Atomic force microscopy of the EcoKI Type I DNA restriction enzyme bound to DNA shows enzyme dimerization and DNA looping. - Wikidata - wikimedia - TriplyDB

Atomic force microscopy of the EcoKI Type I DNA restriction enzyme bound to DNA shows enzyme dimerization and DNA looping.

Atomic force microscopy of the EcoKI Type I DNA restriction enzyme bound to DNA shows enzyme dimerization and DNA looping.

http://www.wikidata.org/entity/Q43150435

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Atomic force microscopy (AFM) imaging suggests that stromal interaction molecule 1 (STIM1) binds to Orai1 with sixfold symmetry Crystal Structure and Molecular Imaging of the Nav Channel 3 Subunit Indicates a Trimeric Assembly DNA bridging and looping by HMO1 provides a mechanism for stabilizing nucleosome-free chromatin.Atomic force microscopy reveals the architecture of the epithelial sodium channel (ENaC)Structural model of FeoB, the iron transporter from Pseudomonas aeruginosa, predicts a cysteine lined, GTP-gated pore Unusual structures are present in DNA fragments containing super-long Huntingtin CAG repeats Assembly of high molecular weight complexes of lipin on a supported lipid bilayer observed by atomic force microscopy Single molecular investigation of DNA looping and aggregation by restriction endonuclease BspMI.Interference of intrinsic curvature of DNA by DNA-intercalating agents.Using DNA as a fiducial marker to study SMC complex interactions with the atomic force microscope.Structure and operation of the DNA-translocating type I DNA restriction enzymes.Regulation by interdomain communication of a headful packaging nuclease from bacteriophage T4.The sigma-1 receptor binds to the Nav1.5 voltage-gated Na+ channel with 4-fold symmetry.AFM studies of lambda repressor oligomers securing DNA loops Single-molecule studies of high-mobility group B architectural DNA bending proteins.DNA translocation by type III restriction enzymes: a comparison of current models of their operation derived from ensemble and single-molecule measurements.Type I restriction enzymes and their relatives.An investigation of the structural requirements for ATP hydrolysis and DNA cleavage by the EcoKI Type I DNA restriction and modification enzyme α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N-methyl-D-aspartate (NMDA) receptors adopt different subunit arrangements.Demonstration of a direct interaction between sigma-1 receptors and acid-sensing ion channels.Oligomerization and DNA binding of Ler, a master regulator of pathogenicity of enterohemorrhagic and enteropathogenic Escherichia coli Single-stranded loops as end-label polarity markers for double-stranded linear DNA templates in atomic force microscopy.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.A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes Direct evidence for functional TRPV1/TRPA1 heteromers

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Atomic force microscopy of the EcoKI Type I DNA restriction enzyme bound to DNA shows enzyme dimerization and DNA looping.

http://www.wikidata.org/entity/Q43150435

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年學術文章

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2009年學術文章

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name

Atomic force microscopy of the ...... dimerization and DNA looping.

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Atomic force microscopy of the ...... dimerization and DNA looping.

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type

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Atomic force microscopy of the ...... dimerization and DNA looping.

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Atomic force microscopy of the ...... dimerization and DNA looping.

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Atomic force microscopy of the ...... dimerization and DNA looping.

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Atomic force microscopy of the ...... dimerization and DNA looping.

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Nucleic Acids Research

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Atomic force microscopy of the ...... dimerization and DNA looping.

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P2093

David T F Dryden

http://www.w3.org/2001/XMLSchema#string

J Michael Edwardson

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John H White

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Kelly J Neaves

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Laurie P Cooper

http://www.w3.org/2001/XMLSchema#string

Robert M Henderson

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Stewart M Carnally

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P2860

Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle)

Nucleoside triphosphate-dependent restriction enzymes

How do site-specific DNA-binding proteins find their targets?

Biology of DNA restriction

On the DNA cleavage mechanism of Type I restriction enzymes

DNA bending by M.EcoKI methyltransferase is coupled to nucleotide flipping.

Structure and mechanism of multifunctional restriction endonucleases

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

Model for how type I restriction enzymes select cleavage sites in DNA.

DNA translocation blockage, a general mechanism of cleavage site selection by type I restriction enzymes.

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2053-2063

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10.1093/NAR/GKP042

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6

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37

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19223329

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2665228

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