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10.1002/pro.15 http://scihub22266oqcxt.onion/10.1002/pro.15 19177346!2708038!19177346     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=19177346&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       Protein+Sci 2009 ; 18 (1): 6-16 Nephropedia Template TP {{tp|p=19177346|t=2009. Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property |pdf=|usr=}}{{19177346}} gab.com Text Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property JO: Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=19177346 #FOAvip The polyproteins of coronaviruses are cleaved by viral proteases into at least 15 nonstructural proteins (Nsps). Consisting of five domains, Nsp3 is the largest of these (180-210 kDa). Among these domains, the so-called X-domain is believed to act as ADP-ribose-1''-phosphate phosphatase or to bind poly(ADP-ribose). However, here we show that the X-domain of Infectious Bronchitis Virus (strain Beaudette), a Group-3 coronavirus, fails to bind ADP-ribose. This is explained on the basis of the crystal structure of the protein, determined at two different pH values. For comparison, we also describe the crystal structure of the homologous X-domain from Human Coronavirus 229E, a Group-1 coronavirus, which does bind ADP-ribose. Twit Text FOAVip Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property ????Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=19177346 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19177346 #FOAvip English Wikipedia <ref>{{Cite pmid|19177346}}</ref> Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property #MMPMID19177346 Piotrowski Y; Hansen G; Boomaars-van der Zanden AL; Snijder EJ; Gorbalenya AE; Hilgenfeld R Protein Sci 2009[Jan]; 18 (1): 6-16 PMID19177346show ga The polyproteins of coronaviruses are cleaved by viral proteases into at least 15 nonstructural proteins (Nsps). Consisting of five domains, Nsp3 is the largest of these (180-210 kDa). Among these domains, the so-called X-domain is believed to act as ADP-ribose-1''-phosphate phosphatase or to bind poly(ADP-ribose). However, here we show that the X-domain of Infectious Bronchitis Virus (strain Beaudette), a Group-3 coronavirus, fails to bind ADP-ribose. This is explained on the basis of the crystal structure of the protein, determined at two different pH values. For comparison, we also describe the crystal structure of the homologous X-domain from Human Coronavirus 229E, a Group-1 coronavirus, which does bind ADP-ribose. |Adenosine Diphosphate Ribose/analogs & derivatives/chemistry/*metabolism[MESH] |Amino Acid Sequence[MESH] |Coronavirus 229E, Human/*chemistry/genetics/metabolism[MESH] |Crystallography, X-Ray[MESH] |Infectious bronchitis virus/*chemistry/genetics/metabolism[MESH] |Models, Molecular[MESH] |Molecular Sequence Data[MESH] |Phosphoric Monoester Hydrolases/chemistry/genetics/metabolism[MESH] |Protein Binding/physiology[MESH] |Protein Conformation[MESH] |Sequence Alignment[MESH] |Severe acute respiratory syndrome-related coronavirus/chemistry/genetics/metabolism[MESH]Crystal structures of the X-domains of a Group-1 and a Group-3 coronav(epmc).pdf DeepDyve Pubget Overpricing