The BTB/POZ domain of the Arabidopsis disease resistance protein NPR1 interacts with the repression domain of TGA2 to negate its function. - Wikidata - awgldk - TriplyDB

The BTB/POZ domain of the Arabidopsis disease resistance protein NPR1 interacts with the repression domain of TGA2 to negate its function.

The BTB/POZ domain of the Arabidopsis disease resistance protein NPR1 interacts with the repression domain of TGA2 to negate its function.

http://www.wikidata.org/entity/Q42463123

about

Deconstruction of the SS18-SSX fusion oncoprotein complex: insights into disease etiology and therapeutics Transcription dynamics in plant immunity Cullin-RING ubiquitin ligases in salicylic acid-mediated plant immune signaling Circadian redox signaling in plant immunity and abiotic stress Horizontal gene transfer is more frequent with increased heterotrophy and contributes to parasite adaptation.Integrating data on the Arabidopsis NPR1/NPR3/NPR4 salicylic acid receptors; a differentiating argument Repression of Lateral Organ Boundary Genes by PENNYWISE and POUND-FOOLISH Is Essential for Meristem Maintenance and Flowering in Arabidopsis.Control of inflorescence architecture in tomato by BTB/POZ transcriptional regulators.Arabidopsis genes, AtNPR1, AtTGA2 and AtPR-5, confer partial resistance to soybean cyst nematode (Heterodera glycines) when overexpressed in transgenic soybean roots.Functional analysis of the Theobroma cacao NPR1 gene in Arabidopsis.Transcriptomic analysis of grain amaranth (Amaranthus hypochondriacus) using 454 pyrosequencing: comparison with A. tuberculatus, expression profiling in stems and in response to biotic and abiotic stress The ubiquitin-proteasome system: central modifier of plant signalling.Dual-function transcription factors and their entourage: unique and unifying themes governing two pathogenesis-related genes.Composition, roles, and regulation of cullin-based ubiquitin e3 ligases.Genome-wide nested association mapping of quantitative resistance to northern leaf blight in maize Interaction specificity and coexpression of rice NPR1 homologs 1 and 3 (NH1 and NH3), TGA transcription factors and Negative Regulator of Resistance (NRR) proteins.β-cyclocitral upregulates salicylic acid signalling to enhance excess light acclimation in Arabidopsis.A rice transient assay system identifies a novel domain in NRR required for interaction with NH1/OsNPR1 and inhibition of NH1-mediated transcriptional activation A Genetic Screen Identifies a Requirement for Cysteine-Rich-Receptor-Like Kinases in Rice NH1 (OsNPR1)-Mediated Immunity Long-distance communication and signal amplification in systemic acquired resistance.Redox-dependent functional switching of plant proteins accompanying with their structural changes Nitric Oxide Mediated Transcriptome Profiling Reveals Activation of Multiple Regulatory Pathways in Arabidopsis thaliana.Transcriptomic analysis of flower development in wintersweet (Chimonanthus praecox)Salicylic acid: an old hormone up to new tricks.Development and validation of KASP markers for the greenbug resistance gene Gb7 and the Hessian fly resistance gene H32 in wheat.Salicylic acid signal transduction: the initiation of biosynthesis, perception and transcriptional reprogramming.Tobacco Transcription Factor NtWRKY12 Interacts with TGA2.2 in vitro and in vivo The NPR1 homolog GhNPR1 plays an important role in the defense response of Gladiolus hybridus.Characterization and RNA-seq analysis of underperformer, an activation-tagged potato mutant.Sumoylation, Phosphorylation, and Acetylation Fine-Tune the Turnover of Plant Immunity Components Mediated by Ubiquitination.Exchanging the as-1-like element of the PR-1 promoter by the as-1 element of the CaMV 35S promoter abolishes salicylic acid responsiveness and regulation by NPR1 and SNI1.The Arabidopsis PR-1 promoter contains multiple integration sites for the coactivator NPR1 and the repressor SNI1.Arabidopsis basic leucine-zipper transcription factors TGA9 and TGA10 interact with floral glutaredoxins ROXY1 and ROXY2 and are redundantly required for anther development.Genome-wide association study of quantitative resistance to southern leaf blight in the maize nested association mapping population.CML9, an Arabidopsis calmodulin-like protein, contributes to plant innate immunity through a flagellin-dependent signalling pathway.Ubiquitination-Related MdBT Scaffold Proteins Target a bHLH Transcription Factor for Iron Homeostasis.The tobacco BLADE-ON-PETIOLE2 gene mediates differentiation of the corolla abscission zone by controlling longitudinal cell expansion.Unique resistance traits against downy mildew from the center of origin of grapevine (Vitis vinifera)TCP Transcription Factors Interact With NPR1 and Contribute Redundantly to Systemic Acquired Resistance

P2860

Q24308344-85BE40F4-EDD9-4DD1-85D7-13C933BC8D0F Q24635642-3ACA8E85-3A52-4205-BC21-65B2F6B21D63 Q28085121-2B7D875B-2FC5-4C76-ADC3-608DFD36D6A4 Q28659049-AC79CA80-8AAF-4C63-97AB-CE45EB2745B8 Q30275577-B6A70028-3929-4858-80AA-2FDD7298AEBC Q30939974-DCC9030C-7845-4B43-A22A-D96C457B2FE6 Q33361613-6790E444-AA19-42A0-B045-06B02FA1C012 Q33364186-87AE3985-A5E8-4FEB-8ED0-9FC5E77EB889 Q33612582-8CCA4288-C373-4048-844F-B7F21C8342C8 Q33747081-173458C1-63B1-4AED-A271-35BD66536202 Q33959908-F7C60436-DD3E-4FB6-8874-669E1B97DA07 Q34294337-A4E0A65D-0A2D-4C81-9767-70EC10F2F0A4 Q34404058-61310DBF-9B08-4DD5-A4DC-0E887EEB82A4 Q34671745-B764C040-F4B7-4EB4-93BF-33CFBAB1E87C Q34881018-3C7FA9A8-EF5D-40AC-BB63-2394443CC8B2 Q35185644-CA46C0D7-932D-4A8F-8A3D-0EFF4B915FE8 Q35638834-C207ADB3-5D1D-4DBD-8BAA-9DFE9923D9AC Q35814907-EED160AF-F209-46A3-8248-2A4087044782 Q36017186-D0CF4EC1-74EE-4180-88FC-2E5BE2F24F3F Q36629040-E9209E43-D024-40B6-B3D1-44F5D7A880E3 Q37046810-12214FC5-7BCD-4D52-8359-E1B2E5561FFD Q37050405-6C72924B-04D3-4C6D-8E8E-8100DA90FCA2 Q37529526-CD57F8A4-F27F-492A-9263-9CB1786A9499 Q38101989-2ED87A09-181B-455F-92F5-4F77B63F4546 Q38669812-196DFAEB-106C-49F1-95C3-EE60BDDE135A Q41826691-BEF174C0-8680-43B9-A080-F6E599D168C1 Q41969708-0C2D3795-D7D3-47B4-8B66-94315021FC33 Q42160403-AC66F343-8526-4E88-8325-F6129E4D3215 Q42251093-D1CCC035-F2F0-4843-867D-536FE1197FE6 Q42700483-BD8C9040-ADAE-462E-8DDF-A74C09409BE3 Q42757596-B71394F6-4D59-4E36-908C-FE939AEAFD4E Q42863313-56712CFB-87C2-46C7-97FF-28818D09C0EB Q42921874-51540EE2-0B71-4FA0-834D-EBFC43CFC09F Q44859528-64374905-999B-48B8-9F88-3D5415C6E1A5 Q44993325-6E718E48-FA5D-4496-93E4-BCA3357B741B Q46486351-4F962CEC-DF4E-40D3-A554-2C32FC6CEB02 Q48050622-DE1F88B4-0225-44F7-B3AA-502D76A5D9E4 Q58730662-1460478D-AAE4-480C-A61F-CCD51D5AD634 Q58781294-14BE8EAE-EAAC-40CA-A518-91FD48EFCC9C

P2860

The BTB/POZ domain of the Arabidopsis disease resistance protein NPR1 interacts with the repression domain of TGA2 to negate its function.

http://www.wikidata.org/entity/Q42463123

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

2009年论文

@zh

2009年论文

@zh-cn

name

The BTB/POZ domain of the Arab ...... f TGA2 to negate its function.

@en

The BTB/POZ domain of the Arab ...... f TGA2 to negate its function.

@nl

type

label

The BTB/POZ domain of the Arab ...... f TGA2 to negate its function.

@en

The BTB/POZ domain of the Arab ...... f TGA2 to negate its function.

@nl

prefLabel

The BTB/POZ domain of the Arab ...... f TGA2 to negate its function.

@en

The BTB/POZ domain of the Arab ...... f TGA2 to negate its function.

@nl

P1433

Q42463123-E9C40525-FBFB-459E-AB5F-A8B13ED8A6A4

P1476

Q42463123-180A2571-F96D-4E61-9229-54B98772CD15

P2093

Q42463123-165C48CB-9918-4E29-BB07-E2248730132C

Q42463123-2B5E0EA1-8DDE-4669-B9CC-359CDFCBE60A

Q42463123-3721F070-B78D-473E-860F-6C89B3092AC3

Q42463123-92175FB4-8FFA-4D79-8661-14B88D2A5A02

Q42463123-A50FD30E-AE43-4AE8-B17F-BF88D1C8DE0F

Q42463123-DD72339B-7649-4224-83BA-80C007B50248

Q42463123-E651B486-F4C9-40C7-AA56-C38B63CAF779

Q42463123-E96B524E-2D43-44B2-9018-AE4C20A3146D

P2860

Q42463123-0093927F-5A80-444A-8CD2-2FC76E23AFF8

Q42463123-0CB8B396-07CA-4D5A-8B7D-B1F84DB42061

Q42463123-10164902-1472-4ACA-8184-AE8722D9AB19

Q42463123-17585600-5E02-4977-BE9C-997B20B7A596

Q42463123-2CA08217-5F83-441F-93FA-DE5FA6951221

Q42463123-310336D7-876C-4A6C-AD82-34266FD7C149

Q42463123-3B3B14AF-4E54-4739-B11C-4BD1C0AC4248

Q42463123-44667B34-B84A-493C-821F-D2DF99DA4A32

Q42463123-46139197-0348-408C-BCA1-6C0A2B6E6BB6

Q42463123-635B1764-8A72-411E-B403-215238AEB2D1

P304

Q42463123-11ED3227-2CA8-4D36-85AE-C858A80E06D6

P31

Q42463123-A304DD24-2694-44D1-BDAD-D9E8056C73EB

P356

Q42463123-2BED44D2-600D-43D7-9B60-438DE49710F8

P433

Q42463123-3E5B66B1-70B0-448E-BD41-21832CF71F44

P478

Q42463123-4D29A58C-3EF8-4750-91D9-CC1F62F4D36A

P577

Q42463123-15FB4799-D454-41B7-BEC4-31520BC0C9A9

P5875

Q42463123-CB160CE8-60D7-4F18-B10A-F20C8D184CED

P698

Q42463123-5D1B9B10-942A-432C-8E0F-9B62E74599E0

P932

Q42463123-5A58ED4A-6D9D-4469-B90C-C147F9C25665

P356

P1433

P1476

The BTB/POZ domain of the Arab ...... f TGA2 to negate its function.

@en

P2093

Amanda Rochon

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

Charles Després

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

Errol Le Su

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

Heather L Shearer

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

Jee Yan Chu

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

Jhadeswar Murmu

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

Patrick Boyle

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

Pierre R Fobert

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

P2860

Crystal structure of the BTB domain from PLZF

Recruitment of SMRT/N-CoR-mSin3A-HDAC-repressing complexes is not a general mechanism for BTB/POZ transcriptional repressors: the case of HIC-1 and gammaFBP-B

Salicylic acid and NPR1 induce the recruitment of trans-activating TGA factors to a defense gene promoter in Arabidopsis

Characterization of an Arabidopsis Mutant That Is Nonresponsive to Inducers of Systemic Acquired Resistance

Sequence and structural analysis of BTB domain proteins

Structure-function studies of the BTB/POZ transcriptional repression domain from the promyelocytic leukemia zinc finger oncoprotein

Crystal structures of Drosophila mutant translin and characterization of translin variants reveal the structural plasticity of translin proteins

The POZ domain: a conserved protein-protein interaction motif

Plant pathogens and integrated defence responses to infection

The translin ring specifically recognizes DNA ends at recombination hot spots in the human genome

P304

3700-3713

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

P31

scholarly article

P356

10.1105/TPC.109.069971

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

P433

11

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

P478

21

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

P577

2009-11-13T00:00:00Z

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

P5875

38091031

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

P698

19915088

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

P932

2798319

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