Evidence map›Paper›PMID 25122472›Full record

ArticlePlant physiology2014

Label-free protein quantification for plant Golgi protein localization and abundance.

Nino Nikolovski, Pavel V Shliaha, Laurent Gatto, Paul Dupree, Kathryn S Lilley

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 14% 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

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 51 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Nino NikolovskiDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom (N.N., P.V.S., L.G., P.D., K.S.L.); Computational Proteomics Unit (L.G.), and Cambridge Centre for Proteomics, Cambridge Systems Biology Centre (N.N., P.S., L.G., K.L.), Department of Biochemistry, University of Cambridge, Cambridge CB2 1QR, United Kingdom.ORCID http://orcid.org/0000-0002-5136-9161
Pavel V ShliahaDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom (N.N., P.V.S., L.G., P.D., K.S.L.); Computational Proteomics Unit (L.G.), and Cambridge Centre for Proteomics, Cambridge Systems Biology Centre (N.N., P.S., L.G., K.L.), Department of Biochemistry, University of Cambridge, Cambridge CB2 1QR, United Kingdom.
Laurent GattoDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom (N.N., P.V.S., L.G., P.D., K.S.L.); Computational Proteomics Unit (L.G.), and Cambridge Centre for Proteomics, Cambridge Systems Biology Centre (N.N., P.S., L.G., K.L.), Department of Biochemistry, University of Cambridge, Cambridge CB2 1QR, United Kingdom.ORCID http://orcid.org/0000-0002-1520-2268
Paul DupreeDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom (N.N., P.V.S., L.G., P.D., K.S.L.); Computational Proteomics Unit (L.G.), and Cambridge Centre for Proteomics, Cambridge Systems Biology Centre (N.N., P.S., L.G., K.L.), Department of Biochemistry, University of Cambridge, Cambridge CB2 1QR, United Kingdom pd101@cam.ac.uk k.s.lilley@bioc.cam.ac.uk.ORCID http://orcid.org/0000-0001-9270-6286
Kathryn S LilleyDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom (N.N., P.V.S., L.G., P.D., K.S.L.); Computational Proteomics Unit (L.G.), and Cambridge Centre for Proteomics, Cambridge Systems Biology Centre (N.N., P.S., L.G., K.L.), Department of Biochemistry, University of Cambridge, Cambridge CB2 1QR, United Kingdom pd101@cam.ac.uk k.s.lilley@bioc.cam.ac.uk.ORCID http://orcid.org/0000-0003-0594-6543
University of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G016240/1Biotechnology and Biological Sciences Research Council BBS/B/10684
6 · The paper itself

Abstract

The proteomic composition of the Arabidopsis (Arabidopsis thaliana) Golgi apparatus is currently reasonably well documented; however, little is known about the relative abundances between different proteins within this compartment. Accurate quantitative information of Golgi resident proteins is of great importance: it facilitates a better understanding of the biochemical processes that take place within this organelle, especially those of different polysaccharide synthesis pathways. Golgi resident proteins are challenging to quantify because the abundance of this organelle is relatively low within the cell. In this study, an organelle fractionation approach targeting the Golgi apparatus was combined with a label-free quantitative mass spectrometry (data-independent acquisition method using ion mobility separation known as LC-IMS-MS(E) [or HDMS(E)]) to simultaneously localize proteins to the Golgi apparatus and assess their relative quantity. In total, 102 Golgi-localized proteins were quantified. These data show that organelle fractionation in conjunction with label-free quantitative mass spectrometry is a powerful and relatively simple tool to access protein organelle localization and their relative abundances. The findings presented open a unique view on the organization of the plant Golgi apparatus, leading toward unique hypotheses centered on the biochemical processes of this organelle.

Indexed as

ArabidopsisArabidopsis ProteinsChromatography, LiquidGolgi ApparatusMass SpectrometryOrganellesArabidopsis Proteins

Identifiers

PMID25122472
PMCPMC4213074
OpenAlexW2149041246

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.