Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Tsueu-Ju Su"'
Publikováno v:
Journal of Fluorescence. 14:65-69
Single molecule fluorescence imaging incorporated with optical tweezers and a laminar flow cell has been used to monitor the kinetic process of DNA condensation induced by spermidine. It was found that at least two steps were involved in the condensa
Autor:
Gareth A. Roberts, Cowan Kennedy, Jakob T. Zipprich, Laurie P. Cooper, David T. F. Dryden, Tsueu-Ju Su, Paul Geary, John H. White
Publikováno v:
Roberts, G A, Cooper, L P, White, J H, Su, T-J, Zipprich, J T, Geary, P, Kennedy, C & Dryden, D T F 2011, ' An investigation of the structural requirements for ATP hydrolysis and DNA cleavage by the EcoKI Type I DNA restriction and modification enzyme ', Nucleic Acids Research, vol. 39, no. 17, pp. 7667-7676 . https://doi.org/10.1093/nar/gkr480
Nucleic Acids Research
Nucleic Acids Research
Type I DNA restriction/modification systems are oligomeric enzymes capable of switching between a methyltransferase function on hemimethylated host DNA and an endonuclease function on unmethylated foreign DNA. They have long been believed to not turn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a9de3f0377fcb01413786605bf02b76
https://www.pure.ed.ac.uk/ws/files/8735313/An_investigation_of_the_structural_requirements.pdf
https://www.pure.ed.ac.uk/ws/files/8735313/An_investigation_of_the_structural_requirements.pdf
Publikováno v:
Su, T-J, Tock, M R, Egelhaaf, S U, Poon, W C K & Dryden, D T F 2005, ' DNA bending by M.EcoKI methyltransferase is coupled to nucleotide flipping ', Nucleic Acids Research, vol. 33, no. 10, pp. 3235-3244 . https://doi.org/10.1093/nar/gki618
Nucleic Acids Research
Nucleic Acids Research
The maintenance methyltransferase M.EcoKI recognizes the bipartite DNA sequence 5'-A (A) under bar CNNN-NNNG (T) under bar GC-3', where N is any nucleotide. M.EcoKI preferentially methylates a sequence already containing a methylated adenine at or co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f913ae2388ba038eaba4c7d41755326c
https://hdl.handle.net/20.500.11820/589e3ab6-5985-4963-b5c0-80a05a880eba
https://hdl.handle.net/20.500.11820/589e3ab6-5985-4963-b5c0-80a05a880eba
Publikováno v:
Keatch, S A, Su, T J & Dryden, D T F 2004, ' Alleviation of restriction by DNA condensation and non-specific DNA binding ligands ', Nucleic Acids Research, vol. 32, no. 19, pp. 5841-5850 . https://doi.org/10.1093/nar/gkh918
During conditions of cell stress, the type I restriction and modification enzymes of bacteria show reduced, but not zero, levels of restriction of unmethylated foreign DNA. In such conditions, chemically identical unmethylated recognition sequences a
Autor:
David T. F. Dryden, Jochen Arlt, Tsueu Ju Su, Jason Crain, William J. Hossack, Eirini Theofanidou, Wilson C. K. Poon
Publikováno v:
Optical Trapping and Optical Micromanipulation.
The stretching and unwinding of polymers under flow is important for understanding the rheological properties of dilute polymer solutions. Scaling theory based on the blob picture of single polymer chains predicts several regimes for the overall shap
Autor:
David T. F. Dryden, Jochen Arlt, Tsueu Ju Su, Wilson C. K. Poon, Eirini Theofanidou, Jason Crain, William J. Hossack
Publikováno v:
Optical Trapping and Optical Micromanipulation.
We have observed a latency time of the order 10 s in the spermidine-induced condensation of YOYO-1-labelled DNA in flow. Higher flow speeds, longer DNA and higher salt all led to an increase in the latency time. We propose that two effects may be rel
Publikováno v:
Su, T J, Connolly, B A, Darlington, C, Mallin, R & Dryden, D T F 2004, ' Unusual 2-aminopurine fluorescence from a complex of DNA and the EcoKI methyltransferase ', Nucleic Acids Research, vol. 32, no. 7, pp. 2223-2230 . https://doi.org/10.1093/nar/gkh531
The methyltransferase, M.EcoKI, recognizes the DNA sequence 5'-A (A) under bar CNNNNNNG (T) under bar TGC-3' and methylates adenine at the underlined positions. DNA methylation has been shown by crystallography to occur via a base flipping mechanism
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f2ae4d98e347914e3cf9f802b140964
https://europepmc.org/articles/PMC407817/
https://europepmc.org/articles/PMC407817/
Publikováno v:
Atanasiu, C, Su, T J, Sturrock, S S & Dryden, D T F 2002, ' Interaction of the ocr gene 0.3 protein of bacteriophage T7 with EcoKI restriction/modification enzyme ', Nucleic Acids Research, vol. 30, no. 18, pp. 3936-3944 . https://doi.org/10.1093/nar/gkf518
The ocr protein, the product of gene 0.3 of bacteriophage T7, is a structural mimic of the phosphate backbone of B-form DNA. In total it mimics 22 phosphate groups over similar to24 bp of DNA. This mimicry allows it to block DNA binding by type I DNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17497d0133baf89bdc718d2c6a8eff3c
https://europepmc.org/articles/PMC137103/
https://europepmc.org/articles/PMC137103/
Autor:
Buck, Amy H.1, Campbell, Colin J.1,2 colin.campbell@ed.ac.uk, Dickinson, Paul1, Mountford, Christopher P.3, Stoquert, Hélène C.1, Terry, Jonathan G.4, Evans, Stuart A. G.2, Keane, Lorraine M.1, Tsueu-Ju Su3, Mount, Andrew R.2, Walton, Anthony J.4, Beattie, John S.1, Crain, Jason3, Ghazal, Peter1 p.ghazal@ed.ac.uk
Publikováno v:
Analytical Chemistry. 6/15/2007, Vol. 79 Issue 12, p4724-4728. 5p. 4 Graphs.