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10.1073/pnas.2004500118 http://scihub22266oqcxt.onion/10.1073/pnas.2004500118 33397718!7812796!33397718     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (2): ä Nephropedia Template TP {{tp|p=33397718|t=2021. ADP-ribose and analogues bound to the deMARylating macrodomain from the bat coronavirus HKU4 |pdf=|usr=}}{{33397718}} gab.com Text ADP-ribose and analogues bound to the deMARylating macrodomain from the bat coronavirus HKU4 JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=33397718 #FOAvip Macrodomains are proteins that recognize and hydrolyze ADP ribose (ADPR) modifications of intracellular proteins. Macrodomains are implicated in viral genome replication and interference with host cell immune responses. They are important to the infectious cycle of Coronaviridae and Togaviridae viruses. We describe crystal structures of the conserved macrodomain from the bat coronavirus (CoV) HKU4 in complex with ligands. The structures reveal a binding cavity that accommodates ADPR and analogs via local structural changes within the pocket. Using a radioactive assay, we present evidence of mono-ADPR (MAR) hydrolase activity. In silico analysis presents further evidence on recognition of the ADPR modification for hydrolysis. Mutational analysis of residues within the binding pocket resulted in diminished enzymatic activity and binding affinity. We conclude that the common structural features observed in the macrodomain in a bat CoV contribute to a conserved function that can be extended to other known macrodomains. Twit Text FOAVip ADP-ribose and analogues bound to the deMARylating macrodomain from the bat coronavirus HKU4 ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=33397718 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33397718 #FOAvip English Wikipedia <ref>{{Cite pmid|33397718}}</ref> ADP-ribose and analogues bound to the deMARylating macrodomain from the bat coronavirus HKU4 #MMPMID33397718 Hammond RG; Schormann N; McPherson RL; Leung AKL; Deivanayagam CCS; Johnson MA Proc Natl Acad Sci U S A 2021[Jan]; 118 (2): ä PMID33397718show ga Macrodomains are proteins that recognize and hydrolyze ADP ribose (ADPR) modifications of intracellular proteins. Macrodomains are implicated in viral genome replication and interference with host cell immune responses. They are important to the infectious cycle of Coronaviridae and Togaviridae viruses. We describe crystal structures of the conserved macrodomain from the bat coronavirus (CoV) HKU4 in complex with ligands. The structures reveal a binding cavity that accommodates ADPR and analogs via local structural changes within the pocket. Using a radioactive assay, we present evidence of mono-ADPR (MAR) hydrolase activity. In silico analysis presents further evidence on recognition of the ADPR modification for hydrolysis. Mutational analysis of residues within the binding pocket resulted in diminished enzymatic activity and binding affinity. We conclude that the common structural features observed in the macrodomain in a bat CoV contribute to a conserved function that can be extended to other known macrodomains. |Adenosine Diphosphate Ribose/*chemistry[MESH] |Animals[MESH] |Binding Sites[MESH] |Chiroptera[MESH] |Coronavirus/*enzymology/genetics[MESH] |Crystallography, X-Ray[MESH] |Hydrolysis[MESH] |Pyrophosphatases/*chemistry/genetics[MESH]ADP-ribose and analogues bound to the deMARylating macrodomain from th(epmc).pdf DeepDyve Pubget Overpricing