Evidence map›Paper›PMID 30534605›Full record

ArticleCommunications biology2018

Rapid characterization of secreted recombinant proteins by native mass spectrometry.

Gili Ben-Nissan, Shay Vimer, Shira Warszawski, Aliza Katz, Meital Yona, Tamar Unger, Yoav Peleg, David Morgenstern, Hadas Cohen-Dvashi, Ron Diskin and 2 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

16 citing papers in PubMed, 33 citations in OpenAlex.

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  6. Surface-Induced Dissociation for Protein Complex Characterization.Methods in molecular biology (Clifton, N.J.) · 2022
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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

12 authors at 1 institution in 1 country.

Gili Ben-Nissan *1Department of Biomolecular Sciences, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Shay Vimer *1Department of Biomolecular Sciences, Weizmann Institute of Science, 7610001 Rehovot, Israel.ORCID 0000-0002-2289-6333
Shira Warszawski1Department of Biomolecular Sciences, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Aliza Katz2Department of Structural Biology, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Meital Yona3Israel Structural Proteomics Center, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Tamar Unger3Israel Structural Proteomics Center, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Yoav Peleg3Israel Structural Proteomics Center, Weizmann Institute of Science, 7610001 Rehovot, Israel.
David Morgenstern4The De Botton protein Profiling Institute of the Nancy and Stephen Grand Israel national Center for Personalized Medicine, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Hadas Cohen-Dvashi2Department of Structural Biology, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Ron Diskin2Department of Structural Biology, Weizmann Institute of Science, 7610001 Rehovot, Israel.ORCID 0000-0002-2837-5897
Sarel J Fleishman1Department of Biomolecular Sciences, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Michal Sharon1Department of Biomolecular Sciences, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Weizmann Institute of Science · IL

Funding

European Research Council 636752
6 · The paper itself

Abstract

Characterization of overexpressed proteins is essential for assessing their quality, and providing input for iterative redesign and optimization. This process is typically carried out following purification procedures that require pronounced cost of time and labor. Therefore, quality assessment of recombinant proteins with no prior purification offers a major advantage. Here, we report a native mass spectrometry method that enables characterization of overproduced proteins directly from culture media. Properties such as solubility, molecular weight, folding, assembly state, overall structure, post-translational modifications and binding to relevant biomolecules are immediately revealed. We show the applicability of the method for in-depth characterization of secreted recombinant proteins from eukaryotic systems such as yeast, insect, and human cells. This method, which can be readily extended to high-throughput analysis, considerably shortens the time gap between protein production and characterization, and is particularly suitable for characterizing engineered and mutated proteins, and optimizing yield and quality of overexpressed proteins.

Identifiers

PMID30534605
PMCPMC6277423
OpenAlexW2902076989

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.