Evidence map›Paper›PMID 30192967›Full record

ReviewPlant & cell physiology2018

Uncoiling CNLs: Structure/Function Approaches to Understanding CC Domain Function in Plant NLRs.

Adam R Bentham, Rafal Zdrzalek, Juan Carlos De la Concepcion, Mark J Banfield

Open access · hybridAbstract readReview
In one paragraph

Review in Plant & cell physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
12.2field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
  2. Article
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  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. NLRscape: an atlas of plant NLR proteins.Nucleic acids research · 2023
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Adam R BenthamDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, UK.
Rafal ZdrzalekDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, UK.
Juan Carlos De la ConcepcionDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, UK.
Mark J BanfieldDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, UK.
John Innes Centre · GBNorwich Research Park · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant nucleotide-binding leucine-rich repeat receptors (NLRs) are intracellular pathogen receptors whose N-terminal domains are integral to signal transduction after perception of a pathogen-derived effector protein. The two major plant NLR classes are defined by the presence of either a Toll/interleukin-1 receptor (TIR) or a coiled-coil (CC) domain at their N-terminus (TNLs and CNLs). Our knowledge of how CC domains function in plant CNLs lags behind that of how TIR domains function in plant TNLs. CNLs are the most abundant class of NLRs in monocotyledonous plants, and further research is required to understand the molecular mechanisms of how these domains contribute to disease resistance in cereal crops. Previous studies of CC domains have revealed functional diversity, making categorization difficult, which in turn makes experimental design for assaying function challenging. In this review, we summarize the current understanding of CC domain function in plant CNLs, highlighting the differences in modes of action and structure. To aid experimental design in exploring CC domain function, we present a 'best-practice' guide to designing constructs through use of sequence and secondary structure comparisons and discuss the relevant assays for investigating CC domain function. Finally, we discuss whether using homology modeling is useful to describe putative CC domain function in CNLs through parallels with the functions of previously characterized helical adaptor proteins.

Indexed as

NLR ProteinsPlant ProteinsPlantsProtein DomainsProtein Structure, SecondaryStructure-Activity RelationshipNLR ProteinsPlant Proteins

Identifiers

PMID30192967
PMCPMC6290485
OpenAlexW2891027636

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.