Suppressor Regulates XPA-Mediated DNA Repair JO: Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=25368379 #FOAvip RASSF1A may be the most frequently inactivated tumor suppressor identified in human cancer so far. It is a proapoptotic Ras effector and plays an important role in the apoptotic DNA damage response (DDR). We now show that in addition to DDR regulation, RASSF1A also plays a key role in the DNA repair process itself. We show that RASSF1A forms a DNA damage-regulated complex with the key DNA repair protein xeroderma pigmentosum A (XPA). XPA requires RASSF1A to exert full repair activity, and RASSF1A-deficient cells exhibit an impaired ability to repair DNA. Moreover, a cancer-associated RASSF1A single-nucleotide polymorphism (SNP) variant exhibits differential XPA binding and inhibits DNA repair. The interaction of XPA with other components of the repair complex, such as replication protein A (RPA), is controlled in part by a dynamic acetylation/deacetylation cycle. We found that RASSF1A and its SNP variant differentially regulate XPA protein acetylation, and the SNP variant hyperstabilizes the XPA-RPA70 complex. Thus, we identify two novel functions for RASSF1A in the control of DNA repair and protein acetylation. As RASSF1A modulates both apoptotic DDR and DNA repair, it may play an important and unanticipated role in coordinating the balance between repair and death after DNA damage. Twit Text FOAVip The RASSF1A Tumor Suppressor Regulates XPA-Mediated DNA Repair ????Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=25368379 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25368379 #FOAvip English Wikipedia <ref>{{Cite pmid|25368379}}</ref> The RASSF1A Tumor Suppressor Regulates XPA-Mediated DNA Repair #MMPMID25368379 Donninger H; Clark J; Rinaldo F; Nelson N; Barnoud T; Schmidt ML; Hobbing KR; Vos MD; Sils B; Clark GJ Mol Cell Biol 2015[Jan]; 35 (1): 277-87 PMID25368379show ga RASSF1A may be the most frequently inactivated tumor suppressor identified in human cancer so far. It is a proapoptotic Ras effector and plays an important role in the apoptotic DNA damage response (DDR). We now show that in addition to DDR regulation, RASSF1A also plays a key role in the DNA repair process itself. We show that RASSF1A forms a DNA damage-regulated complex with the key DNA repair protein xeroderma pigmentosum A (XPA). XPA requires RASSF1A to exert full repair activity, and RASSF1A-deficient cells exhibit an impaired ability to repair DNA. Moreover, a cancer-associated RASSF1A single-nucleotide polymorphism (SNP) variant exhibits differential XPA binding and inhibits DNA repair. The interaction of XPA with other components of the repair complex, such as replication protein A (RPA), is controlled in part by a dynamic acetylation/deacetylation cycle. We found that RASSF1A and its SNP variant differentially regulate XPA protein acetylation, and the SNP variant hyperstabilizes the XPA-RPA70 complex. Thus, we identify two novel functions for RASSF1A in the control of DNA repair and protein acetylation. As RASSF1A modulates both apoptotic DDR and DNA repair, it may play an important and unanticipated role in coordinating the balance between repair and death after DNA damage. äThe RASSF1A Tumor Suppressor Regulates XPA-Mediated DNA Repair (epmc).pdf DeepDyve Pubget Overpricing