Search Results - "Bellamy, Stuart R.W."

rapid reaction analysis of uracil DNA glycosylase indicates an active mechanism of base flipping by Bellamy, Stuart R.W, Krusong, Kuakarun, Baldwin, Geoff S

“…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…”
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One recognition sequence, seven restriction enzymes, five reaction mechanisms by Gowers, Darren M., Bellamy, Stuart R.W., Halford, Stephen E.

“…The diversity of reaction mechanisms employed by Type II restriction enzymes was investigated by analysing the reactions of seven endonucleases at the same DNA…”
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Targeting individual subunits of the FokI restriction endonuclease to specific DNA strands by Sanders, Kelly L, Catto, Lucy E, Bellamy, Stuart R.W, Halford, Stephen E

“…Many restriction endonucleases are dimers that act symmetrically at palindromic DNA sequences, with each active site cutting one strand. In contrast, FokI acts…”
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Dissecting protein-induced DNA looping dynamics in real time by Laurens, Niels, Bellamy, Stuart R.W, Harms, August F, Kovacheva, Yana S, Halford, Stephen E, Wuite, Gijs J.L

“…Many proteins that interact with DNA perform or enhance their specific functions by binding simultaneously to multiple target sites, thereby inducing a loop in…”
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The Asymmetric ATPase Cycle of the Thermosome: Elucidation of the Binding, Hydrolysis and Product-release Steps by Bigotti, Maria Giulia, Bellamy, Stuart R.W., Clarke, Anthony R.

“…Using a combination of intrinsic fluorescence to report ATP-induced rearrangements, quenched-flow to measure ATP hydrolysis “on-enzyme” and optical methods to…”
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A Switch in the Mechanism of Communication between the Two DNA-Binding Sites in the SfiI Restriction Endonuclease by Bellamy, Stuart R.W., Milsom, Susan E., Kovacheva, Yana S., Sessions, Richard B., Halford, Stephen E.

“…While many Type II restriction enzymes are dimers with a single DNA-binding cleft between the subunits, SfiI is a tetramer of identical subunits. Two of its…”
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Differences between Ca²⁺ and Mg²⁺ in DNA binding and release by the SfiI restriction endonuclease: implications for DNA looping by Bellamy, Stuart R.W, Kovacheva, Yana S, Zulkipli, Ishan Haji, Halford, Stephen E

“…Many enzymes acting on DNA require Mg²⁺ ions not only for catalysis but also to bind DNA. Binding studies often employ Ca²⁺ as a substitute for Mg²⁺, to…”
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A Comparative Study of Uracil-DNA Glycosylases from Human and Herpes Simplex Virus Type 1 by Krusong, Kuakarun, Carpenter, Elisabeth P., Bellamy, Stuart R.W., Savva, Renos, Baldwin, Geoff S.

“…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…”
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Dynamics and consequences of DNA looping by the FokI restriction endonuclease by Catto, Lucy E., Bellamy, Stuart R. W., Retter, Susan E., Halford, Stephen E.

“…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…”
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The Impact of Bending and Twisting Rigidity of DNA on Protein Induced Looping Dynamics by Laurens, Niels, Pernstich, Christian, Catto, Lucy E., Harms, August F., Kovacheva, Yana S., Bellamy, Stuart R.W., Halford, Stephen E., Wuite, Gijs J.L.

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Cleavage of Individual DNA Strands by the Different Subunits of the Heterodimeric Restriction Endonuclease BbvCI by Bellamy, Stuart R.W., Milsom, Susan E., Scott, David J., Daniels, Lucy E., Wilson, Geoffrey G., Halford, Stephen E.

“…BbvCI cleaves an asymmetric DNA sequence, 5′-CC↓TCAGC-3′/5′-GC↓TGAGG-3′, as indicated. While many Type II restriction enzymes consist of identical subunits,…”
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Fidelity of DNA Sequence Recognition by the SfiI Restriction Endonuclease Is Determined by Communications between Its Two DNA-Binding Sites by Bellamy, Stuart R.W., Mina, Petros, Retter, Susan E., Halford, Stephen E.

“…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…”
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A kinetic analysis of substrate recognition by uracil-DNA glycosylase from herpes simplex virus type 1 by Bellamy, S R, Baldwin, G S

“…Uracil-DNA glycosylase (UDG) is responsible for the removal of uracil from DNA. It has previously been demonstrated that UDG exhibits some sequence dependence…”
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