Evidence map›Paper›PMID 32724895›Full record

ArticleBMC materials2020

Optimization of skeletal protein preparation for LC-MS/MS sequencing yields additional coral skeletal proteins in

Yanai Peled, Jeana L Drake, Assaf Malik, Ricardo Almuly, Maya Lalzar, David Morgenstern, Tali Mass

Open access · diamondAbstract read
In one paragraph

Article in BMC materials, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

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  16. The spatial network of skeletal proteins in a stony coral.Journal of the Royal Society, Interface · 2021
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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

7 authors at 2 institutions in 1 country.

Yanai Peled *Marine Biology Department, University of Haifa, Haifa, Israel.
Jeana L Drake *Marine Biology Department, University of Haifa, Haifa, Israel.ORCID 0000-0002-9851-379X
Assaf MalikMarine Biology Department, University of Haifa, Haifa, Israel.
Ricardo AlmulyMarine Biology Department, University of Haifa, Haifa, Israel.
Maya LalzarBioinformatics Core Unit, University of Haifa, Haifa, Israel.
David MorgensternDe Botton Protein Profiling Institute of the Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot, Israel.
Tali MassMarine Biology Department, University of Haifa, Haifa, Israel.
University of Haifa · ILWeizmann Institute of Science · IL

Funding

European Research Council 755876
6 · The paper itself

Abstract

Stony corals generate their calcium carbonate exoskeleton in a highly controlled biomineralization process mediated by a variety of macromolecules including proteins. Fully identifying and classifying these proteins is crucial to understanding their role in exoskeleton formation, yet no optimal method to purify and characterize the full suite of extracted coral skeletal proteins has been established and hence their complete composition remains obscure. Here, we tested four skeletal protein purification protocols using acetone precipitation and ultrafiltration dialysis filters to present a comprehensive scleractinian coral skeletal proteome. We identified a total of 60 proteins in the coral skeleton, 44 of which were not present in previously published stony coral skeletal proteomes. Extracted protein purification protocols carried out in this study revealed that no one method captures all proteins and each protocol revealed a unique set of method-exclusive proteins. To better understand the general mechanism of skeletal protein transportation, we further examined the proteins' gene ontology, transmembrane domains, and signal peptides. We found that transmembrane domain proteins and signal peptide secretion pathways, by themselves, could not explain the transportation of proteins to the skeleton. We therefore propose that some proteins are transported to the skeleton via non-traditional secretion pathways.

Indexed as

BiomineralizationScleractiniaSkeleton organic matrix proteins (SOMPs)

Identifiers

PMID32724895
PMCPMC7115838
OpenAlexW3042648811

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.