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10.1002/pro.225 http://scihub22266oqcxt.onion/10.1002/pro.225 19691129!2788276!19691129     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Protein+Sci 2009 ; 18 (11): 2209-18 Nephropedia Template TP {{tp|p=19691129|t=2009. Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein |pdf=|usr=}}{{19691129}} gab.com Text Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein JO: Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=19691129 #FOAvip Human coronavirus OC43 (HCoV-OC43) is one of the causes of the "common cold" in human during seasons of cold weather. The primary function of the HCoV-OC43 nucleocapsid protein (N protein) is to recognize viral genomic RNA, which leads to ribonucleocapsid formation. Here, we characterized the stability and identified the functional regions of the recombinant HCoV-OC43 N protein. Circular dichroism and fluorescence measurements revealed that the HCoV-OC43 N protein is more highly ordered and stabler than the SARS-CoV N protein previously studied. Surface plasmon resonance (SPR) experiments showed that the affinity of HCoV-OC43 N protein for RNA was approximately fivefold higher than that of N protein for DNA. Moreover, we found that the HCoV-OC43 N protein contains three RNA-binding regions in its N-terminal region (residues 1-173) and central-linker region (residues 174-232 and 233-300). The binding affinities of the truncated N proteins and RNA follow the order: residues 1-173-residues 233-300 > residues 174-232. SPR experiments demonstrated that the C-terminal region (residues 301-448) of HCoV-OC43 N protein lacks RNA-binding activity, while crosslinking and gel filtration analyses revealed that the C-terminal region is mainly involved in the oligomerization of the HCoV-OC43 N protein. This study may benefit the understanding of the mechanism of HCoV-OC43 nucleocapsid formation. Twit Text FOAVip Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein ????Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=19691129 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19691129 #FOAvip English Wikipedia <ref>{{Cite pmid|19691129}}</ref> Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein #MMPMID19691129 Huang CY; Hsu YL; Chiang WL; Hou MH Protein Sci 2009[Nov]; 18 (11): 2209-18 PMID19691129show ga Human coronavirus OC43 (HCoV-OC43) is one of the causes of the "common cold" in human during seasons of cold weather. The primary function of the HCoV-OC43 nucleocapsid protein (N protein) is to recognize viral genomic RNA, which leads to ribonucleocapsid formation. Here, we characterized the stability and identified the functional regions of the recombinant HCoV-OC43 N protein. Circular dichroism and fluorescence measurements revealed that the HCoV-OC43 N protein is more highly ordered and stabler than the SARS-CoV N protein previously studied. Surface plasmon resonance (SPR) experiments showed that the affinity of HCoV-OC43 N protein for RNA was approximately fivefold higher than that of N protein for DNA. Moreover, we found that the HCoV-OC43 N protein contains three RNA-binding regions in its N-terminal region (residues 1-173) and central-linker region (residues 174-232 and 233-300). The binding affinities of the truncated N proteins and RNA follow the order: residues 1-173-residues 233-300 > residues 174-232. SPR experiments demonstrated that the C-terminal region (residues 301-448) of HCoV-OC43 N protein lacks RNA-binding activity, while crosslinking and gel filtration analyses revealed that the C-terminal region is mainly involved in the oligomerization of the HCoV-OC43 N protein. This study may benefit the understanding of the mechanism of HCoV-OC43 nucleocapsid formation. |Binding Sites[MESH] |Circular Dichroism[MESH] |Coronavirus Nucleocapsid Proteins[MESH] |Coronavirus OC43, Human/*chemistry[MESH] |Glutaral/chemistry[MESH] |Humans[MESH] |Nucleic Acids/metabolism[MESH] |Nucleocapsid Proteins/chemistry/*metabolism[MESH] |Protein Multimerization[MESH] |Protein Stability[MESH] |RNA-Binding Proteins/chemistry/*metabolism[MESH] |Recombinant Proteins/chemistry/*metabolism[MESH] |Spectrometry, Fluorescence[MESH]Elucidation of the stability and functional regions of the human coron(epmc).pdf DeepDyve Pubget Overpricing