Evidence map›Paper›PMID 37638851›Full record

ArticleProtein science : a publication of the Protein Society2023

Hydrophobicity and molecular mass-based separation method for autoantibody discovery from mammalian total cellular proteins.

Mirei Date, Ai Miyamoto, Tomoko Honjo, Tsugumi Shiokawa, Hiroko Tada, Nobuhiro Okada, Junichiro Futami

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.1field-weighted citation impact, top 21% 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

5 citing papers in PubMed, 5 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

7 authors at 2 institutions in 1 country.

Mirei DateGraduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.
Ai MiyamotoGraduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.
Tomoko HonjoGraduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.
Tsugumi ShiokawaDivision of Instrumental Analysis, Department of Instrumental Analysis and Cryogenics, Advanced Science Research Center, Okayama University, Okayama, Japan.
Hiroko TadaDivision of Instrumental Analysis, Department of Instrumental Analysis and Cryogenics, Advanced Science Research Center, Okayama University, Okayama, Japan.
Nobuhiro OkadaGraduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.
Junichiro FutamiGraduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.ORCID 0000-0002-0020-2855
Okayama University · JPOkayama University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Serum autoantibody profiles are unique to individuals and reflect the level and history of autoimmunity and tumor immunity. The identification of autoantibody biomarkers is critical for the development of immune monitoring systems for immune-related disorders. Here, we present a practical method for large-scale autoantibody discovery using total cellular proteins from cultured mammalian cells. We found that nucleic acid-free and fully denatured water-soluble total cellular proteins from mammalian cells were superior, allowing precise separation by reversed-phase HPLC after preparing a large set of homogeneous total cellular proteins. After separating the proteins based on hydrophobicity, the fractionated samples were subjected to molecular mass analysis using conventional SDS-PAGE. The resulting two-dimensional gel electrophoresis was successfully employed for immune blotting and LC-MS/MS analysis. All procedures, including TRIzol-based total cellular protein extraction, solubilization of denatured proteins, reversed-phase HPLC separation, and SDS-PAGE, were highly reproducible and easily scalable. We propose this novel two-dimensional gel electrophoresis system as an alternative proteomics-based methodology suitable for large-scale autoantibody discovery.

Indexed as

AutoantibodiesTandem Mass SpectrometryAnimalsChromatography, LiquidElectrophoresis, Polyacrylamide GelHumansHydrophobic and Hydrophilic InteractionsMammalsProteinsAutoantibodiesProteinsautoantibodybiomarkerprotein chemistryprotein denaturationprotein engineeringproteomics

Identifiers

PMID37638851
PMCPMC10503409
OpenAlexW4386209638

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.