The importance of size and disorder in the cryoprotective effects of dehydrins. - Wikidata - awgldk - TriplyDB

The importance of size and disorder in the cryoprotective effects of dehydrins.

The importance of size and disorder in the cryoprotective effects of dehydrins.

http://www.wikidata.org/entity/Q39085840

about

Comparison of amino acids physico-chemical properties and usage of late embryogenesis abundant proteins, hydrophilins and WHy domain Structural and Functional Insights into the Cryoprotection of Membranes by the Intrinsically Disordered Dehydrins YSK2 Type Dehydrin (SbDhn1) from Sorghum bicolor Showed Improved Protection under High Temperature and Osmotic Stress Condition.The K-segments of wheat dehydrin WZY2 are essential for its protective functions under temperature stress.Natural variation in the C-repeat binding factor cold response pathway correlates with local adaptation of Arabidopsis ecotypes.Genetic diversity at the Dhn3 locus in Turkish Hordeum spontaneum populations with comparative structural analyses.Disorder and function: a review of the dehydrin protein family.CRISPR-induced null alleles show that Frost protects Drosophila melanogaster reproduction after cold exposure.A glass menagerie of low complexity sequences.Different dehydrins perform separate functions in Physcomitrella patens.Structure of an Intrinsically Disordered Stress Protein Alone and Bound to a Membrane Surface.Expression of CdDHN4, a Novel YSK2-Type Dehydrin Gene from Bermudagrass, Responses to Drought Stress through the ABA-Dependent Signal Pathway.Genome Analysis of Conserved Dehydrin Motifs in Vascular Plants.Structural disorder in plant proteins: where plasticity meets sessility.Multifunctional Roles of Plant Dehydrins in Response to Environmental Stresses.Inhibition of ice recrystallization and cryoprotective activity of wheat proteins in liver and pancreatic cells.Dissecting the cryoprotection mechanisms for dehydrins.A dehydrin-dehydrin interaction: the case of SK3 from Opuntia streptacantha.The genetic architecture of freezing tolerance varies across the range of Arabidopsis thaliana.In vivo evidence for homo- and heterodimeric interactions of Arabidopsis thaliana dehydrins AtCOR47, AtERD10, and AtRAB18.Discovery of Cryoprotective Activity in Human Genome-Derived Intrinsically Disordered Proteins.

P2860

Q28543617-BD41A287-65B3-4B99-B972-B225946185BB Q30379169-EF86B070-0240-495B-A446-7DB3E510B129 Q30853880-C65677D9-3BEB-4973-BC50-F0A12E762F30 Q35743035-DB4FF0C0-90CD-4082-8BCD-DA1955C4FA02 Q35775090-C37DED09-42B4-4051-84AA-DEC9A85A54E0 Q36574321-B19C218D-6C0A-4E58-A305-9005690952E0 Q38268640-E504E6F9-32E0-4FBC-805B-51BE616B18E0 Q38657989-35D0D794-CFF5-448B-A004-5EC57173840F Q38852916-409F96A2-BA24-4D14-A99E-96230409E959 Q38861990-12DB7CCD-CDF7-43E3-B874-04416F36112E Q38883107-6AC4F37B-D973-49E7-972A-EEBFD5800A64 Q39195666-094E0400-32A1-454C-9BB9-B41133D6DFC8 Q39208160-2E912B34-6B6A-451B-BAE1-99AF21CD1F34 Q39393201-6F55D1CA-66FC-4475-86CB-D3FACC7B3A53 Q39397712-CEB88083-97B9-4394-88C1-F994A1850B62 Q40413094-E7C1F61E-38D8-4EFA-9551-1BD390FE2940 Q42693586-BE6436B3-0BD8-4F83-B82E-7BA77AD0E0A3 Q42939838-45F5BFB2-54C5-4AA8-917D-D58A3E4625CF Q44710541-66CEDA10-8F55-4032-94F3-59276EDEFA15 Q47321952-94726C36-5DC0-42BE-BC84-5BB34CF9EE0D Q47701746-C4DBFC7C-5344-4A2A-B871-E562C7547AEE

P2860

The importance of size and disorder in the cryoprotective effects of dehydrins.

http://www.wikidata.org/entity/Q39085840

description

2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

@zh-cn

name

The importance of size and disorder in the cryoprotective effects of dehydrins.

@en

The importance of size and disorder in the cryoprotective effects of dehydrins.

@nl

type

label

The importance of size and disorder in the cryoprotective effects of dehydrins.

@en

The importance of size and disorder in the cryoprotective effects of dehydrins.

@nl

prefLabel

The importance of size and disorder in the cryoprotective effects of dehydrins.

@en

The importance of size and disorder in the cryoprotective effects of dehydrins.

@nl

P1433

Q39085840-636005A7-E205-4727-AAED-7E48BCBCAF0F

P1476

Q39085840-4F6F157F-8BEE-4524-B81A-807206BAD4FB

P2093

Q39085840-1E6DF7CA-377B-4936-845E-B40F5CE5DEB0

Q39085840-5599E8D7-ACDD-4CA8-8853-403CFF4B704C

Q39085840-6AA6E1BB-85F2-4152-8044-A3AED22DAEC0

Q39085840-79125AFD-B390-46B7-B04E-76310FCDA7AD

Q39085840-C088D54E-326C-44A1-B9ED-43CDE9C70B68

Q39085840-E5B8F67C-8D83-460D-BF13-E9E86EF1522F

Q39085840-FCD11234-D038-46FF-8B8E-F85E0F26C669

Q39085840-FE024DB0-938B-4270-9AA8-3CE9E287CEB6

P2860

Q39085840-06C90D28-AEE0-4DC7-A053-269EF0A82F57

Q39085840-0B85A9EE-5907-4C4C-A96B-36A2772E147B

Q39085840-0C3A9915-1AD4-4235-93B8-2194F045E7DC

Q39085840-0DFD6BD3-32A1-4904-A502-C3DBC402F25F

Q39085840-12D76E8C-CE1E-4FE3-8ECE-175FA19D3EE3

Q39085840-14B6D21A-D5CF-4F6E-92AE-BD30CBDE3B58

Q39085840-1D190CF7-4D12-4D42-99A3-2820CE06B227

Q39085840-1D93783F-AB9B-4CC1-A231-7DCCE05B25B2

Q39085840-206B2FD4-FE6B-4076-9862-04FABC0B08AA

Q39085840-220380F7-C1F3-4532-AF1F-8E7F73212B99

P304

Q39085840-AB38111D-9FD2-4CC5-8332-D04185ED238E

P31

Q39085840-3571B672-226C-41C9-B753-AF6D902D0B5C

P356

Q39085840-35CF7A7B-C6D0-4933-A409-F13393608EFC

P407

Q39085840-1D352E3B-E4B0-4A91-BF9F-A5D46F5FC0AF

P433

Q39085840-09B614FD-8381-4128-B886-22DE7E268FB2

P478

Q39085840-B13BC442-0FF3-4CF9-9935-4D145CBB7B50

P577

Q39085840-DEEC051F-BB23-4B75-A1DC-E76E404FE9CE

P5875

Q39085840-3AD3009D-CC26-4517-873A-EA25A9168A0D

P698

Q39085840-6AA1384F-3AF5-4F70-821B-74924CFE39B7

P932

Q39085840-1D68D057-12DD-4E51-9BFF-B04B4ABEF5C8

P356

P1433

Plant Physiology

P1476

The importance of size and disorder in the cryoprotective effects of dehydrins.

@en

P2093

David M Martynowicz

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

Erik Tralman-Baker

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

Janet Malcolmson

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

Kaley A Hogarth

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

Shruti N Patel

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

Steffen P Graether

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

Stephanie L Hughes

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

Verena Schart

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

P2860

LEA proteins prevent protein aggregation due to water stress

Spruce budworm antifreeze protein: changes in structure and dynamics at low temperature

Anchored clathrate waters bind antifreeze proteins to ice

Intrinsically disordered proteins as molecular shields

Intrinsically unstructured proteins

Natively unfolded proteins: a point where biology waits for physics

Cold survival in freeze-intolerant insects: the structure and function of beta-helical antifreeze proteins.

Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects

Ion binding properties of the dehydrin ERD14 are dependent upon phosphorylation.

Purification and characterisation of an antifreeze protein from Forsythia suspensa (L.).

P304

1376-1386

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

P31

scholarly article

P356

10.1104/PP.113.226803

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

P407

P433

3

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

P478

163

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

P577

2013-09-18T00:00:00Z

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

P5875

256763404

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

P698

24047864

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

P932

3813657

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