Evidence map›Paper›PMID 23290725›Full record

ArticleStructure (London, England : 1993)2013

Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities.

Graham M West, Bruce D Pascal, Ley-Moy Ng, Fen-Fen Soon, Karsten Melcher, H Eric Xu, Michael J Chalmers, Patrick R Griffin

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
6.9field-weighted citation impact, top 4% 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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Optimized Workflow for Selecting Peptides for HDX-MS Data Analyses.Journal of the American Society for Mass Spectrometry · 2018
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Time window expansion for HDX analysis of an intrinsically disordered protein.Journal of the American Society for Mass Spectrometry · 2013
    Article
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.

Graham M WestDepartment of Molecular Therapeutics, The Scripps Research Institute, Scripps Florida, Jupiter, FL 33458, USA.
Bruce D Pascal
Ley-Moy Ng
Fen-Fen Soon
Karsten Melcher
H Eric Xu
Michael J Chalmers
Patrick R Griffin
Scripps Research Institute · USVan Andel Institute · US

Funding

Structural Genomics of Orphan Nuclear ReceptorsR01DK071662 · NIDDK · VAN ANDEL RESEARCH INSTITUTE · PI XU, H ERIC · 2005 to 2017
$5.1M
Development of H/D exchange technology for the study of large protein complexesR01GM084041 · NIGMS · SCRIPPS FLORIDA · PI GRIFFIN, PATRICK ROBERT · 2009 to 2012
$1.6M
Structural and functional analysis of a dynamic ABA signaling complexR01GM102545 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI MELCHER, KARSTEN · 2012 to 2014
$1.1M
Acquisition of a LTQ/Orbitrap MS to advance the study of protein dynamicsS10RR027270 · NCRR · SCRIPPS RESEARCH INSTITUTE, THE · PI GRIFFIN, PATRICK ROBERT · 2010 to 2010
$500k
NCRR NIH HHS S10 RR027270NIDDK NIH HHS R01 DK071662NIGMS NIH HHS R01 GM084041NIGMS NIH HHS R01 GM102545
6 · The paper itself

Abstract

Plants regulate growth and respond to environmental stress through abscisic acid (ABA) regulated pathways, and as such these pathways are of primary interest for biological and agricultural research. The ABA response is first perceived by the PYR/PYL/RCAR class of START protein receptors. These ABA activated receptors disrupt phosphatase inhibition of Snf1-related kinases (SnRKs), enabling kinase signaling. Here, insights into the structural mechanism of proteins in the ABA signaling pathway (the ABA receptor PYL2, HAB1 phosphatase, and two kinases, SnRK2.3 and 2.6) are discerned through hydrogen/deuterium exchange (HDX) mass spectrometry. HDX on the phosphatase in the presence of binding partners provides evidence for receptor-specific conformations involving the Trp385 "lock" that is necessary for signaling. Furthermore, kinase activity is linked to a more stable "closed" conformation. These solution-based studies complement the static crystal structures and provide a more detailed understanding of the ABA signaling pathway.

Indexed as

ArabidopsisSignal TransductionAbscisic AcidAdenosine TriphosphateAmino Acid SequenceArabidopsis ProteinsDeuterium Exchange MeasurementHydrogen BondingModels, MolecularMolecular Sequence DataPhosphoprotein PhosphatasesProtein BindingProtein Interaction Domains and MotifsProtein KinasesProtein Serine-Threonine KinasesProtein StabilityAbscisic AcidAdenosine TriphosphateArabidopsis ProteinsHAB1 protein, ArabidopsisOST1 protein, ArabidopsisPhosphoprotein PhosphatasesProtein KinasesProtein Serine-Threonine KinasesPYL2 protein, ArabidopsisSnRK2 protein, Arabidopsis

Identifiers

PMID23290725
PMCPMC3570687
OpenAlexW2056764195

What OpenQuestion holds

Textmetadata
LicenceTDM
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.