Evidence map›Paper›PMID 28078551›Full record

ArticlePhotosynthesis research2017

The proteolysis adaptor, NblA, binds to the N-terminus of β-phycocyanin: Implications for the mechanism of phycobilisome degradation.

Amelia Y Nguyen, William P Bricker, Hao Zhang, Daniel A Weisz, Michael L Gross, Himadri B Pakrasi

Open access · greenAbstract read
In one paragraph

Article in Photosynthesis research, 2017. 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
2.0field-weighted citation impact, top 13% 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, 38 citations in OpenAlex.

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  9. Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  14. Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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

6 authors at 3 institutions in 1 country.

Amelia Y NguyenDepartment of Biology, Washington University, Campus Box 1095, One Brookings Drive, St. Louis, MO, 63130-4899, USA.
William P BrickerLaboratory for Computational Biology & Biophysics, Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.ORCID http://orcid.org/0000-0001-9724-0905
Hao ZhangDepartment of Chemistry, Washington University, St. Louis, MO, 63130, USA.
Daniel A WeiszDepartment of Biology, Washington University, Campus Box 1095, One Brookings Drive, St. Louis, MO, 63130-4899, USA.
Michael L GrossDepartment of Chemistry, Washington University, St. Louis, MO, 63130, USA.
Himadri B PakrasiDepartment of Biology, Washington University, Campus Box 1095, One Brookings Drive, St. Louis, MO, 63130-4899, USA. pakrasi@wustl.edu.ORCID http://orcid.org/0000-0001-8240-2123
Washington University in St. Louis · USEnvironmental Protection Agency · USMassachusetts Institute of Technology · US

Funding

TrainingP41GM103422 · NIGMS · WASHINGTON UNIVERSITY · PI YARASHESKI, KEVIN E · 2012 to 2019
$12.0M
A MASS SPECTROMETER FOR PROTEIN FOOTPRINTINGS10OD016298 · OD · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 2014 to 2014
$450k
NIGMS NIH HHS P41 GM103422NIH HHS S10 OD016298
6 · The paper itself

Abstract

Phycobilisome (PBS) complexes are massive light-harvesting apparati in cyanobacteria that capture and funnel light energy to the photosystem. PBS complexes are dynamically degraded during nutrient deprivation, which causes severe chlorosis, and resynthesized during nutrient repletion. PBS degradation occurs rapidly after nutrient step down, and is specifically triggered by non-bleaching protein A (NblA), a small proteolysis adaptor that facilitates interactions between a Clp chaperone and phycobiliproteins. Little is known about the mode of action of NblA during PBS degradation. In this study, we used chemical cross-linking coupled with LC-MS/MS to investigate the interactions between NblA and phycobiliproteins. An isotopically coded BS

Indexed as

Bacterial ProteinsCross-Linking ReagentsMass SpectrometryPhycobilisomesPhycocyaninRecombinant Fusion ProteinsSynechococcusTandem Mass SpectrometryBacterial ProteinsCross-Linking ReagentsPhycobilisomesPhycocyaninRecombinant Fusion ProteinsCross-linkingCyanobacteriaMass spectrometryNitrogen starvationPhycobilisome proteolysisProtein docking

Identifiers

PMID28078551
PMCPMC5576716
OpenAlexW2571939031

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.