Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Sharon J. Schultz"'
Autor:
Sharon J. Schultz, James J. Champoux
Publikováno v:
FEBS Journal. 276:1506-1516
Retroviral reverse transcriptases possess both a DNA polymerase and an RNase H activity. The linkage with the DNA polymerase activity endows the retroviral RNases H with unique properties not found in the cellular counterparts. In addition to the typ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::665023102cb36a0bacc4523bd4236044
https://doi.org/10.1111/j.1742-4658.2009.06909.x
https://doi.org/10.1111/j.1742-4658.2009.06909.x
Publikováno v:
Journal of Biological Chemistry. 281:1943-1955
The RNase H activity of reverse transcriptase is essential for retroviral replication. RNA 5'-end-directed cleavages represent a form of RNase H activity that is carried out on RNA/DNA hybrids that contain a recessed RNA 5'-end. Previously, the dista
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b42819a3a11ff221785d877342b1a3ba
https://doi.org/10.1074/jbc.m510504200
https://doi.org/10.1074/jbc.m510504200
Publikováno v:
Journal of Biological Chemistry. 275:32299-32309
The ability of reverse transcriptase to generate, extend, and remove the primer derived from the polypurine tract (PPT) is vital for reverse transcription, since this process determines one of the ends required for integration of the viral DNA. Based
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ab178ebd756fe522912fd8ac48ee7eb
https://doi.org/10.1074/jbc.m000021200
https://doi.org/10.1074/jbc.m000021200
Publikováno v:
Journal of Biological Chemistry. 274:34547-34555
During reverse transcription, the RNase H activity of reverse transcriptase specifically cleaves the viral genome within the polypurine tract (PPT) to create the primer used for the initiation of plus-strand DNA synthesis and nonspecifically cleaves
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f614be062a807309c9a5266d8e28b82c
https://doi.org/10.1074/jbc.274.49.34547
https://doi.org/10.1074/jbc.274.49.34547
Autor:
James J. Champoux, Sharon J. Schultz
Publikováno v:
Journal of Virology. 70:8630-8638
The reverse transcriptase-associated RNase H activity of Moloney murine leukemia virus specifically cleaves within the polypurine tract region of the viral genome to generate the primer for plus-strand DNA synthesis and removes the tRNA primer after
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d3b4b4cccba55343fd17c01a1fd139c
https://doi.org/10.1128/jvi.70.12.8630-8638.1996
https://doi.org/10.1128/jvi.70.12.8630-8638.1996
Publikováno v:
The Journal of Cell Biology
The activity of cyclin-dependent kinases (cdks) depends on the phosphorylation of a residue corresponding to threonine 161 in human p34cdc2. One enzyme responsible for phosphorylating this critical residue has recently been purified from Xenopus and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ed0c98b424bcc2e98786ab8ec0b1069
https://doi.org/10.1083/jcb.127.2.467
https://doi.org/10.1083/jcb.127.2.467
Autor:
Andrew Ziemiecki, Erich A. Nigg, Sharon J. Schultz, Roy M. Golsteyn, Jiri Bartek, Thomas Ried
Publikováno v:
Europe PubMed Central
polo and CDC5 are two genes required for passage through mitosis in Drosophila melanogaster and Saccharomyces cerevisiae, respectively. Both genes encode structurally related protein kinases that have been implicated in regulating the function of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fba62eba601ae480eade6e8b1a6593e9
https://doi.org/10.1242/jcs.107.6.1509
https://doi.org/10.1242/jcs.107.6.1509
Multiple nucleotide preferences determine cleavage site recognition by the HIV-1 and M-MuLV RNases H
The RNase H activity of reverse transcriptase is required during retroviral replication and represents a potential target in anti-viral drug therapies. Sequence features flanking a cleavage site influence the three types of retroviral RNase H activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68b3dfb9a68a30e21c74109feb2dbd9c
https://europepmc.org/articles/PMC2830385/
https://europepmc.org/articles/PMC2830385/
The RNase H activity of reverse transcriptase carries out three types of cleavage termed internal, RNA 5′ end-directed, and DNA 3′ end-directed. Given the strong association between the polymerase domain of reverse transcriptase and a DNA 3′ pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf09187e66a89fd6714edfd283c01263
https://europepmc.org/articles/PMC2781635/
https://europepmc.org/articles/PMC2781635/
Autor:
Sharon J. Schultz, James J. Champoux
This review compares the well-studied RNase H activities of human immunodeficiency virus, type 1 (HIV-1) and Moloney murine leukemia virus (MoMLV) reverse transcriptases. The RNase H domains of HIV-1 and MoMLV are structurally very similar, with func
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9672ccc9191cf7efce72df74827fb0b5
https://europepmc.org/articles/PMC2464458/
https://europepmc.org/articles/PMC2464458/