Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping. - Wikidata - awgldk - TriplyDB

Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping.

Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping.

http://www.wikidata.org/entity/Q30479841

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Filming biomolecular processes by high-speed atomic force microscopy Direct observation of ATP-induced conformational changes in single P2X(4) receptors Imaging of nucleic acids with atomic force microscopy.Single-molecule dynamics of the DNA-EcoRII protein complexes revealed with high-speed atomic force microscopy.High-speed atomic force microscopy combined with inverted optical microscopy for studying cellular events.Long-tip high-speed atomic force microscopy for nanometer-scale imaging in live cells Opportunities in high-speed atomic force microscopy.Single molecular investigation of DNA looping and aggregation by restriction endonuclease BspMI.Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases Type III restriction-modification enzymes: a historical perspective MmeI: a minimal Type II restriction-modification system that only modifies one DNA strand for host protection DNA cleavage site selection by Type III restriction enzymes provides evidence for head-on protein collisions following 1D bidirectional motion.Visual analysis of concerted cleavage by type IIF restriction enzyme SfiI in subsecond time region Chromosome Compaction by Active Loop Extrusion.Type III restriction enzymes communicate in 1D without looping between their target sites.AFM for analysis of structure and dynamics of DNA and protein-DNA complexes Maintaining a sense of direction during long-range communication on DNA.Preparation of DNA and nucleoprotein samples for AFM imaging.High-resolution imaging and nano-manipulation of biological structures on surface.Conflicts targeting epigenetic systems and their resolution by cell death: novel concepts for methyl-specific and other restriction systems DNA translocation by type III restriction enzymes: a comparison of current models of their operation derived from ensemble and single-molecule measurements.Visualizing cellulase activity.Highlights of the DNA cutters: a short history of the restriction enzymes DNA substrate preparation for atomic force microscopy studies of protein-DNA interactions.Structural dynamics of single molecules studied with high-speed atomic force microscopy.Type III restriction endonucleases are heterotrimeric: comprising one helicase-nuclease subunit and a dimeric methyltransferase that binds only one specific DNA.Re-evaluating the kinetics of ATP hydrolysis during initiation of DNA sliding by Type III restriction enzymes.High-speed atomic force microscopy imaging of live mammalian cells.Single-stranded loops as end-label polarity markers for double-stranded linear DNA templates in atomic force microscopy.Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity.Dissociation from DNA of Type III Restriction-Modification enzymes during helicase-dependent motion and following endonuclease activity.Direct visualization of G-quadruplexes in DNA using atomic force microscopy.The single polypeptide restriction-modification enzyme LlaGI is a self-contained molecular motor that translocates DNA loops.Atomic force microscopy of the EcoKI Type I DNA restriction enzyme bound to DNA shows enzyme dimerization and DNA looping.Protein-DNA interactions in high speed AFM: single molecule diffusion analysis of human RAD54.Mathematical model suitable for efficient simulation of thin semi-flexible polymers in complex environments.Imaging DNA Structure by Atomic Force Microscopy.Fast microscopical dissection of action scenes played by Escherichia coli RNA polymerase.

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Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping.

http://www.wikidata.org/entity/Q30479841

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2007 nî lūn-bûn

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2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2007 թվականի հուլիսին հրատարակված գիտական հոդված

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2007年の論文

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Fast-scan atomic force microsc ...... DNA translocation and looping.

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Fast-scan atomic force microsc ...... DNA translocation and looping.

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Fast-scan atomic force microsc ...... DNA translocation and looping.

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Fast-scan atomic force microsc ...... DNA translocation and looping.

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Fast-scan atomic force microsc ...... DNA translocation and looping.

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Fast-scan atomic force microsc ...... DNA translocation and looping.

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Proceedings of the National Academy of Sciences of the United States of America

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Fast-scan atomic force microsc ...... DNA translocation and looping.

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David T F Dryden

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Desirazu N Rao

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J Michael Edwardson

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Kunio Takeyasu

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Masatoshi Yokokawa

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Neal Crampton

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Robert M Henderson

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Shige H Yoshimura

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P2860

Real-time observation of DNA looping dynamics of Type IIE restriction enzymes NaeI and NarI.

When a helicase is not a helicase: dsDNA tracking by the motor protein EcoR124I.

Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL.

A DNA-translocating Snf2 molecular motor: Saccharomyces cerevisiae Rdh54 displays processive translocation and extrudes DNA loops.

Direct visualization of dynamic protein-DNA interactions with a dedicated atomic force microscope.

A high-speed atomic force microscope for studying biological macromolecules.

Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I.

Direct observation of one-dimensional diffusion and transcription by Escherichia coli RNA polymerase.

Origin-specific unwinding of herpes simplex virus 1 DNA by the viral UL9 and ICP8 proteins: visualization of a specific preunwinding complex.

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104

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