Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Ammar A. E. Ali"'
Autor:
Mathieu Rappas, Ammar A. E. Ali, Kirstie A. Bennett, Jason D. Brown, Sarah J. Bucknell, Miles Congreve, Robert M. Cooke, Gabriella Cseke, Chris de Graaf, Andrew S. Doré, James C. Errey, Ali Jazayeri, Fiona H. Marshall, Jonathan S. Mason, Richard Mould, Jayesh C. Patel, Benjamin G. Tehan, Malcolm Weir, John A. Christopher
[Image: see text] The orexin system, which consists of the two G protein-coupled receptors OX(1) and OX(2), activated by the neuropeptides OX-A and OX-B, is firmly established as a key regulator of behavioral arousal, sleep, and wakefulness and has b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee0d1e9cf558d3f2bc1e5e706f4b6a9b
https://europepmc.org/articles/PMC7050010/
https://europepmc.org/articles/PMC7050010/
Autor:
Paul C. Driscoll, Stephanie Reich, Caroline L Cheetham, Renos Savva, Uma Bhattacharyya, Ammar A E Ali, Laurence H. Pearl, Richard Harris, Loretto H Puckey, Keith A Powell, Chrisostomos Prodromou, Kate Maclagan
Publikováno v:
Protein Science. 15:2356-2365
Exploitation of potential new targets for drug and vaccine development has an absolute requirement for multimilligram quantities of soluble protein. While recombinant expression of full-length proteins is frequently problematic, high-yield soluble ex
Autor:
Ammar A E Ali, Gyula Timinszky, Andreas G. Ladurner, Raquel Arribas-Bosacoma, Laurence H. Pearl, Paul O. Hassa, M. Kozlowski, Antony W. Oliver, Markus Hassler
Poly(ADP-ribose) polymerase I (PARP1) is a primary DNA damage sensor whose (ADP-ribose) polymerase activity is acutely regulated by interaction with DNA breaks. Upon activation at sites of DNA damage, PARP1 modifies itself and other proteins by coval
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b79c24c43cc714d1552232cac7a6e02f
https://europepmc.org/articles/PMC4826610/
https://europepmc.org/articles/PMC4826610/
Publikováno v:
Nucleic Acids Research
Short-patch repair of DNA single-strand breaks and gaps (SSB) is coordinated by XRCC1, a scaffold protein that recruits the DNA polymerase and DNA ligase required for filling and sealing the damaged strand. XRCC1 can also recruit end-processing enzym
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c28e41226fe8922b797adbb96c6f854
http://sro.sussex.ac.uk/id/eprint/29483/1/Nucl._Acids_Res.-2009-Ali-1701-12.pdf
http://sro.sussex.ac.uk/id/eprint/29483/1/Nucl._Acids_Res.-2009-Ali-1701-12.pdf
Autor:
M. Kozlowski, Raquel Arribas-Bosacoma, Laurence H. Pearl, Antony W. Oliver, Markus Hassler, Andreas G. Ladurner, Gyula Timinszky, Paul O. Hassa, Ammar A E Ali
Publikováno v:
Nature Structural & Molecular Biology. 22:645-645
Nat. Struct. Mol. Biol. 19, 685–692 (2012); published online 10 June 2012; corrected after print 10 July 2015 In the version of this article initially published, the image in the bottom row of Figure 4a (full-length PARP1-EGFP mutant R138E) was mis
Autor:
Antony W. Oliver, Markus Hassler, M. Kozlowski, Andreas G. Ladurner, Gyula Timinszky, Ammar A E Ali, Raquel Arribas-Bosacoma, Laurence H. Pearl, Paul O. Hassa
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 69:s69-s69