prikaz prve stranice dokumenta Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components
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Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components
Journal of General Virology, 97 (2016), 7; 1676-1685. https://doi.org/10.1099/jgv.0.000495
Sonntag, Eric; Hamilton, Stuart T.; Bahsi, Hanife; Wagner, Sabrina; Jonjić, Stipan; Rawlinson, William D.; Marschall, Manfred; Milbradt, Jens

Institucijski repozitorij: Repozitorij Medicinskog fakulteta u Rijeci

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Sonntag, E., Hamilton, S. T., Bahsi, H., Wagner, S., Jonjić, S., Rawlinson, W. D. ... Milbradt, J. (2016). Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components. Journal of General Virology, 97. (7), 1676-1685. doi: 10.1099/jgv.0.000495

Sonntag, Eric, et al. "Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components." Journal of General Virology, vol. 97, br. 7, 2016, str. 1676-1685. https://doi.org/10.1099/jgv.0.000495

Sonntag, Eric, Stuart T. Hamilton, Hanife Bahsi, Sabrina Wagner, Stipan Jonjić, William D. Rawlinson, Manfred Marschall i Jens Milbradt. "Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components." Journal of General Virology 97, br. 7 (2016): 1676-1685. https://doi.org/10.1099/jgv.0.000495

Sonntag, E., et al. (2016) 'Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components', Journal of General Virology, 97(7), str. 1676-1685. doi: 10.1099/jgv.0.000495

Sonntag E, Hamilton ST, Bahsi H, Wagner S, Jonjić S, Rawlinson WD, i sur.. Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components. Journal of General Virology [Internet]. 01.07.2016. [pristupljeno 24.12.2024.];97(7):1676-1685. doi: 10.1099/jgv.0.000495

E. Sonntag, et al., "Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components", Journal of General Virology, vol. 97, br. 7, str. 1676-1685, Srpanj 2016. [Online]. Dostupno na: https://urn.nsk.hr/urn:nbn:hr:184:757453. [Citirano: 24.12.2024.]

Za citiranje koristite ovu mrežnu adresu: https://urn.nsk.hr/urn:nbn:hr:184:757453
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Naslov (engleski)Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components
AutorEric Sonntag
AutorStuart T. Hamilton
AutorHanife Bahsi
AutorSabrina Wagner
AutorStipan Jonjić
AutorWilliam D. Rawlinson
AutorManfred Marschall
AutorJens Milbradt
Autorova ustanovaSveučilište u Rijeci
Medicinski fakultet
(Katedra za histologiju i embriologiju)
Znanstveno / umjetničko
područje, polje i grana		BIOMEDICINA I ZDRAVSTVO
Temeljne medicinske znanosti
Sažetak (hrvatski)
Nuclear egress of herpesvirus capsids through the nuclear envelope is mediated by the multimeric nuclear egress complex (NEC). The human cytomegalovirus (HCMV) core NEC is defined by an interaction between the membrane- anchored pUL50 and its nuclear co-factor pUL53, tightly associated through heterodimeric corecruitment to the nuclear envelope. Cellular proteins, such as p32/gC1qR, emerin and protein kinase C (PKC), are recruited by direct interaction with pUL50 for the multimeric extension of the NEC. As a functionally important event, the recruitment of both viral and cellular protein kinases leads to site- specific lamin phosphorylation and nuclear lamina disassembly. In this study, interaction domains within pUL50 for its binding partners were defined by co-immunoprecipitation. The interaction domain for pUL53 is located within the pUL50 N-terminus (residues 10-169), interaction domains for p32/gC1qR (100-358) and PKC (100-280) overlap in the central part of pUL50, and the interaction domain for emerin is located in the C-terminus (265-397). Moreover, expression and formation of core NEC proteins at the nuclear rim were consistently detected in cells permissive for productive HCMV replication, including two trophoblast-cell lines. Importantly, regular nuclear-rim formation of the core NEC was blocked by inhibition of cyclin-dependent kinase (CDK) activity. In relation to the recently published crystal structure of the HCMV core NEC, our findings result in a refined view of NEC assembly. In particular, we suggest that CDKs may play an important regulatory role in NEC formation during HCMV replica.
Ključne riječi (engleski)
Jezikengleski
Vrsta publikacijeZnanstveni rad - Izvorni znanstveni rad
Status objaveObjavljen
Vrsta recenzijeRecenziran - međunarodna recenzija
Verzija publikacijeObjavljena verzija rada (izdavačev PDF)
Naslov časopisaJournal of General Virology
Brojčani podacivol. 97, br. 7, str. 1676-1685
p-ISSN0022-1317
e-ISSN1465-2099
DOIhttps://doi.org/10.1099/jgv.0.000495
URN:NBNurn:nbn:hr:184:757453
Datum objave publikacije2016-07-01
ProjektŠifra: 062-0621261-1263
Naziv (hrvatski): Molekularni mehanizmi citomegalovirusnog izmicanja imunološkom nadzoru
Voditelj: Stipan Jonjić
Pravna nadležnost: Hrvatska
Financijer: MZOS
Linija financiranja: ZP
ProjektŠifra: 262067
Naziv (engleski): Proteomics Research Infrastructure Maximising knowledge EXchange and access (XS)
Kratica: PRIME-XS
Pravna nadležnost: eu
Financijer: EC
Linija financiranja: FP7
URL dokumentahttp://www.microbiologyresearch.org/content/journal/jgv/10.1099/jgv.0.000495
Vrsta resursaTekst
Prava pristupaOtvoreni pristup
Uvjeti korištenjaIkona licence Imenovanje-Nekomercijalno-Bez prerada 4.0 međunarodna (CC BY-NC-ND 4.0)
Datum i vrijeme pohrane2018-11-07 09:36:29