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230202 ||| eng |
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|a 9783036556963
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|a books978-3-0365-5695-6
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|a 9783036556956
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|a Coen, Donald M.
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| 245 |
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|a Viruses and Nuclear Egress
|h Elektronische Ressource
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| 260 |
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|a Basel
|b MDPI - Multidisciplinary Digital Publishing Institute
|c 2022
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| 300 |
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|a 1 electronic resource (182 p.)
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| 653 |
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|a herpesvirus
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|a virus assembly
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|a VAPB
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|a pseudorabies virus
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|a CMV
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|a pUL34
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|a de-envelopment
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|a PrV
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|a n/a
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|a phosphorylation
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|a vesicle-associated membrane protein associated protein
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|a VAPA
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|a major capsid protein
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|a HSV1
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|a CRISPR/Cas9 genome editing
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| 653 |
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|a mass spectrometry
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|a targeting integral membrane proteins
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|a virus-cell interactions
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|a herpesviruses
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|a nuclear import
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|a enveloped virus budding
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|a complementing cells
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|a BFRF1
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|a UL53
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|a UL50
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|a capsid migration
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|a NEC
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|a nuclear envelope modulation
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|a membrane scission
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| 653 |
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|a Research & information: general / bicssc
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|a differential functional relevance
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| 653 |
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|a importins
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| 653 |
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|a virus genetics
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| 653 |
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|a Biology, life sciences / bicssc
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| 653 |
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|a BGLF4 kinase
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| 653 |
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|a ORF-UL50 deletion
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| 653 |
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|a core nuclear egress complex
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|a ESCRT
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|a primary envelopment
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|a human cytomegalovirus
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|a nuclear envelopment complex
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|a pUL50 phosphosite mutants
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| 653 |
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|a Microbiology (non-medical) / bicssc
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|a Epstein-Barr virus
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| 653 |
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|a peptide therapy
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|a null mutants
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| 653 |
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|a nuclear egress
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| 653 |
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|a membrane fusion
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| 653 |
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|a TA membrane proteins
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|a tegument
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|a pUL31
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|a phenotypical changes
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|a hemi-fusion
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|a myosin Va
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| 653 |
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|a inner nuclear membrane (INM)
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| 700 |
1 |
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|a Coen, Donald M.
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| 041 |
0 |
7 |
|a eng
|2 ISO 639-2
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| 989 |
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|b DOAB
|a Directory of Open Access Books
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| 500 |
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|a Creative Commons (cc), https://creativecommons.org/licenses/by/4.0/
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| 028 |
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|a 10.3390/books978-3-0365-5695-6
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| 856 |
4 |
2 |
|u https://directory.doabooks.org/handle/20.500.12854/93861
|z DOAB: description of the publication
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| 856 |
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|u https://www.mdpi.com/books/pdfview/book/6291
|7 0
|x Verlag
|3 Volltext
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| 082 |
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|a 000
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|a 576
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|a 333
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|a 304
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|a 140
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|a This Special Issue of Viruses focuses on the topic of viruses and nuclear egress. Nuclear egress is a fascinating process by which herpesvirus nucleocapsids make their way from the nuclear interior to the cytoplasm. As nuclear egress and the viral proteins that orchestrate it differ from host processes and proteins in important ways, there is interest in targeting antiviral therapies to disrupt this process. Indeed, the recently approved drug maribavir acts in large part by inhibiting a step of nuclear egress. The Special Issue includes five reviews-three on nuclear egress of two alphaherpesviruses, herpes simplex virus and pseudorabies virus; one on a betaherpevirus, human cytomegalovirus; and one on a gammaherpesvirus, Epstein-Barr virus-and five research papers-two on alphaherpesviruses and three on human cytomegalovirus.
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