Photoactivation of the BLUF Protein PixD Probed by the Site-Specific Incorporation of Fluorotyrosine Residues.

about

Light-induced chromophore and protein responses and mechanical signal transduction of BLUF proteins.

P2860

Q47255199-8E1B7CDF-D324-4A0E-B27B-2A9226FA1629

P2860

Photoactivation of the BLUF Protein PixD Probed by the Site-Specific Incorporation of Fluorotyrosine Residues.

Item

http://www.wikidata.org/entity/Q47849729

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

@zh-hant

name

Photoactivation of the BLUF Pr ...... on of Fluorotyrosine Residues.

@en

Photoactivation of the BLUF Pr ...... on of Fluorotyrosine Residues.

@nl

type

Item

label

Photoactivation of the BLUF Pr ...... on of Fluorotyrosine Residues.

@en

Photoactivation of the BLUF Pr ...... on of Fluorotyrosine Residues.

@nl

prefLabel

Photoactivation of the BLUF Pr ...... on of Fluorotyrosine Residues.

@en

Photoactivation of the BLUF Pr ...... on of Fluorotyrosine Residues.

@nl

P1476

Photoactivation of the BLUF Pr ...... ion of Fluorotyrosine Residues

@en

P2093

Anil Verma

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

Grace E Yoon

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

Gregory M Greetham

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

P2860

Light modulation of cellular cAMP by a small bacterial photoactivated adenylyl cyclase, bPAC, of the soil bacterium Beggiatoa

Mutational and Structural Studies of the PixD BLUF Output Signal That Affects Light-Regulated Interactions with PixE

Biochemical and functional characterization of BLUF-type flavin-binding proteins of two species of cyanobacteria.

Ultrafast structural dynamics in BLUF domains: transient infrared spectroscopy of AppA and its mutants.

Ultrafast Structural Dynamics of BlsA, a Photoreceptor from the Pathogenic Bacterium Acinetobacter baumannii.

Structure of a bacterial BLUF photoreceptor: insights into blue light-mediated signal transduction.

BLUF: a novel FAD-binding domain involved in sensory transduction in microorganisms.

Time-resolved multiple probe spectroscopy.

Hydrogen-bond switching through a radical pair mechanism in a flavin-binding photoreceptor.

Photoreceptor proteins, "star actors of modern times": a review of the functional dynamics in the structure of representative members of six different photoreceptor families.

P304

14638-14648

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

P31

scholarly article

P356

10.1021/JACS.7B07849

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

P407

English

P433

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

P478

139

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

P50

P577

2017-10-05T00:00:00Z

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

P698

28876066

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

P921

photoactivation

P932

5647244

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

Photoactivation of the BLUF Protein PixD Probed by the Site-Specific Incorporation of Fluorotyrosine Residues.

about

P2860

P2860

Photoactivation of the BLUF Protein PixD Probed by the Site-Specific Incorporation of Fluorotyrosine Residues.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932