Zobrazeno 1 - 10
of 58
pro vyhledávání: '"William J. McGrath"'
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Extremely compact environments can inhibit protein interactions by preventing 3-dimensional diffusion. Here the authors show that an 11-amino acid long peptide can function as a ‘molecular sled’, able to transport cargo linearly along DNA to enab
Externí odkaz:
https://doaj.org/article/17ca686a1607463e8cf9d6dac2de694a
Publikováno v:
BioTechniques, Vol 29, Iss 5, Pp 1108-1113 (2000)
Cells and body fluids contain numerous, different proteinases; to identify and characterize them are both important and difficult tasks. Especially difficult to identify and characterize are highly specific proteinases. Here, we present an extremely
Externí odkaz:
https://doaj.org/article/ae1fdaf632f142168ba70718601e3d52
Autor:
Seamus Morrone, Walter F. Mangel, Andrew Robinson, Antoine M. van Oijen, Aartje C. Schulte, Jungsan Sohn, Lisanne M. Spenkelink, William J. McGrath, Hylkje Geertsema
Publikováno v:
Biophysical Journal. 108(4):949-956
Single-molecule fluorescence microscopy is a powerful tool for observing biomolecular interactions with high spatial and temporal resolution. Detecting fluorescent signals from individual labeled proteins above high levels of background fluorescence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6c58ed18b41738c0ffdaed09eee7f9f
Publikováno v:
Journal of Biological Chemistry. 288:2081-2091
The adenovirus proteinase (AVP), the first member of a new class of cysteine proteinases, is essential for the production of infectious virus, and here we report its structure at 0.98 A resolution. AVP, initially synthesized as an inactive enzyme, re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::41de1be943e21c1df2077ccb5f07f584
https://doi.org/10.1074/jbc.m112.407429
https://doi.org/10.1074/jbc.m112.407429
Autor:
S. Jane Flint, Walter F. Mangel, Ana J. Pérez-Berná, William J. McGrath, X. Sunney Xie, Vito Graziano, Paul C. Blainey, Carmen San Martín
Publikováno v:
Journal of Biological Chemistry. 288:2092-2102
Precursor proteins used in the assembly of adenovirus virions must be processed by the virally encoded adenovirus proteinase (AVP) before the virus particle becomes infectious. An activated adenovirus proteinase, the AVP-pVIc complex, was shown to sl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d65d28e866ac3016424ddea75ff5255c
https://doi.org/10.1074/jbc.m112.407460
https://doi.org/10.1074/jbc.m112.407460
Autor:
Urs F. Greber, Guobin Luo, William J. McGrath, Walter F. Mangel, Paul C. Blainey, Maarit Suomalainen, Paul Freimuth, X. Sunney Xie, Vito Graziano
Publikováno v:
Journal of Biological Chemistry. 288:2068-2080
SUMMARY Late in an adenovirus infection, the viral proteinase (AVP) becomes activated to process virion precursor proteins used in virus assembly. AVP is activated by two cofactors- the viral DNA and pVIc, an 11-amino acid peptide originating from th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41e4f2fe38a76ecc8b0e97d58151b9a7
https://doi.org/10.1074/jbc.m112.407312
https://doi.org/10.1074/jbc.m112.407312
Publikováno v:
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Nature Publishing Group
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Nature Publishing Group
Recently, we showed the adenovirus proteinase interacts productively with its protein substrates in vitro and in vivo in nascent virus particles via one-dimensional diffusion along the viral DNA. The mechanism by which this occurs has heretofore been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cef06525647a79cad1d6e6761edb0d09
https://pubmed.ncbi.nlm.nih.gov/26831565
https://pubmed.ncbi.nlm.nih.gov/26831565
Publikováno v:
Biochemistry. 45:14632-14641
The SARS coronavirus main proteinase (SARS CoV main proteinase) is required for the replication of the severe acute respiratory syndrome coronavirus (SARS CoV), the virus that causes SARS. One function of the enzyme is to process viral polyproteins.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46833bfbf46b18a33ebdb51f46303d22
https://doi.org/10.1021/bi061746y
https://doi.org/10.1021/bi061746y
Publikováno v:
Biochemistry. 44:8721-8729
The interactions of the human adenovirus proteinase (AVP) with polymers with high negative charge densities were characterized. AVP utilizes two viral cofactors for maximal enzyme activity (k(cat)/K(m)), the 11-amino acid peptide from the C-terminus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2baa545d05183f43bb54953fa375eaa6
https://doi.org/10.1021/bi0502240
https://doi.org/10.1021/bi0502240
Autor:
Keiji Takamoto, Walter F. Mangel, Sayan Gupta, Jennifer L. Perek, William J. McGrath, Donna W. Lee, Mark R. Chance
Publikováno v:
Molecular & Cellular Proteomics. 3:950-959
Human adenovirus proteinase (AVP) requires two cofactors for maximal activity: pVIc, a peptide derived from the C terminus of adenovirus precursor protein pVI, and the viral DNA. Synchrotron protein footprinting was used to map the solvent accessible
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07698836910246b0de059ff62b3673f9
https://doi.org/10.1074/mcp.m400037-mcp200
https://doi.org/10.1074/mcp.m400037-mcp200