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Quantitative analysis of single-molecule RNA-protein interaction.

Quantitative analysis of single-molecule RNA-protein interaction.

http://www.wikidata.org/entity/Q37265282

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An hnRNP-like RNA-binding protein affects alternative splicing by in vivo interaction with transcripts in Arabidopsis thaliana Quantitative modeling assesses the contribution of bond strengthening, rebinding and force sharing to the avidity of biomolecule interactions.Antibody-unfolding and metastable-state binding in force spectroscopy and recognition imaging Long lifetime of hydrogen-bonded DNA basepairs by force spectroscopy.Directly measuring single-molecule heterogeneity using force spectroscopy.Analysis of DNA interactions using single-molecule force spectroscopy.Catch bond interaction between cell-surface sulfatase Sulf1 and glycosaminoglycans.Single-molecule force spectroscopy: a method for quantitative analysis of ligand-receptor interactions.Genome-wide identification and phylogenetic analysis of plant RNA binding proteins comprising both RNA recognition motifs and contiguous glycine residues.

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Quantitative analysis of single-molecule RNA-protein interaction.

http://www.wikidata.org/entity/Q37265282

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on June 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Quantitative analysis of single-molecule RNA-protein interaction.

@en

Quantitative analysis of single-molecule RNA-protein interaction.

@nl

type

label

Quantitative analysis of single-molecule RNA-protein interaction.

@en

Quantitative analysis of single-molecule RNA-protein interaction.

@nl

prefLabel

Quantitative analysis of single-molecule RNA-protein interaction.

@en

Quantitative analysis of single-molecule RNA-protein interaction.

@nl

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J.BPJ.2009.03.022

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Biophysical Journal

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Quantitative analysis of single-molecule RNA-protein interaction

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Alexander Fuhrmann

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Jan C Schoening

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Robert Ros

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Effector-stimulated single molecule protein-DNA interactions of a quorum-sensing system in Sinorhizobium meliloti.

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Binding of IRE-BP to its cognate RNA sequence: SFM studies on a universal RNA backbone for the analysis of RNA-protein interaction.

Dynamic force spectroscopy: optimized data analysis.

Specific binding of the regulatory protein ExpG to promoter regions of the galactoglucan biosynthesis gene cluster of Sinorhizobium meliloti--a combined molecular biology and force spectroscopy investigation.

Refined procedure of evaluating experimental single-molecule force spectroscopy data.

Dynamic force spectroscopy of parallel individual Mucin1-antibody bonds.

Detection and localization of single molecular recognition events using atomic force microscopy.

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5030-5039

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scholarly article

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10.1016/J.BPJ.2009.03.022

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12

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Dario Anselmetti

Dorothee Staiger

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2009-06-01T00:00:00Z

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26293200

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19527663

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2712025

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