2014
DOI: 10.1016/j.coviro.2014.01.003
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Segmented negative strand RNA virus nucleoprotein structure

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Cited by 39 publications
(35 citation statements)
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“…The NP/N protein is the most abundant element in the NSV RNPs, it provides the basis for their helical structure and is essential for the transcription and replication of full-length templates (for reviews see Ivanov et al, 2011;Reguera et al, 2014;Ruigrok et al, 2010;Ruigrok et al, 2011). The NSV NP/N proteins show a general crescent form with two domains.…”
Section: The Nucleoproteinmentioning
confidence: 99%
See 1 more Smart Citation
“…The NP/N protein is the most abundant element in the NSV RNPs, it provides the basis for their helical structure and is essential for the transcription and replication of full-length templates (for reviews see Ivanov et al, 2011;Reguera et al, 2014;Ruigrok et al, 2010;Ruigrok et al, 2011). The NSV NP/N proteins show a general crescent form with two domains.…”
Section: The Nucleoproteinmentioning
confidence: 99%
“…Due to space limitations, many important contributions could not be directly cited. More detailed information is available in recent specific reviews (Albertini et al, 2011;Boivin et al, 2010;Eisfeld et al, 2014;Fodor, 2013;Ivanov et al, 2011;Kranzusch and Whelan, 2012;MartinBenito and Ortin, 2013;Morin et al, 2013;Reguera et al, 2014;Resa-Infante et al, 2011;Ruigrok et al, 2010;Ruigrok et al, 2011;.…”
Section: Introductionmentioning
confidence: 96%
“…In the viral context, the negative-stranded genome RNA is entirely encapsidated by viral nucleoprotein and the promoter covered by the polymerase complex [21,22]. Moreover, recently solved atomic structures revealed that the canonical ''panhandle'' is actually not formed when in the polymerase-associated state, since the 5 0 and 3 0 extremities are bound on separate sites [23,24].…”
Section: How Can Rig-i Access the Encapsidated Panhandle?mentioning
confidence: 98%
“…The protein N thus has an important role in the protection of the viral genetic information. In the last 5 years, the crystal structure of N has been solved for many bunyavirus members, providing new insights into the mechanism of RNP assembly [69][70][71][72][73][74][75][76][77][78][79][80][81]. Briefly, the protein N of orthobunyaviruses binds to RNA in a positively charged cleft, formed by two-helical lobes [69][70][71][72][73]75].…”
Section: Virion Structurementioning
confidence: 99%