Kinetics of conformational changes of the FKF1-LOV domain upon photoexcitation. - Wikidata - awgldk - TriplyDB

Kinetics of conformational changes of the FKF1-LOV domain upon photoexcitation.

Kinetics of conformational changes of the FKF1-LOV domain upon photoexcitation.

http://www.wikidata.org/entity/Q33757187

about

LOV domain-containing F-box proteins: light-dependent protein degradation modules in Arabidopsis Identification and molecular characterization of FKF1 and GI homologous genes in soybean Structure and Function of the ZTL/FKF1/LKP2 Group Proteins in Arabidopsis Functional and topological diversity of LOV domain photoreceptors.Evolution of three LOV blue light receptor families in green plants and photosynthetic stramenopiles: phototropin, ZTL/FKF1/LKP2 and aureochrome.Optogenetic control of signaling in mammalian cells.A search for radical intermediates in the photocycle of LOV domains.

P2860

Q26865417-1D7722E8-1989-4BAE-AA36-C28064A1232C Q35043678-7CE5C0E5-CC22-406D-8DC4-C034CA043627 Q35142361-E0D77B8D-11E5-483F-AE57-3A2A97D3FBAF Q36710481-1ED80852-7EC1-4F07-90B5-C13D72563C0E Q38065690-DEB674CD-922D-459F-ACB8-F80017215433 Q38248690-3C853D28-490E-41EF-A7B4-6066ECEF87FD Q50220671-A7673A80-AB35-43B7-8B4B-963359784C04

P2860

Kinetics of conformational changes of the FKF1-LOV domain upon photoexcitation.

http://www.wikidata.org/entity/Q33757187

description

2010 nî lūn-bûn

@nan

2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Kinetics of conformational changes of the FKF1-LOV domain upon photoexcitation.

@ast

Kinetics of conformational changes of the FKF1-LOV domain upon photoexcitation.

@en

type

label

Kinetics of conformational changes of the FKF1-LOV domain upon photoexcitation.

@ast

Kinetics of conformational changes of the FKF1-LOV domain upon photoexcitation.

@en

prefLabel

Kinetics of conformational changes of the FKF1-LOV domain upon photoexcitation.

@ast

Kinetics of conformational changes of the FKF1-LOV domain upon photoexcitation.

@en

P1433

Q33757187-8F8E2684-22E4-4C03-A072-9D0BFFA3DE36

P1476

Q33757187-996CD59E-818C-4FCC-A420-66E5C40B35AA

P2093

Q33757187-16166CBB-B760-4761-AD28-747B9BE48168

Q33757187-6C8B4D7C-8770-4DE5-BCB8-39ECDE5A47AA

Q33757187-97874DC3-091C-4E9F-985D-BDDCF9C547D0

Q33757187-DD57ABEE-2BF0-4087-84C3-80C869BFA20C

P2860

Q33757187-07D77EBB-9387-4D5C-B569-673024DC3CF4

Q33757187-1049F6FD-034A-49EC-B61F-E6EC5DF4D0A3

Q33757187-10BD6E28-9110-430F-B28A-8E3263689861

Q33757187-1399FB4C-1344-4C8B-A71B-DA272DE34390

Q33757187-167905A1-15DE-4B59-A76D-022B912BBA7C

Q33757187-1877D317-EFA9-4296-A7C8-B5B0208A20A2

Q33757187-18F0E96D-F193-493A-AE77-DBE3D6D9E938

Q33757187-2BB385C4-EA6E-46A1-805D-9E633E6F1CEF

Q33757187-33006FD0-0FC7-493A-8B27-F615AE025185

Q33757187-3A7DF7ED-4018-40C2-B97E-97E004C5C522

P304

Q33757187-5B57DA30-2B3E-442E-AB47-0EDEC26E90BD

P31

Q33757187-E32803C8-2131-4A76-B0DA-B78A08E1E35C

P356

Q33757187-D7B8BBCA-9750-437E-9E70-14C605C7CD18

P407

Q33757187-061793B6-648A-47C0-8377-AB7686CD340B

P433

Q33757187-75B478C6-4325-4961-8842-081DA071472D

P478

Q33757187-4D71A5F1-23E9-474A-AB77-10E3AF034CAB

P577

Q33757187-6C9B4946-2C2E-485E-8AC1-D1A75DB3FBD4

P5875

Q33757187-F11B6F1C-E79A-4BFC-8E97-D7A78D1E36F0

P698

Q33757187-4EF39756-091B-4C9A-9ED2-781ED73BAEEB

P932

Q33757187-2FA8B6B2-E69F-4504-8DA4-C8DCBC9ADEAB

P356

J.BPJ.2010.10.005

P1433

Biophysical Journal

P1476

Kinetics of conformational changes of the FKF1-LOV domain upon photoexcitation.

@en

P2093

Kazunori Zikihara

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

Masahide Terazima

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

Satoru Tokutomi

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

Yusuke Nakasone

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

P2860

Conformational Switching in the Fungal Light Sensor Vivid

Structural Basis for Light-dependent Signaling in the Dimeric LOV Domain of the Photosensor YtvA

Light Activation of the LOV Protein Vivid Generates a Rapidly Exchanging Dimer † ‡

Structural basis of the LOV1 dimerization of Arabidopsis phototropins 1 and 2

Illuminating Solution Responses of a LOV Domain Protein with Photocoupled Small-Angle X-Ray Scattering

Mechanism-based tuning of a LOV domain photoreceptor

Recording of blue light-induced energy and volume changes within the wild-type and mutated phot-LOV1 domain from Chlamydomonas reinhardtii.

Conformational dynamics of phototropin 2 LOV2 domain with the linker upon photoexcitation.

Diffusion coefficients as a monitor of reaction kinetics of biological molecules.

Kinetic measurement of transient dimerization and dissociation reactions of Arabidopsis phototropin 1 LOV2 domain.

P304

3831-3839

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

P31

scholarly article

P356

10.1016/J.BPJ.2010.10.005

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

P407

P433

11

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

P478

99

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

P577

2010-12-01T00:00:00Z

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

P5875

49640157

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

P698

21112308

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

P932

2998605

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