Evidence map›Paper›PMID 32696394›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2020

In-Cell NMR of Intrinsically Disordered Proteins in Mammalian Cells.

Juan A Gerez, Natalia C Prymaczok, Roland Riek

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2020. 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
11.6field-weighted citation impact, top 1% 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, 12 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

3 authors at 1 institution in 1 country.

Juan A GerezLaboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zurich, Zurich, Switzerland. juan.gerez@phys.chem.ethz.ch.
Natalia C PrymaczokLaboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zurich, Zurich, Switzerland.
Roland RiekLaboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zurich, Zurich, Switzerland. roland.riek@phys.chem.ethz.ch.
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In-cell NMR enables structural insights at atomic resolution of proteins in their natural environment. To date, very few methods have been developed to study proteins by in-cell NMR in mammalian systems. Here we describe a detailed protocol to conduct in-cell NMR on the intrinsically disordered protein of alpha-Synuclein (αSyn) in mammalian cells. This chapter includes a simplified expression and purification protocol of recombinant αSyn and its delivery into mammalian cells. The chapter also describes how to assess the cell leakage that might occur to the cells, the setup of the instrument, and how to perform basic analyses with the obtained NMR data.

Indexed as

alpha-SynucleinAnimalsElectrophoresis, Polyacrylamide GelElectroporationEscherichia coliHEK293 CellsHumansIntrinsically Disordered ProteinsIsotope LabelingMammalsNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularRecombinant ProteinsRosaniline DyesSingle-Cell AnalysisStaining and Labelingalpha-Synucleincoomassie Brilliant BlueIntrinsically Disordered ProteinsNitrogen-15Nitrogen IsotopesRecombinant ProteinsRosaniline DyesElectroporationIDPLeakageNuclear magnetic resonanceα-synuclein

Identifiers

PMID32696394
OpenAlexW3044931079

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.