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The protease of adenovirus serotype 2 requires cysteine residues for both activation and catalysis.
Grierson AW, Nicholson R, Talbot P, Webster A, Kemp G. Grierson AW, et al. Among authors: webster a. J Gen Virol. 1994 Oct;75 ( Pt 10):2761-4. doi: 10.1099/0022-1317-75-10-2761. J Gen Virol. 1994. PMID: 7931163
All conserved serine and cysteine residues were mutated separately and following expression in Escherichia coli their activity in a synthetic peptide assay was compared to that of wild-type recombinant protease. ...These results taken together with the known inhibition pro …
All conserved serine and cysteine residues were mutated separately and following expression in Escherichia coli their activity in a s …
Characterization of the adenovirus proteinase: development and use of a specific peptide assay.
Webster A, Russell WC, Kemp GD. Webster A, et al. J Gen Virol. 1989 Dec;70 ( Pt 12):3215-23. doi: 10.1099/0022-1317-70-12-3215. J Gen Virol. 1989. PMID: 2691632
MSGGAFSW was shown to be cleaved at the G-A bond when incubated with a source of Ad2 proteinase. Digestions were readily monitored by either fast protein liquid chromatography or thin layer electrophoresis, enabling the rapid production of quantitative data. ...The …
MSGGAFSW was shown to be cleaved at the G-A bond when incubated with a source of Ad2 proteinase. Digestions were readily monit …
Adenovirus DNA polymerase: domain organisation and interaction with preterminal protein.
Parker EJ, Botting CH, Webster A, Hay RT. Parker EJ, et al. Among authors: webster a. Nucleic Acids Res. 1998 Mar 1;26(5):1240-7. doi: 10.1093/nar/26.5.1240. Nucleic Acids Res. 1998. PMID: 9469832 Free PMC article.
These data indicate that, like other members of the pol alpha family of DNA polymerases, the adenovirus DNA polymerase has a multidomain structure and that interaction with preterminal protein takes place with non-contiguous regions of the polypeptide chain over a l …
These data indicate that, like other members of the pol alpha family of DNA polymerases, the adenovirus DNA polymerase has a multidom …
Role of preterminal protein processing in adenovirus replication.
Webster A, Leith IR, Nicholson J, Hounsell J, Hay RT. Webster A, et al. J Virol. 1997 Sep;71(9):6381-9. doi: 10.1128/JVI.71.9.6381-6389.1997. J Virol. 1997. PMID: 9261355 Free PMC article.
In vitro and in vivo studies of viral DNA replication reveal that iTP can act as a template for initiation and elongation and argue against a role for virus-encoded protease in switching off DNA replication. ...Therefore, a likely role for the processing of p …
In vitro and in vivo studies of viral DNA replication reveal that iTP can act as a template for initiation and elongation and argue a …
Domain organization of the adenovirus preterminal protein.
Webster A, Leith IR, Hay RT. Webster A, et al. J Virol. 1997 Jan;71(1):539-47. doi: 10.1128/JVI.71.1.539-547.1997. J Virol. 1997. PMID: 8985382 Free PMC article.
In adenovirus-infected cells, the virus-encoded preterminal protein and DNA polymerase form a heterodimer that is directly involved in initiation of DNA replication. ...These results suggest that preterminal protein contains a large, noncontiguous surface required f …
In adenovirus-infected cells, the virus-encoded preterminal protein and DNA polymerase form a heterodimer that is directly involved i …
The adenovirus protease is activated by a virus-coded disulphide-linked peptide.
Webster A, Hay RT, Kemp G. Webster A, et al. Cell. 1993 Jan 15;72(1):97-104. doi: 10.1016/0092-8674(93)90053-s. Cell. 1993. PMID: 8422686
Activity was reconstituted by a component of adenovirus virions, which was identified as GVQSLKRRRCF, a peptide derived from the virus protein pVI. ...This represents a novel strategy for controlling the activity of a protease that is required for viru …
Activity was reconstituted by a component of adenovirus virions, which was identified as GVQSLKRRRCF, a peptide derived from t …
The active adenovirus protease is the intact L3 23K protein.
Webster A, Kemp G. Webster A, et al. J Gen Virol. 1993 Jul;74 ( Pt 7):1415-20. doi: 10.1099/0022-1317-74-7-1415. J Gen Virol. 1993. PMID: 8336124
Molecular exclusion chromatography indicated that the protease is active as a monomer. Purified protease was shown to be inhibited by Zn2+ and Cu2+ and by some, but not all, recognized cysteine protease inhibitors, indicating participation of a thiol group and provi …
Molecular exclusion chromatography indicated that the protease is active as a monomer. Purified protease was shown to be inhibited by …
Adenovirus DNA binding protein: helix destabilising properties.
Monaghan A, Webster A, Hay RT. Monaghan A, et al. Among authors: webster a. Nucleic Acids Res. 1994 Mar 11;22(5):742-8. doi: 10.1093/nar/22.5.742. Nucleic Acids Res. 1994. PMID: 8139913 Free PMC article.
Duplex regions of DNA, created when a short DNA strand is annealed to its complementary sequence present in the single stranded form of M13 phage DNA, were efficiently unwound by DNA binding protein in a reaction that required neither ATP nor MgCl2. ...In support of …
Duplex regions of DNA, created when a short DNA strand is annealed to its complementary sequence present in the single stranded form …
Activation of adenovirus-coded protease and processing of preterminal protein.
Webster A, Leith IR, Hay RT. Webster A, et al. J Virol. 1994 Nov;68(11):7292-300. doi: 10.1128/JVI.68.11.7292-7300.1994. J Virol. 1994. PMID: 7933113 Free PMC article.
Adenoviruses code for a protease that is essential for infectivity and is activated by a disulfide-linked peptide, derived from the C terminus of the virus structural protein pVI (pVI-CT). ...DNA was not found to be a cofactor of the protease, as previously p …
Adenoviruses code for a protease that is essential for infectivity and is activated by a disulfide-linked peptide, derived fro …
Molecular interactions during adenovirus DNA replication.
Hay RT, Freeman A, Leith I, Monaghan A, Webster A. Hay RT, et al. Among authors: webster a. Curr Top Microbiol Immunol. 1995;199 ( Pt 2):31-48. doi: 10.1007/978-3-642-79499-5_2. Curr Top Microbiol Immunol. 1995. PMID: 7555069 Review. No abstract available.
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