Zobrazeno 1 - 10
of 67
pro vyhledávání: '"Richard J Roller"'
Autor:
Elizabeth B Draganova, Hui Wang, Melanie Wu, Shiqing Liao, Amber Vu, Gonzalo L Gonzalez-Del Pino, Z Hong Zhou, Richard J Roller, Ekaterina E Heldwein
Publikováno v:
PLoS Pathogens, Vol 20, Iss 1, p e1011936 (2024)
Nuclear egress is an essential process in herpesvirus replication whereby nascent capsids translocate from the nucleus to the cytoplasm. This initial step of nuclear egress-budding at the inner nuclear membrane-is coordinated by the nuclear egress co
Externí odkaz:
https://doaj.org/article/4ec664c6fbd343e48c9bf997df69f327
Autor:
Patrick M. Schlievert, Richard J. Roller, Samuel H. Kilgore, Miguel Villarreal, Aloysius J. Klingelhutz, Donald Y. M. Leung
Publikováno v:
mSphere, Vol 6, Iss 4 (2021)
Atopic dermatitis (eczema, AD) with concurrent herpes simplex virus infection (eczema herpeticum, ADEH) is a severe form of AD. We show that ADEH patients are colonized with Staphylococcus aureus
Externí odkaz:
https://doaj.org/article/e5432896453a400eab3651f9e5d0ae5f
Autor:
Richard J. Roller, David C. Johnson
Publikováno v:
Viruses, Vol 13, Iss 12, p 2356 (2021)
Herpesvirus capsids are assembled in the nucleus and undergo a two-step process to cross the nuclear envelope. Capsids bud into the inner nuclear membrane (INM) aided by the nuclear egress complex (NEC) proteins UL31/34. At that stage of egress, enve
Externí odkaz:
https://doaj.org/article/240cb7605756475a862b816fdf9af65d
Publikováno v:
bioRxiv
Herpesviruses transport nucleocapsids from the nucleus to the cytoplasm by capsid envelopment into the inner nuclear membrane and de-envelopment from the outer nuclear membrane, a process that is coordinated by nuclear egress complex (NEC) proteins,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21de35af8a47615289b8bff15ca24f18
https://doi.org/10.1101/2023.03.20.533584
https://doi.org/10.1101/2023.03.20.533584
Dynein motors are microtubule associated protein complexes that mediate multiple essential cellular processes, such as long-distance cargo trafficking and stabilization of the microtubule organization center. Most of these functions and their regulat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::637cbea8360bae528eee5948f89d4933
https://doi.org/10.1101/2022.03.21.485087
https://doi.org/10.1101/2022.03.21.485087
Autor:
David C. Johnson, Richard J. Roller
Publikováno v:
Viruses
Viruses, Vol 13, Iss 2356, p 2356 (2021)
Viruses, Vol 13, Iss 2356, p 2356 (2021)
Herpesvirus capsids are assembled in the nucleus and undergo a two-step process to cross the nuclear envelope. Capsids bud into the inner nuclear membrane (INM) aided by the nuclear egress complex (NEC) proteins UL31/34. At that stage of egress, enve
Publikováno v:
J Virol
Herpes simplex virus (HSV) and varicella-zoster virus (VZV) are both members of the alphaherpesvirus subfamily but belong to different genera. Substitution of the HSV-1 UL34 coding sequence with that of its VZV homolog, open reading frame 24 (ORF24),
Autor:
Aloysius J. Klingelhutz, Donald Y.M. Leung, Richard J. Roller, Patrick M. Schlievert, Samuel H. Kilgore, Miguel Villarreal
Publikováno v:
mSphere
mSphere, Vol 6, Iss 4 (2021)
mSphere, Vol 6, Iss 4 (2021)
Atopic dermatitis (AD) is a condition affecting 30 million persons in the United States. AD patients are heavily infected with Staphylococcus aureus on the skin. A particularly severe form of AD is eczema herpeticum (ADEH), where the patients’ AD i
Publikováno v:
J Virol
Nuclear envelope budding in herpesvirus nuclear egress may be negatively regulated, since the pUL31/pUL34 nuclear egress complex heterodimer can induce membrane budding without capsids when expressed ectopically or on artificial membranes in vitro, b
HSV and VZV are both members of the alphaherpesvirus subfamily, but are of different genera. Substitution of the HSV-1 UL34 coding sequence with that of its VZV homolog, ORF24, results in a virus that has defects in viral growth, spread, capsid egres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8d30e5db77668d9cfd665115b0a9f136
https://doi.org/10.1101/2021.06.18.449081
https://doi.org/10.1101/2021.06.18.449081