Light-induced electron transfer in Arabidopsis cryptochrome-1 correlates with in vivo function. - Wikidata - awgldk - TriplyDB

Light-induced electron transfer in Arabidopsis cryptochrome-1 correlates with in vivo function.

Light-induced electron transfer in Arabidopsis cryptochrome-1 correlates with in vivo function.

http://www.wikidata.org/entity/Q46387096

about

Human and Drosophila cryptochromes are light activated by flavin photoreduction in living cells Light-activated cryptochrome reacts with molecular oxygen to form a flavin-superoxide radical pair consistent with magnetoreception Chemical magnetoreception in birds: the radical pair mechanism Magnetic field effects on plant growth, development, and evolution Cryptochromes--a potential magnetoreceptor: what do we know and what do we want to know?Acuity of a cryptochrome and vision-based magnetoreception system in birds Separation of photo-induced radical pair in cryptochrome to a functionally critical distance The quantum needle of the avian magnetic compass Decrypting cryptochrome: revealing the molecular identity of the photoactivation reaction HFR1 is crucial for transcriptome regulation in the cryptochrome 1-mediated early response to blue light in Arabidopsis thaliana ATP binding turns plant cryptochrome into an efficient natural photoswitch Directed evolution and in silico analysis of reaction centre proteins reveal molecular signatures of photosynthesis adaptation to radiation pressure.Light-induced conformational changes in full-length Arabidopsis thaliana cryptochrome Searching for a photocycle of the cryptochrome photoreceptors.Formation and function of flavin anion radical in cryptochrome 1 blue-light photoreceptor of monarch butterfly.Animal type 1 cryptochromes. Analysis of the redox state of the flavin cofactor by site-directed mutagenesis.Hydrogen-bond switching through a radical pair mechanism in a flavin-binding photoreceptor.Plant flavoprotein photoreceptors Fluorescence-detected magnetic field effects on radical pair reactions from femtolitre volumes.Arabidopsis cryptochrome 2 (CRY2) functions by the photoactivation mechanism distinct from the tryptophan (trp) triad-dependent photoreduction Magnetic field effects in Arabidopsis thaliana cryptochrome-1.Reaction kinetics and mechanism of magnetic field effects in cryptochrome The action mechanisms of plant cryptochromes Magnetically sensitive light-induced reactions in cryptochrome are consistent with its proposed role as a magnetoreceptor.Trp triad-dependent rapid photoreduction is not required for the function of Arabidopsis CRY1.Resolving cryptic aspects of cryptochrome signaling.Conformational and Intermolecular Interaction Dynamics of Photolyase/Cryptochrome Proteins Monitored by the Time-Resolved Diffusion Technique.Photochemistry and photobiology of cryptochrome blue-light photopigments: the search for a photocycle.Unexpected electron transfer in cryptochrome identified by time-resolved EPR spectroscopy.Variable electron transfer pathways in an amphibian cryptochrome: tryptophan versus tyrosine-based radical pairs Optimized second-generation CRY2-CIB dimerizers and photoactivatable Cre recombinase.Magnetic-field effect on the photoactivation reaction of Escherichia coli DNA photolyase.Flavin-based Blue-Light photosensors: a photobiophysics update.Ultrafast dynamics and anionic active states of the flavin cofactor in cryptochrome and photolyase Structure and function of animal cryptochromes.Magnetoreception through cryptochrome may involve superoxide.Magnetic field effects in flavoproteins and related systems The tricks plants use to reach appropriate light.Tripping the light fantastic: blue-light photoreceptors as examples of environmentally modulated protein-protein interactions.Algal photoreceptors: in vivo functions and potential applications.

P2860

Q21563550-695CF132-A5AA-44BA-BE7B-493FFBEF08EC Q24606914-D31CA541-2FF9-4C16-9E57-375F39AE6D60 Q24648535-B0EA7358-BCEF-484B-8824-21342A94CB37 Q28656019-C74A4613-B021-4FFF-9A33-A8DC6CC93C39 Q28748346-C76595C9-7DD1-4247-B39F-C441F8DCDBAD Q28750648-4718514D-E288-45B2-A41A-4D41C482B1A5 Q28828999-E666C00C-C261-4F52-AE4D-84729A14DA4A Q28833613-84C49F6E-C939-42EE-A72F-52465BB3E60E Q30528462-2800AF84-7B05-4A6F-B190-96F1FB49D435 Q33381534-D2602D68-3366-4998-9DE6-65840A70EE3A Q33714081-EF5A489E-CA85-4BDC-B494-97F9B476E7AC Q33797801-66BE66EF-B5FB-4EB2-98C6-A782A2F8E786 Q34004987-B85A68E4-CDB9-4D1C-9607-4A0914FEC856 Q34273460-6466B68B-2768-4904-9140-9166C0C1E2AC Q34622886-8B64B612-023B-4741-A084-94366B35E300 Q34721506-34E9F02B-FB0E-4A55-81E8-4655E8B39FEE Q34984165-D2DBF302-91CE-477C-991B-A213DA11E04A Q35171424-1EC43129-4D0F-4E0D-A8AF-C3436636AE40 Q35599812-8B48897C-7189-451A-AC3D-FF58162BE200 Q35650882-4707BD64-520B-45E3-A589-CB50165B4E08 Q35696577-E52ADF3D-47B4-4FAA-9CD1-9DEBB43EC7D0 Q35700171-65674200-351A-482B-8F89-1179AA1710BF Q35751826-F167A075-0D61-4483-8CFF-314CE1960900 Q35882295-D67B79D4-6601-4646-9126-66D3294EEFBD Q35895497-467366BD-1570-4176-9384-1650D7979D15 Q35895717-B12B3245-DB2F-4F36-94CE-35B63315831C Q36214789-3D406AFF-9D5B-4E1E-B8C0-0C968E420F85 Q36257939-CC46C60D-0C62-4B9B-AEC6-D9440F0DABEE Q36452661-59CB34E4-3876-4767-BB96-21E2AB2850E3 Q36725038-BB9B05EB-9ACD-4328-9239-DE4690DA7EF5 Q36913498-6E20189F-5549-4BA2-9F9A-EC2BD25F353D Q36936209-247C78B3-E8A0-46BF-A800-E38776F949B9 Q37008958-79EA6511-A6E3-4948-AB72-9631D68514BC Q37140893-471A0CFF-69CB-4223-908A-DE5BB8A6B1EA Q37140984-A8843E2E-3AFD-497E-9555-77D0480E9C69 Q37265321-8DA5142C-D149-4351-B4A6-542FCAE2616E Q37561406-61BF0553-47AE-493E-8AB3-698A9FA97A5F Q37785868-DF3F17F6-4B35-4BEF-B03D-B10EBA2D16F4 Q37818106-B9728935-0216-4234-87CF-A876F2A8448E Q38148006-94BED66D-B9D2-427E-A906-8D729C772D28

P2860

Light-induced electron transfer in Arabidopsis cryptochrome-1 correlates with in vivo function.

http://www.wikidata.org/entity/Q46387096

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

2005年學術文章

@zh

2005年學術文章

@zh-hant

name

Light-induced electron transfe ...... relates with in vivo function.

@en

Light-induced electron transfe ...... relates with in vivo function.

@nl

type

label

Light-induced electron transfe ...... relates with in vivo function.

@en

Light-induced electron transfe ...... relates with in vivo function.

@nl

prefLabel

Light-induced electron transfe ...... relates with in vivo function.

@en

Light-induced electron transfe ...... relates with in vivo function.

@nl

P1433

Q46387096-EC7E8052-E3FC-4CF8-A19E-8F51D285AAEE

P1476

Q46387096-B052757A-FDDF-490E-9109-07064DBC90C5

P2093

Q46387096-0FB3E96D-A2E2-4E5E-B76C-3F31C866293D

Q46387096-226710E9-4E7E-4900-8E67-D989786A4CA3

Q46387096-3CED27B1-DD91-4161-B502-7DAF88365A6A

Q46387096-4BEFEB01-B2A5-44E8-9230-5F23D3A0CE91

Q46387096-CF001F5F-2A20-43E4-9C7A-090177A6015C

Q46387096-DD660CE3-4E3F-4FE4-BF9E-657BDCF3B10E

P2860

Q46387096-08A98621-1AFC-4516-B1DB-9FC0BC5515AA

Q46387096-09EFD0D9-AB61-4090-BB07-F395A044888D

Q46387096-19DC8E0A-6955-4EE9-846C-0065929C4AA9

Q46387096-210065B0-6826-47DA-A165-8B84F438E942

Q46387096-254CC4CD-7832-4408-8573-8CBACE723E85

Q46387096-2F8286B5-CD47-4D5E-853A-732BEA7FABD5

Q46387096-31B04EAB-16A3-43D0-ADCC-14FCB5D49365

Q46387096-3B670A54-3351-4150-B3D4-E7654DAE9BD6

Q46387096-4789B927-C0AA-477E-92B0-D8F5593202B1

Q46387096-486BF35F-9C06-4FFD-B07D-F6A4475E2052

P304

Q46387096-13067EDD-8674-4B12-9B87-22492DBFA20F

P31

Q46387096-8959A9C6-D293-4ACE-9DD4-EBDFE1C67521

P356

Q46387096-B8252C1E-8996-4FB1-8176-14182EE2B756

P407

Q46387096-C88B5EB6-BEE6-4B92-ABCD-52BC67BB8CA6

P433

Q46387096-FEAD7389-9BAD-44ED-BC74-50DBFD5368FC

P478

Q46387096-1565A37D-00A8-4984-8595-60E10F891D4A

P50

Q46387096-0F976C65-3EEB-4EE3-BC2F-B352894BE03B

P577

Q46387096-0CE92B2B-9098-4693-B9C6-CA58BF269639

P698

Q46387096-265E32CC-B422-430A-98D7-BC5863964891

P356

P1433

Journal of Biological Chemistry

P1476

Light-induced electron transfe ...... rrelates with in vivo function

@en

P2093

Anke Zeugner

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

Baldissera Giovani

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

Jean-Pierre Bouly

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

Klaus Brettel

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

Margaret Ahmad

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

Nadia Bakrim

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

P2860

Crystal structure of DNA photolyase from Escherichia coli

Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors

A putative flavin electron transport pathway is differentially utilized in Xenopus CRY1 and CRY2.

Cryptochromes: tail-ored for distinct functions.

Active site of DNA photolyase: tryptophan-306 is the intrinsic hydrogen atom donor essential for flavin radical photoreduction and DNA repair in vitro.

Natural engineering principles of electron tunnelling in biological oxidation-reduction.

Femtosecond dynamics of flavoproteins: charge separation and recombination in riboflavine (vitamin B2)-binding protein and in glucose oxidase enzyme.

Photoactivation of the flavin cofactor in Xenopus laevis (6 - 4) photolyase: observation of a transient tyrosyl radical by time-resolved electron paramagnetic resonance

Pathways of electron transfer in Escherichia coli DNA photolyase: Trp306 to FADH

Blue light sensing in higher plants.

P304

19437-19440

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

P31

scholarly article

P356

10.1074/JBC.C500077200

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

P407

P433

20

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

P478

280

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

P50

P577

2005-03-17T00:00:00Z

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

P698

15774475

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