Evidence map›Paper›PMID 30097007›Full record

ArticleBMC plant biology2018

In silico insights on diverse interacting partners and phosphorylation sites of respiratory burst oxidase homolog (Rbohs) gene families from Arabidopsis and rice.

Gurpreet Kaur, Pratap Kumar Pati

Abstract read
In one paragraph

Article in BMC plant biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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3 · Its place in the literature

Who cites it

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Arabidopsis RboHB Encoded byInternational journal of molecular sciences · 2020
    Article
  6. Article
  7. Superoxide Radical Metabolism in Sweet Pepper (Frontiers in plant science · 2020
    Article
  8. Article
  9. Article
4 · The record

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5 · Who and what money

Authors and funding

2 authors.

Gurpreet KaurDepartment of Biotechnology, Guru Nanak Dev University (GNDU), Amritsar, Punjab, 143005, India.
Pratap Kumar PatiDepartment of Biotechnology, Guru Nanak Dev University (GNDU), Amritsar, Punjab, 143005, India. pkpati@yahoo.com.ORCID http://orcid.org/0000-0001-9017-7608

Funding

Department of Biotechnology (DBT), Government of India BT/PR13965/BRB/10/883/2010Innovation in Science Pursuit for Inspired Research (INSPIRE) Programme, Department of Science and Technology (DST), Government of India DST/INSPIRE Fellowship/2010[79]
6 · The paper itself

Abstract

backgroundNADPH oxidase (Nox) is a critical enzyme involved in the generation of apoplastic superoxide (O

resultsIn this work, an extensive range of potential partners (unique and common), leading to diverse functions were revealed from interaction networks and gene ontology classifications, where majority of AtRbohs and OsRbohs play role in stress-related activities, followed by cellular development. Further, 68 and 38 potential phosphorylation sites were identified in AtRbohs and OsRbohs, respectively. Their distribution, location and kinase specificities were also predicted and correlated with experimental data as well as verified with the other EF-hand containing proteins within both genomes.

conclusionsAnalysis of regulatory mechanisms including interaction with diverse partners and post-translational modifications like phosphorylation have provided insights regarding functional multiplicity of Rbohs. The bioinformatics-based workflow in the current study can be used to get insights for interacting partners and phosphorylation sites from Rbohs of other plant species.

Indexed as

Amino AcidsArabidopsisArabidopsis ProteinsComputer SimulationGene Regulatory NetworksGenes, PlantGenome-Wide Association StudyOryzaOxidoreductasesPhosphorylationPlant ProteinsProtein Interaction MapsRespiratory BurstSubstrate SpecificityAmino AcidsArabidopsis ProteinsOxidoreductasesPlant ProteinsEF-handsInteracting partnersNetworkPhosphorylation sitesPlant NADPH oxidaseRboh

Identifiers

PMID30097007
PMCPMC6086027

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.