Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Stuart R.W. Bellamy"'
Autor:
Samantha J. Pitt, Rebecca Sitsapesan, Elena Galfrè, Elisa Venturi, Stuart R.W. Bellamy, Richard B. Sessions, Fiona O'Brien
Publikováno v:
Biophysical Journal. 106:824-833
Funding: British Heart Foundation We have previously shown that FKBP12 associates with RyR2 in cardiac muscle and that it modulates RyR2 function differently to FKBP12.6. We now investigate how these proteins affect the single-channel behavior of RyR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04fdfe02e5ef1a64b2e2ff77dd263b31
https://doi.org/10.1016/j.bpj.2013.12.041
https://doi.org/10.1016/j.bpj.2013.12.041
Publikováno v:
Composites Science and Technology. 74:150-159
The work describes the fibre extraction, manufacturing and testing of biocomposites made from cactus fibres and polyester matrix. A novel fibre extraction process has been developed, allowing the production of fibres from cactus cladodes with three d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ad02907295875284d92f3f889bd72d6b
https://doi.org/10.1016/j.compscitech.2012.10.009
https://doi.org/10.1016/j.compscitech.2012.10.009
Publikováno v:
Nucleic Acids Research
Many enzymes acting on DNA require Mg(2+) ions not only for catalysis but also to bind DNA. Binding studies often employ Ca(2+) as a substitute for Mg(2+), to promote DNA binding whilst disallowing catalysis. The SfiI endonuclease requires divalent m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bc5c0fd4e9a8093188c89060cc00bb6
https://doi.org/10.1093/nar/gkp569
https://doi.org/10.1093/nar/gkp569
Autor:
Stephen E. Halford, Stuart R.W. Bellamy, Niels Laurens, August F. Harms, Gijs J.L. Wuite, Yana S. Kovacheva
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, 5454-5464. Oxford University Press
STARTPAGE=5454;ENDPAGE=5464;ISSN=0305-1048;TITLE=Nucleic Acids Research
Laurens, N, Bellamy, S R W, Harms, A F, Kovacheva, Y S, Halford, S E & Wuite, G J L 2009, ' Dissecting protein-induced DNA looping dynamics in real time ', Nucleic Acids Research, pp. 5454-5464 . https://doi.org/10.1093/nar/gkp570
Nucleic Acids Research, 37(16), 5454-5464
Nucleic Acids Research, 5454-5464. Oxford University Press
STARTPAGE=5454;ENDPAGE=5464;ISSN=0305-1048;TITLE=Nucleic Acids Research
Laurens, N, Bellamy, S R W, Harms, A F, Kovacheva, Y S, Halford, S E & Wuite, G J L 2009, ' Dissecting protein-induced DNA looping dynamics in real time ', Nucleic Acids Research, pp. 5454-5464 . https://doi.org/10.1093/nar/gkp570
Nucleic Acids Research, 37(16), 5454-5464
Many proteins that interact with DNA perform or enhance their specific functions by binding simultaneously to multiple target sites, thereby inducing a loop in the DNA. The dynamics and energies involved in this loop formation influence the reaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d71090647f90ae9c27235ee26060a133
https://doi.org/10.1093/nar/gkp570
https://doi.org/10.1093/nar/gkp570
Publikováno v:
Nucleic Acids Research
Genetic events often require proteins to be activated by interacting with two DNA sites, trapping the intervening DNA in a loop. While much is known about looping equilibria, only a few studies have examined DNA-looping dynamics experimentally. The r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fd0a1ff81628e9a89e018348a5d9c32
https://doi.org/10.1093/nar/gkn051
https://doi.org/10.1093/nar/gkn051
Publikováno v:
Journal of Biological Chemistry. 281:4983-4992
Uracil-DNA glycosylase (UNG) is the key enzyme responsible for initiation of base excision repair. We have used both kinetic and binding assays for comparative analysis of UNG enzymes from humans and herpes simplex virus type 1 (HSV-1). Steady-state
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c81a8a7984ec5f9b795f3bdd88f95ae5
https://doi.org/10.1074/jbc.m509137200
https://doi.org/10.1074/jbc.m509137200
Publikováno v:
Nucleic Acids Research. 32:3469-3479
The diversity of reaction mechanisms employed by Type II restriction enzymes was investigated by analysing the reactions of seven endonucleases at the same DNA sequence. NarI, KasI, Mly113I, SfoI, EgeI, EheI and BbeI cleave DNA at several different p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d97b2dcf79a7c01f1a222ffd68224d7
https://doi.org/10.1093/nar/gkh685
https://doi.org/10.1093/nar/gkh685
Publikováno v:
Nucleic Acids Research
Many restriction endonucleases are dimers that act symmetrically at palindromic DNA sequences, with each active site cutting one strand. In contrast, FokI acts asymmetrically at a non-palindromic sequence, cutting ‘top’ and ‘bottom’ strands 9
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdb70a16181987482a8dfd5699ae3e32
https://pubmed.ncbi.nlm.nih.gov/19223323
https://pubmed.ncbi.nlm.nih.gov/19223323
Publikováno v:
Journal of molecular biology. 384(3)
The SfiI restriction endonuclease is a tetramer in which two subunits form a dimeric unit that contains one DNA binding cleft and the other two subunits contain a second cleft on the opposite side of the protein. Full activity requires both clefts to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5226ce55d83bcfd1ac52b4d22f85255
https://pubmed.ncbi.nlm.nih.gov/18848951
https://pubmed.ncbi.nlm.nih.gov/18848951
Publikováno v:
Nucleic Acids Research
Uracil DNA glycosylase (UNG) is the primary enzyme for the removal of uracil from the genome of many organisms. A key question is how the enzyme is able to scan large quantities of DNA in search of aberrant uracil residues. Central to this is the mec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f3303da61b577113647d7e50318059a
https://pubmed.ncbi.nlm.nih.gov/17284454
https://pubmed.ncbi.nlm.nih.gov/17284454