Evidence map›Paper›PMID 25372696›Full record

ArticleActa crystallographica. Section D, Biological crystallography2014

Structure of the OsSERK2 leucine-rich repeat extracellular domain.

Ryan McAndrew, Rory N Pruitt, Shizuo G Kamita, Jose Henrique Pereira, Dipali Majumdar, Bruce D Hammock, Paul D Adams, Pamela C Ronald

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

4 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
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

8 authors at 2 institutions in 1 country.

Ryan McAndrewPhysical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA.
Rory N PruittPlant Pathology Faculty, The Genome Center, University of California, Davis, CA 95616, USA.
Shizuo G KamitaDepartment of Entomology, University of California, Davis, CA 95616, USA.
Jose Henrique PereiraPhysical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA.
Dipali MajumdarPlant Pathology Faculty, The Genome Center, University of California, Davis, CA 95616, USA.
Bruce D HammockDepartment of Entomology, University of California, Davis, CA 95616, USA.
Paul D AdamsPhysical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA.
Pamela C RonaldPlant Pathology Faculty, The Genome Center, University of California, Davis, CA 95616, USA.
University of California, Davis · USLawrence Berkeley National Laboratory · US

Funding

HYDROLYTIC ENZYMES IN THE METABOLISM OF TOXINSR01ES002710 · NIEHS · UNIVERSITY OF CALIFORNIA DAVIS · PI HAMMOCK, BRUCE D · 1985 to 2018
$4.0M
Receptor Kinase-Mediated Signaling in the Innate Immune ResponseR01GM055962 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI RONALD, PAMELA C · 1999 to 2013
$2.9M
Howard Hughes Medical InstituteNIEHS NIH HHS R01 ES002710NIGMS NIH HHS GM55962NIGMS NIH HHS R01 GM055962
6 · The paper itself

Abstract

Somatic embryogenesis receptor kinases (SERKs) are leucine-rich repeat (LRR)-containing integral membrane receptors that are involved in the regulation of development and immune responses in plants. It has recently been shown that rice SERK2 (OsSERK2) is essential for XA21-mediated resistance to the pathogen Xanthomonas oryzae pv. oryzae. OsSERK2 is also required for the BRI1-mediated, FLS2-mediated and EFR-mediated responses to brassinosteroids, flagellin and elongation factor Tu (EF-Tu), respectively. Here, crystal structures of the LRR domains of OsSERK2 and a D128N OsSERK2 mutant, expressed as hagfish variable lymphocyte receptor (VLR) fusions, are reported. These structures suggest that the aspartate mutation does not generate any significant conformational change in the protein, but instead leads to an altered interaction with partner receptors.

Indexed as

Amino Acid SequenceAnimalsCell LineCrystallography, X-RayLeucine ZippersModels, MolecularMolecular Sequence DataOryzaPlant ProteinsPoint MutationProtein ConformationProtein KinasesProtein Structure, TertiaryRecombinant Fusion ProteinsPlant ProteinsProtein KinasesRecombinant Fusion ProteinsSERK protein, plantleucine-rich repeatsOsSERK2SERKs

Identifiers

PMID25372696
PMCPMC4220978
OpenAlexW2040334086

What OpenQuestion holds

Textmetadata
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.