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Structural Basis for Assembly and Function of a Heterodimeric Plant Immune Receptor

Science(2014)10.1126/science.1247357Source: DataRank Database

Structural Basis for Assembly and Function of a Heterodimeric Plant Immune Receptor is a research paper published in Science (2014). On theSindex it has a DataRank of 0.888. It has been cited 371 times.

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0.888DataRank · unranked

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371 citations

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datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (4 grants)OA: closedTopics (61)Linked Datasets (8)DataCite Reuse (8)IDs (PubMed)SDGs (1)

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DataRank Breakdown

Base Score 100%Citation Network 0%

Base Score Contribution

0.888

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Authors (21)

Kee Hoon Sohn ORCID,Li Wan ORCID,Maud Bernoux ORCID,Panagiotis F. Sarris ORCID,Cecile Segonzac

Live enrichment

PubMed:24744375

Australian Research Council (ARC)

Grant: DP120100685

Understanding the molecular function of plant disease resistance proteins, pathogen effectors and their interaction to protect Australian agriculture

European Commission

Grant: 299621

Investigating how pathogen effector recognition by plant resistance proteins activates defence

National Health and Medical Research Council (NHMRC)

Grant: 1003325

Structural biology of infection and immunity

Australian Research Council (ARC)

Grant: DE130101292

Plant immune receptors: what are the first steps that trigger defence signalling?

closed

publisherhttps://www.science.org/doi/pdf/10.1126/science.1247357

https://doi.org/10.1126/science.1247357

https://pubmed.ncbi.nlm.nih.gov/24744375

https://espace.library.uq.edu.au/view/UQ:329106

https://api.library.uq.edu.au/view/UQ:329106

Fields of Study

0301 basic medicine03 medical and health sciences0303 health sciences

MeSH Terms

Plants, Genetically ModifiedArabidopsisPlant LeavesBacterial ProteinsReceptors, ImmunologicPlant ProteinsArabidopsis ProteinsCrystallography, X-RaySignal TransductionCell DeathPlant DiseasesAmino Acid MotifsProtein Structure, SecondaryProtein Structure, TertiaryMutationModels, MolecularProtein Interaction Domains and MotifsImmunity, InnateProtein MultimerizationAgrobacteriumNicotiana

Keywords

Models, Molecular570572Biochemistry and cell biology not elsewhere classifiedAmino Acid MotifsArabidopsisBLAST RESISTANCEEFFECTOR610AgrobacteriumCrystallography, X-RayProtein Structure, SecondaryBacterial ProteinsMOLECULAR-BASISTIR DOMAINBINDINGDISEASE RESISTANCECRYSTAL-STRUCTUREProtein Interaction Domains and MotifsReceptors, ImmunologicPlant DiseasesPlant ProteinsCell DeathMULTIDISCIPLINARY SCIENCESArabidopsis ProteinsPlants, Genetically ModifiedImmunity, InnateProtein Structure, TertiaryPlant LeavesCELL-DEATH1000 GeneralMutationARABIDOPSIS-THALIANAScience & Technology - Other TopicsProtein MultimerizationRESISTANCE PROTEINSignal Transduction

Sustainable Development Goals

SDG 3: 3. Good health

Additional file 1 of Genome-wide association analysis reveals a novel pathway mediated by a dual-TIR domain protein for pathogen resistance in cotton

10.6084/m9.figshare.26588391.v1figshare

Additional file 1 of Genome-wide association analysis reveals a novel pathway mediated by a dual-TIR domain protein for pathogen resistance in cotton

10.6084/m9.figshare.26588391figshare

Additional file 2 of Genome-wide association analysis reveals a novel pathway mediated by a dual-TIR domain protein for pathogen resistance in cotton

10.6084/m9.figshare.26588394.v1figshare

Additional file 2 of Genome-wide association analysis reveals a novel pathway mediated by a dual-TIR domain protein for pathogen resistance in cotton

10.6084/m9.figshare.26588394figshare

Additional file 3 of Genome-wide association analysis reveals a novel pathway mediated by a dual-TIR domain protein for pathogen resistance in cotton

10.6084/m9.figshare.26588397.v1figshare