Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Joanna Strachan"'
Autor:
Joanna Strachan, Orsolya Leidecker, Christos Spanos, Clementine Le Coz, Elliott Chapman, Ana Arsenijevic, Haidao Zhang, Ning Zhao, Elizabeth H. Bayne
Regulation by the small modifier SUMO is heavily dependent on spatial control of enzymes that mediate the attachment and removal of SUMO on substrate proteins. Here we show that in fission yeast, delocalisation of the SUMO protease Ulp1 from the nucl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::02671ae35a1b4e1e17b544d07bf1f63e
https://doi.org/10.1101/2022.11.02.514898
https://doi.org/10.1101/2022.11.02.514898
Autor:
Sarah Blair-Reid, Balraj Johal, Nicholas H. Keep, James F.J. Beesley, Ruth M Densham, Alice Fletcher, Joanna R. Morris, Joanna Strachan, Felicity Z. Watts, Robert A Baldock, Manuel Daza-Martin, Helen R Stone, Alexander J Garvin, Laurence H. Pearl, Robert K. Neely
The opposing activities of 53BP1 and BRCA1 influence pathway choice in DNA double-strand-break repair. How BRCA1 counteracts the inhibitory effect of 53BP1 on DNA resection and homologous recombination is unknown. Here we identify the site of BRCA1-B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d5102b97baddc2097e062b182765f63
http://sro.sussex.ac.uk/id/eprint/60891/1/28390_2_merged_1460992707.pdf
http://sro.sussex.ac.uk/id/eprint/60891/1/28390_2_merged_1460992707.pdf
Autor:
Debora Ruth Channing, Neil J. Oldham, Robert Layfield, Lucy V. Roach, Kleitos Sokratous, Jed Long, Mark S. Searle, Joanna Strachan
Publikováno v:
Journal of the American Chemical Society. 134:6416-6424
Non-covalent interactions between ubiquitin (Ub)-modified substrates and Ub-binding domains (UBDs) are fundamental to signal transduction by Ub receptor proteins. Poly-Ub chains, linked through isopeptide bonds between internal Lys residues and the C
Autor:
Neil J. Oldham, Jed Long, Lucy V. Roach, David Tooth, Robert Layfield, Joanna Strachan, Thomas P. Garner, Mark S. Searle, Kleitos Sokratous
Publikováno v:
Journal of Proteome Research. 11:1969-1980
The diverse influences of ubiquitin, mediated by its post-translational covalent modification of other proteins, have been extensively investigated. However, more recently roles for unanchored (nonsubstrate linked) polyubiquitin chains have also been
Autor:
Thomas P. Garner, Mark S. Searle, Joanna Strachan, Barry Shaw, Elizabeth C. Shedden, James R. Cavey, Jed Long, Robert Layfield
Publikováno v:
Biochemistry. 50:9076-9087
Ubiquitin (Ub) modifications are transduced by receptor proteins that use Ub-binding domains (UBDs) to recognize distinct interaction faces on the Ub surface. We report the nuclear magnetic resonance (NMR) solution structures of the A20-like zinc fin
Autor:
Thomas P. Garner, Barry Shaw, Joanna Strachan, Jed Long, Robert Layfield, Jennifer Adlington, James R. Cavey, Mark S. Searle
Publikováno v:
Biochemical Society transactions. 40(2)
UBDs [Ub (ubiquitin)-binding domains], which are typically small protein motifs of
Autor:
Joanna Strachan
Publikováno v:
Targeted Protein Database.
Publikováno v:
FEBS Letters. (23):4144-4147
Ubiquitin (Ub) is able to form polymeric isopeptide-linked chains through condensation of any of its seven lysine (Lys) residues with the C-terminus of an adjacent Ub monomer. Electrospray ionisation mass spectrometry (ESI-MS) of commercial in vitro-