Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Jeffrey J. Hollins"'
Publikováno v:
Journal of Molecular Biology. 430:2468-2477
The BCL-2 family of proteins plays a central role in regulating cell survival and apoptosis. Disordered BH3-only proteins bind promiscuously to a number of different BCL-2 proteins, with binding affinities that vary by orders of magnitude. Here we in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1c5d6f11bddc8e74276f86c66a4870d
https://doi.org/10.1016/j.jmb.2018.04.004
https://doi.org/10.1016/j.jmb.2018.04.004
Autor:
Stephan Wickles, Roland Beckmann, Ola B. Nilsson, Gunnar von Heijne, Annette Steward, Adrian A. Nickson, Jane Clarke, Jeffrey J. Hollins
Publikováno v:
Nature Structural & Molecular Biology. 24:221-225
How do the key features of protein folding, elucidated from studies on native, isolated proteins, manifest in cotranslational folding on the ribosome? Using a well-characterized family of homologous α-helical proteins with a range of biophysical pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c2d8a13206fed1ab2a04a2860619ace
https://doi.org/10.1038/nsmb.3355
https://doi.org/10.1038/nsmb.3355
Autor:
Pengfei, Tian, Annette, Steward, Renuka, Kudva, Ting, Su, Patrick J, Shilling, Adrian A, Nickson, Jeffrey J, Hollins, Roland, Beckmann, Gunnar, von Heijne, Jane, Clarke, Robert B, Best
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Most proteins need to fold into a specific 3D structure to function. The mechanism by which isolated proteins fold has been thoroughly studied by experiment and theory. However, in the cell proteins do not fold in isolation but are synth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b1da5287b17dd6d5cc33f4434e108d86
https://pubmed.ncbi.nlm.nih.gov/30413621
https://pubmed.ncbi.nlm.nih.gov/30413621
Autor:
Jeffrey J. Hollins, Renuka Kudva, Patrick J. Shilling, Robert B. Best, Pengfei Tian, Gunnar von Heijne, Jane Clarke, Adrian A. Nickson, Ting Su, Annette Steward, Roland Beckmann
Proteins that fold cotranslationally may do so in a restricted configurational space, due to the volume occupied by the ribosome. How does this environment, coupled with the close proximity of the ribosome, affect the folding pathway of a protein? Pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e708943f8d9aaad72c5e0d3b2678d59
https://doi.org/10.1101/253013
https://doi.org/10.1101/253013
Publikováno v:
Biochemical Society Transactions. 41:1072-1077
Phosphorylation is a ubiquitous protein post-translational modification, and the importance of phosphorylation of serine, threonine and tyrosine is well established. What is lesser known is that almost all heteroatom-containing amino acids can be pho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f09930797842f4cfb8d44c25bcb32f2
https://doi.org/10.1042/bst20130071
https://doi.org/10.1042/bst20130071
Autor:
Natalia Rukazenkova, Geoffrey P. Margison, Ghazala Begum, Cátia M P F Caetano, Amna Butt, Andrew S. Marriott, Jeffrey J. Hollins, Mauro Santibanez-Koref, Steven J Pearson, Amanda J. Watson, Stephen J. Wharton
Publikováno v:
DNA Repair. 6:1222-1228
Recent in silico analysis has revealed the presence of a group of proteins in pro and lower eukaryotes, but not in Man, that show extensive amino acid sequence similarity to known O6-alkylguanine-DNA alkyltransferases, but where the cysteine at the p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecf166a3b30031ae404ed9fffe87829f
https://doi.org/10.1016/j.dnarep.2007.03.014
https://doi.org/10.1016/j.dnarep.2007.03.014
Publikováno v:
Physical Chemistry Chemical Physics. 13:19427
We report herein the study of Förster resonance energy transfer (FRET) between a CdSe/ZnS core/shell quantum dot (QD) capped with three different small-molecule ligands, 3-mercaptopropionic acid (MPA), glutathione (GSH), and dihydrolipoic acid (DHLA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::925b06ca15f8d9050db836949c72f843
https://doi.org/10.1039/c1cp22024a
https://doi.org/10.1039/c1cp22024a