About: Viral calciomics: Interplays between Ca(2+) and virus

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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	Viral calciomics: Interplays between Ca(2+) and virus
Creator	Frey, Teryl Zhou, Yubin Yang, Jenny
Source	Elsevier; Medline; PMC
abstract	Ca(2+) is one of the most universal and versatile signaling molecules and is involved in almost every aspect of cellular processes. Viruses are adept at utilizing the universal Ca(2+) signal to create a tailored cellular environment that meets their own demands. This review summarizes most of the known mechanisms by which viruses perturb Ca(2+) homeostasis and utilize Ca(2+) and cellular Ca(2+)-binding proteins to their benefit in their replication cycles. Ca(2+) plays important roles in virion structure formation, virus entry, viral gene expression, posttranslational processing of viral proteins and virion maturation and release. As part of the review, we introduce an algorithm to identify linear “EF-hand” Ca(2+)-binding motifs which resulted in the prediction of a total of 93 previously unrecognized Ca(2+)-binding motifs in virus proteins. Many of these proteins are nonstructural proteins, a class of proteins among which Ca(2+) interactions had not been formerly appreciated. The presence of linear Ca(2+)-binding motifs in viral proteins enlarges the spectrum of Ca(2+)–virus interplay and expands the total scenario of viral calciomics.
has issue date	2009-07-01(xsd:dateTime)
bibo:doi	10.1016/j.ceca.2009.05.005
bibo:pmid	19535138
has license	green-oa
sha1sum (hex)	2545b20123907d2cac6f0b3dfc6ec6715ff37c34
schema:url	https://doi.org/10.1016/j.ceca.2009.05.005
resource representing a document's title	Viral calciomics: Interplays between Ca(2+) and virus
has PubMed Central identifier	PMC3449087
has PubMed identifier	19535138
schema:publication	Cell Calcium
resource representing a document's body	covid:2545b20123907d2cac6f0b3dfc6ec6715ff37c34#body_text
is schema:about of	named entity 'VIRUS' named entity 'VIRAL' named entity 'MATERIALS' named entity 'materials' named entity 'Glycoprotein' named entity 'viruses' named entity 'Polyprotein' named entity 'ssRNA' named entity 'Immediate-early protein' named entity 'protein' named entity 'Neuraminidase' named entity 'protein' named entity 'mRNA' named entity 'nsP1' named entity 'nsP1' named entity 'antigen' named entity 'capping enzyme' named entity 'HIV-1' named entity 'nsP1' named entity 'protein kinase' named entity 'capping enzyme' named entity 'Neuraminidase' named entity 'virus' named entity 'capping enzyme' named entity 'protein' named entity 'VP6' named entity 'RNA polymerase' named entity 'Envelope protein' named entity 'PRV' named entity 'capping enzyme' named entity 'DNA polymerase' named entity 'coronavirus' named entity 'Spike protein' named entity 'mRNA' named entity 'virus' named entity 'Spike protein' named entity 'viruses' named entity 'threonine' named entity 'Protease' named entity 'protein' named entity 'mRNA' named entity 'capping enzyme' named entity 'mRNA' named entity 'Capsid protein' named entity 'nsP1' named entity 'mRNA' named entity 'virus' named entity 'DNA-directed RNA polymerase' named entity 'Serine' named entity 'nsP1' named entity 'virus' named entity 'PsV' named entity 'protein' named entity 'RNA polymerase' named entity 'protein' named entity 'virus' named entity 'Viral'
is part of of	Viral calciomics: Interplays between Ca(2+) and virus covid:2545b20123907d2cac6f0b3dfc6ec6715ff37c34#body_text Ca(2+) is one of the most universal and versatile signaling molecules and is involved in almost every aspect of cellular processes. Viruses are adept at utilizing the universal Ca(2+) signal to create a tailored cellular environment that meets their own demands. This review summarizes most of the known mechanisms by which viruses perturb Ca(2+) homeostasis and utilize Ca(2+) and cellular Ca(2+)-binding proteins to their benefit in their replication cycles. Ca(2+) plays important roles in virion structure formation, virus entry, viral gene expression, posttranslational processing of viral proteins and virion maturation and release. As part of the review, we introduce an algorithm to identify linear “EF-hand” Ca(2+)-binding motifs which resulted in the prediction of a total of 93 previously unrecognized Ca(2+)-binding motifs in virus proteins. Many of these proteins are nonstructural proteins, a class of proteins among which Ca(2+) interactions had not been formerly appreciated. The presence of linear Ca(2+)-binding motifs in viral proteins enlarges the spectrum of Ca(2+)–virus interplay and expands the total scenario of viral calciomics.

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