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10.1631/jzus.B2000319 http://scihub22266oqcxt.onion/10.1631/jzus.B2000319 33448184!7818011!33448184     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Zhejiang+Univ+Sci+B 2021 ; 22 (1): 21-30 Nephropedia Template TP {{tp|p=33448184|t=2021. ADP-ribosylhydrolases: from DNA damage repair to COVID-19 |pdf=|usr=}}{{33448184}} gab.com Text ADP-ribosylhydrolases: from DNA damage repair to COVID-19 JO: J Zhejiang Univ Sci B http://www.kidney.de/pget.php?&tw=1&pmid=33448184 #FOAvip Adenosine diphosphate (ADP)-ribosylation is a unique post-translational modification that regulates many biological processes, such as DNA damage repair. During DNA repair, ADP-ribosylation needs to be reversed by ADP-ribosylhydrolases. A group of ADP-ribosylhydrolases have a catalytic domain, namely the macrodomain, which is conserved in evolution from prokaryotes to humans. Not all macrodomains remove ADP-ribosylation. One set of macrodomains loses enzymatic activity and only binds to ADP-ribose (ADPR). Here, we summarize the biological functions of these macrodomains in DNA damage repair and compare the structure of enzymatically active and inactive macrodomains. Moreover, small molecular inhibitors have been developed that target macrodomains to suppress DNA damage repair and tumor growth. Macrodomain proteins are also expressed in pathogens, such as severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). However, these domains may not be directly involved in DNA damage repair in the hosts or pathogens. Instead, they play key roles in pathogen replication. Thus, by targeting macrodomains it may be possible to treat pathogen-induced diseases, such as coronavirus disease 2019 (COVID-19). Twit Text FOAVip ADP-ribosylhydrolases: from DNA damage repair to COVID-19 ????J Zhejiang Univ Sci B http://www.kidney.de/pget.php?&tw=1&pmid=33448184 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33448184 #FOAvip English Wikipedia <ref>{{Cite pmid|33448184}}</ref> ADP-ribosylhydrolases: from DNA damage repair to COVID-19 #MMPMID33448184 Yu L; Liu X; Yu X J Zhejiang Univ Sci B 2021[Jan]; 22 (1): 21-30 PMID33448184show ga Adenosine diphosphate (ADP)-ribosylation is a unique post-translational modification that regulates many biological processes, such as DNA damage repair. During DNA repair, ADP-ribosylation needs to be reversed by ADP-ribosylhydrolases. A group of ADP-ribosylhydrolases have a catalytic domain, namely the macrodomain, which is conserved in evolution from prokaryotes to humans. Not all macrodomains remove ADP-ribosylation. One set of macrodomains loses enzymatic activity and only binds to ADP-ribose (ADPR). Here, we summarize the biological functions of these macrodomains in DNA damage repair and compare the structure of enzymatically active and inactive macrodomains. Moreover, small molecular inhibitors have been developed that target macrodomains to suppress DNA damage repair and tumor growth. Macrodomain proteins are also expressed in pathogens, such as severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). However, these domains may not be directly involved in DNA damage repair in the hosts or pathogens. Instead, they play key roles in pathogen replication. Thus, by targeting macrodomains it may be possible to treat pathogen-induced diseases, such as coronavirus disease 2019 (COVID-19). |ADP-Ribosylation[MESH] |COVID-19/*metabolism[MESH] |DNA Repair/*physiology[MESH] |Evolution, Molecular[MESH] |Humans[MESH] |Models, Biological[MESH] |Models, Molecular[MESH] |N-Glycosyl Hydrolases/chemistry/*metabolism[MESH] |Poly(ADP-ribose) Polymerases/chemistry/metabolism[MESH] |Protein Domains[MESH]ADP-ribosylhydrolases: from DNA damage repair to COVID-19 (epmc).pdf DeepDyve Pubget Overpricing