Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Thomas A Ceska"'
Autor:
David McMillan, Laurence H. Pearl, Keith A Powell, Carl Brendan Doyle, Thomas A Ceska, Giles P Saville, Adeel Mushtaq, Stefanie Reich, Renos Savva, Rodger A. Allen, Daniel Christopher Brookings, David Knight, Haiping Gong, Christoph Meier
Publikováno v:
Journal of Structural Biology. 177:329-334
Structural biology studies typically require large quantities of pure, soluble protein. Currently the most widely-used method for obtaining such protein involves the use of bioinformatics and experimental methods to design constructs of the target, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73b39ccde00844740b3a6f2325c77790
https://doi.org/10.1016/j.jsb.2012.01.002
https://doi.org/10.1016/j.jsb.2012.01.002
Autor:
James O'Connell, Martyn Kim Robinson, Matthew P. Crump, Leo Spyracopoulos, Richard J. K. Taylor, Stuart C. Findlow, Thomas Allen Ceska, Rikki Peter Alexander, Sarah Catherine Archibald, Alistair James Henry, Anthony Shock
Publikováno v:
Biochemistry. 43:2394-2404
LFA-1 (lymphocyte function-associated antigen-1) plays a role in intercellular adhesion and lymphocyte trafficking and activation and is an attractive anti-inflammatory drug target. The alpha-subunit of LFA-1, in common with several other integrins,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d62849b0e28572e7e37b4f453c7a82ad
https://doi.org/10.1021/bi035422a
https://doi.org/10.1021/bi035422a
Autor:
Jane A. Grasby, Thomas A. Ceska, Dipak Patel, Jon R. Sayers, Joe J. Dervan, Min Feng, Peter J. Artymiuk
Publikováno v:
Proceedings of the National Academy of Sciences. 99:8542-8547
Previous structural studies on native T5 5′ nuclease, a member of the flap endonuclease family of structure-specific nucleases, demonstrated that this enzyme possesses an unusual helical arch mounted on the enzyme's active site. Based on this struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2db243db947b84a4edc4bd99c4d7400a
https://doi.org/10.1073/pnas.082241699
https://doi.org/10.1073/pnas.082241699
Autor:
Thomas A. Ceska, Jon R. Sayers
Publikováno v:
Trends in Biochemical Sciences. 23:331-336
Many processes, such as DNA replication, recombination and repair, produce branched DNA structures. These bifurcated molecules are trimmed by a group of homologous 5′–3′ exonucleases (also known as 5′ nucleases) in structure-specific cleavage
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63236018fabefeb3a38ec0c0b09ebe82
https://doi.org/10.1016/s0968-0004(98)01259-6
https://doi.org/10.1016/s0968-0004(98)01259-6
Autor:
Mark D. Carr, Mariusz Muzylak, David McMillan, Richard J. Franklin, Vaclav Veverka, Daniel Christopher Brookings, Joanne E. Compson, Kelly Le Riche, Laura Ellen Newnham, Carl Brendan Doyle, Thomas A Ceska, Rachael Garlish, James Petrie Turner, Jiye Shi, Bernadette Sweeney, Alistair James Henry, Patrick M. Slocombe, Jeffery Kennedy, Gill Holdsworth, Martyn K. Robinson
Publikováno v:
The Journal of biological chemistry. 287(32)
LRP5 and LRP6 are proteins predicted to contain four six-bladed β-propeller domains and both bind the bone-specific Wnt signaling antagonist sclerostin. Here, we report the crystal structure of the amino-terminal region of LRP6 and using NMR show th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::264cb99223c5808bb96a9f6cf30f0c4e
https://pubmed.ncbi.nlm.nih.gov/22696217
https://pubmed.ncbi.nlm.nih.gov/22696217
Autor:
Oliver Rausch, Kerry Jenkins, Joanne L. Fraser, George M. Buckley, Verity Margaret Sabin, Thomas A. Ceska, Lewis Gowers, William R. Pitt, Colin R. Groom, Alicia P. Higueruelo, Marianna D. Richard, David M. Parry, Trevor Morgan, Stephen Robert Mack
Publikováno v:
Bioorganicmedicinal chemistry letters. 18(11)
A potent IRAK-4 inhibitor was identified through routine project cross screening. The binding mode was inferred using a combination of in silico docking into an IRAK-4 homology model, surrogate crystal structure analysis and chemical analogue SAR.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73458a1509b3183d1d38a023eccb4ea9
https://pubmed.ncbi.nlm.nih.gov/18482836
https://pubmed.ncbi.nlm.nih.gov/18482836
Autor:
Thomas A. Ceska, Min Feng, Joe J. Dervan, Ihtshamul Haq, Dietrich Suck, Jon R. Sayers, Dipak Patel
Publikováno v:
Nature structuralmolecular biology. 11(5)
Flap endonucleases (FENs) have essential roles in DNA processing. They catalyze exonucleolytic and structure-specific endonucleolytic DNA cleavage reactions. Divalent metal ions are essential cofactors in both reactions. The crystal structure of FEN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72cae48d1bdf504a8b2a4505b27a2968
https://pubmed.ncbi.nlm.nih.gov/15077103
https://pubmed.ncbi.nlm.nih.gov/15077103
Efficient cellular DNA replication requires the activity of a 5′-3′ exonuclease. These enzymes are able to hydrolyze DNA⋅DNA and RNA⋅DNA substrates exonucleolytically, and they are structure-specific endonucleases. The 5′-3′ exonucleases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4944e718cc8a9c8a3d98246f5cad394d
https://europepmc.org/articles/PMC15089/
https://europepmc.org/articles/PMC15089/
Publikováno v:
Nucleic acids research. 25(21)
The three dimensional crystal structure of T5 5'-3' exonuclease was compared with that of two other members of the 5'-3' exonuclease family: T4 ribonuclease H and the N-terminal domain of Thermus aquaticus DNA polymerase I. Though these structures we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5abe6828a81daa6ca4ea5508d330fc37
https://pubmed.ncbi.nlm.nih.gov/9336450
https://pubmed.ncbi.nlm.nih.gov/9336450
Autor:
John OʼHara, Andrew Nesbitt, Alistair James Henry, Sam Philip Heywood, Thomas Allen Ceska, Alison Turner, James T. Heads, Bryan Smith
Publikováno v:
American Journal of Gastroenterology. 103:S430
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::49d20b3354cd32314a7edc4db9c6fd5c
https://doi.org/10.14309/00000434-200809001-01102
https://doi.org/10.14309/00000434-200809001-01102