About: Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein

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About: Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein
Creator	Hou, Ming-Hon Wang, Chin-Tien Wang, Shiu-Mei Huang, Tai-Huang Lin, Shing-Yen Chiu, Ya-Li Lo, Yu-Sheng
Source	Elsevier; Medline; PMC
abstract	The coronavirus (CoV) N protein oligomerizes via its carboxyl terminus. However, the oligomerization mechanism of the C-terminal domains (CTD) of CoV N proteins remains unclear. Based on the protein disorder prediction system, a comprehensive series of HCoV-229E N protein mutants with truncated CTD was generated and systematically investigated by biophysical and biochemical analyses to clarify the role of the C-terminal tail of the HCoV-229E N protein in oligomerization. These results indicate that the last C-terminal tail plays an important role in dimer–dimer association. The C-terminal tail peptide is able to interfere with the oligomerization of the CTD of HCoV-229E N protein and performs the inhibitory effect on viral titre of HCoV-229E. This study may assist the development of anti-viral drugs against HCoV. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: N and C-terminal tail peptidebind by cosedimentation in solution (View interaction) N and Nbind by cosedimentation in solution (View Interaction: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12) C-terminal tail peptide and Nbind by fluorescence technology (View interaction) N and Nbind by cross-linking study (View interaction) N and Nbind by cross-linking study (View Interaction: 1, 2, 3, 4)
has issue date	2013-01-16(xsd:dateTime)
bibo:doi	10.1016/j.febslet.2012.11.016
bibo:pmid	23178926
has license	no-cc
sha1sum (hex)	166a54dc27b6e0a56a5e1a7e52fde365e466c99a
schema:url	https://doi.org/10.1016/j.febslet.2012.11.016
resource representing a document's title	Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein
has PubMed Central identifier	PMC7089611
has PubMed identifier	23178926
schema:publication	FEBS Lett
resource representing a document's body	covid:166a54dc27b6e0a56a5e1a7e52fde365e466c99a#body_text
is schema:about of	named entity 'tail' named entity 'C-terminal' named entity 'anti-viral' named entity 'interfere' named entity 'oligomerization' named entity 'STUDY' named entity 'VIRAL TITRE' named entity 'ASSOCIATION' named entity 'truncated' named entity 'titre' named entity 'oligomerization' named entity 'C-terminal' named entity 'oligomerization' named entity 'CTD' named entity 'dimer' named entity 'coronavirus' named entity '229E' named entity 'protein' named entity 'C-terminal tail' named entity 'protein' named entity 'protein' named entity 'dissociation constant' named entity 'transcription' named entity 'protein' named entity 'HCoV-229E' named entity 'lysis buffer' named entity 'gene' named entity 'centrifugation' named entity 'secondary structure' named entity 'C-terminal' named entity 'C-terminal tail' named entity 'RNP' named entity 'plasmid' named entity 'Taiwan' named entity 'archaeal proteins' named entity 'immunocompromised patients' named entity 'lysate' named entity 'amino acid sequence' named entity 'C-terminal' named entity 'fluorescence quenching' named entity 'PCR' named entity 'protein' named entity 'HCoV-229E' named entity 'C-terminal tail' named entity 'protein' named entity 'C-terminal tail' named entity 'C-terminal tail' named entity 'Sedimentation velocity' named entity 'MHV' named entity 'dissociation constant' named entity 'protein' named entity 'secondary structure' named entity 'protein' named entity 'Hill equation' named entity 'N377' named entity 'denaturation' named entity 'gene transcription' named entity 'C-terminal domain' named entity 'virion' named entity 'Netherlands' named entity 'Tris-HCl' named entity 'pneumonia' named entity 'C-terminal tail' named entity 'centrifugation' named entity 'peptide' named entity 'SARS-CoV' named entity 'HCoV-229E' named entity 'spectropolarimeter' named entity 'coronaviruses' named entity 'protein' named entity 'C-terminal domains' named entity 'bacteria' named entity 'protein' named entity 'structural domain' named entity 'C-terminal'

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