Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Kristine E. Yoder"'
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
Abstract Retrovirus integration into a host genome is essential for productive infections. The integration strand transfer reaction is catalyzed by a nucleoprotein complex (Intasome) containing the viral integrase (IN) and the reverse transcribed (RT
Externí odkaz:
https://doaj.org/article/df319467e85541b5bb97a1a92aab50a7
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
Retroviruses are obligate intracellular parasites that must integrate a copy of the viral genome into the host DNA. The integration reaction is performed by the viral enzyme integrase in complex with the two ends of the viral cDNA genome and yields a
Externí odkaz:
https://doaj.org/article/bcf1d9da2b6b49bd90f5d328072acb32
Publikováno v:
Frontiers in Cellular and Infection Microbiology, Vol 10 (2020)
CRISPR editing of retroviral proviruses has been limited to HIV-1. We propose human T-cell leukemia virus type 1 (HTLV-1) as an excellent model to advance CRISPR/Cas9 genome editing technologies against actively expressing and latent retroviral provi
Externí odkaz:
https://doaj.org/article/4e2e2c79877a491bacacece2b1bd73ba
Publikováno v:
Biomolecules, Vol 11, Iss 12, p 1910 (2021)
Integrases of different retroviruses assemble as functional complexes with varying multimers of the protein. Retroviral integrases require a divalent metal cation to perform one-step transesterification catalysis. Tetrameric prototype foamy virus (PF
Externí odkaz:
https://doaj.org/article/50d6c6106d0c4d368abdd692035608cf
Publikováno v:
Frontiers in Microbiology, Vol 9 (2018)
HIV-1 infection can be successfully controlled with anti-retroviral therapy (ART), but is not cured. A reservoir of cells harboring transcriptionally silent integrated provirus is able to reestablish replicating infection if ART is stopped. Latently
Externí odkaz:
https://doaj.org/article/8331a60cf6164b1b9036f26a0d40fefa
Autor:
Nathan D. Jones, Miguel A. Lopez Jr, Jeungphill Hanne, Mitchell B. Peake, Jong-Bong Lee, Richard Fishel, Kristine E. Yoder
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
Retroviral Integration into the host DNA is a rare event with evidence suggesting that it relies on DNA topology and sequence. Here the authors present single molecule evidence that shows the retroviral integration machinery vigorously scans the targ
Externí odkaz:
https://doaj.org/article/4c0178fb357c4b6c9e3c7ff0e81765af
Human immunodeficiency virus (HIV-1) requires integration of the viral genome into the host DNA for replication. Efficient HIV-1 integration employs a host co-factor LEDGF/p75 to stabilize the HIV-1 integration complex and tether that complex to host
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f7371a2122cb8479effb08e1fa8e4460
https://doi.org/10.1101/2022.09.19.508505
https://doi.org/10.1101/2022.09.19.508505
Publikováno v:
Biotechnologies for Gene Therapy ISBN: 9783030933326
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::25f7aef110756732415de6f314a08377
https://doi.org/10.1007/978-3-030-93333-3_7
https://doi.org/10.1007/978-3-030-93333-3_7
Autor:
L. E. Baltierra-Jasso, A. Ballandras-Collas, Richard Fishel, Alan Engelman, Nathan D. Jones, Kristine E. Yoder
Retroviral intasomes are complexes assembled from purified integrase (IN) and oligonucleotides mimicking viral DNA ends (vDNA). Recombinant intasomes faithfully recapitulate integration of vDNA into a target DNA. Structural studies of retroviral inta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7ea2a8f7ee5942d0fc1a68700172f5d8
https://doi.org/10.1101/2021.11.17.468995
https://doi.org/10.1101/2021.11.17.468995
Integrase enzymes of different retroviruses assemble as functional complexes with varying multimers of the protein. Retroviral integrases require a divalent metal cation to perform one-step transesterification catalysis. Tetrameric prototype foamy vi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bdf8a9ecd7aec3433e047cbb2677be22
https://doi.org/10.1101/2021.11.17.469013
https://doi.org/10.1101/2021.11.17.469013