Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein - Wikidata - awgldk - TriplyDB

Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

http://www.wikidata.org/entity/Q27676501

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Phytochromes: an atomic perspective on photoactivation and signaling Optogenetic control of cell function using engineered photoreceptors Crystallographic and Electron Microscopic Analyses of a Bacterial Phytochrome Reveal Local and Global Rearrangements during Photoconversion Advances in Imaging Techniques and Genetically Encoded Probes for Photoacoustic Imaging.An infrared reporter to detect spatiotemporal dynamics of protein-protein interactions A far-red fluorescent protein evolved from a cyanobacterial phycobiliprotein.Tolerance of a Knotted Near-Infrared Fluorescent Protein to Random Circular Permutation Structural heterogeneity in a parent ground-state structure of AnPixJg2 revealed by theory and spectroscopy.Advanced in vivo applications of blue light photoreceptors as alternative fluorescent proteins.Origins of fluorescence in evolved bacteriophytochromes Near-infrared light responsive synthetic c-di-GMP module for optogenetic applications.Atomic force microscopy of red-light photoreceptors using peakforce quantitative nanomechanical property mapping.Fast Photochemistry of Prototypical Phytochromes-A Species vs. Subunit Specific Comparison A naturally monomeric infrared fluorescent protein for protein labeling in vivo.Ultrafast excited-state dynamics and fluorescence deactivation of near-infrared fluorescent proteins engineered from bacteriophytochromes.Near-infrared fluorescent proteins engineered from bacterial phytochromes.Fluoromodule-based reporter/probes designed for in vivo fluorescence imaging.The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography.Removal of Chromophore-Proximal Polar Atoms Decreases Water Content and Increases Fluorescence in a Near Infrared Phytofluor Molecular Basis of Spectral Diversity in Near-Infrared Phytochrome-Based Fluorescent Proteins.Natural photoreceptors as a source of fluorescent proteins, biosensors, and optogenetic tools.Allosteric effects of chromophore interaction with dimeric near-infrared fluorescent proteins engineered from bacterial phytochromes.The terminal phycobilisome emitter, LCM: A light-harvesting pigment with a phytochrome chromophore.Engineering of bacterial phytochromes for near-infrared imaging, sensing, and light-control in mammals.Rational design of a monomeric and photostable far-red fluorescent protein for fluorescence imaging in vivo Arm-in-Arm Response Regulator Dimers Promote Intermolecular Signal Transduction Near-infrared fluorescent proteins for multicolor in vivo imaging.Bright monomeric near-infrared fluorescent proteins as tags and biosensors for multiscale imaging.Light-induced structural changes in a monomeric bacteriophytochrome.Unraveling the Primary Isomerization Dynamics in Cyanobacterial Phytochrome Cph1 with Multi-pulse Manipulations.Bright blue-shifted fluorescent proteins with Cys in the GAF domain engineered from bacterial phytochromes: fluorescence mechanisms and excited-state dynamics.Natural Resources for Optogenetic Tools.The role of local and remote amino acid substitutions for optimizing fluorescence in bacteriophytochromes: A case study on iRFP The Growing and Glowing Toolbox of Fluorescent and Photoactive Proteins.Dynamic inhomogeneity in the photodynamics of cyanobacterial phytochrome Cph1.Minimal domain of bacterial phytochrome required for chromophore binding and fluorescence.Light-induced Changes in the Dimerization Interface of Bacteriophytochromes.Designing brighter near-infrared fluorescent proteins: insights from structural and biochemical studies.Bacterial Phytochromes, Cyanobacteriochromes and Allophycocyanins as a Source of Near-Infrared Fluorescent Probes.Interaction of Biliverdin Chromophore with Near-Infrared Fluorescent Protein BphP1-FP Engineered from Bacterial Phytochrome.

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P2860

Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

http://www.wikidata.org/entity/Q27676501

description

2012 nî lūn-bûn

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2012 թուականի Մարտին հրատարակուած գիտական յօդուած

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2012 թվականի մարտին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

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Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

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Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

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type

label

Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

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Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

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Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

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prefLabel

Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

@ast

Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

@en

Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

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JBC.M111.295121

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Journal of Biological Chemistry

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Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein

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David M Anstrom

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Katrina T Forest

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Michele E Auldridge

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P2860

Bright and stable near-infrared fluorescent protein for in vivo imaging

Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome

High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution

Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion

The structure of a complete phytochrome sensory module in the Pr ground state

Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: Photoconversion and signal transduction

Conformational differences between the Pfr and Pr states in Pseudomonas aeruginosa bacteriophytochrome

Use of TLS parameters to model anisotropic displacements in macromolecular refinement

Phasercrystallographic software

Refinement of macromolecular structures by the maximum-likelihood method

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7000-9

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scholarly article

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575225

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10.1074/JBC.M111.295121

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10

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287

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Kenneth A Satyshur

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2012-03-02T00:00:00Z

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22210774

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protein structure

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3293566

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