Evidence map›Paper›PMID 34944399›Full record

ArticleBiomolecules2021

Planar Boronic Graphene and Nitrogenized Graphene Heterostructure for Protein Stretch and Confinement.

Xuchang Su, Zhi He, Lijun Meng, Hong Liang, Ruhong Zhou

Abstract read
In one paragraph

Article in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Xuchang SuDepartment of Physics, Hangzhou Dianzi University, Hangzhou 310018, China.
Zhi HeInstitute of Quantitative Biology, College of Life Sciences, Zhejiang University, Hangzhou 310027, China.
Lijun MengInstitute of Quantitative Biology, College of Life Sciences, Zhejiang University, Hangzhou 310027, China.
Hong LiangDepartment of Physics, Hangzhou Dianzi University, Hangzhou 310018, China.
Ruhong ZhouInstitute of Quantitative Biology, College of Life Sciences, Zhejiang University, Hangzhou 310027, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-molecule techniques such as electron tunneling and atomic force microscopy have attracted growing interests in protein sequencing. For these methods, it is critical to refine and stabilize the protein sample to a "suitable mode" before applying a high-fidelity measurement. Here, we show that a planar heterostructure comprising boronic graphene (BC

Indexed as

alpha-SynucleinAmyloid beta-PeptidesAnimalsBoronGraphiteHumansIntrinsically Disordered ProteinsModels, MolecularMolecular Dynamics SimulationNitrogenPeptide FragmentsPeptidesProtein ConformationSingle Molecule Imagingalpha-SynucleinAmyloid beta-Peptidesamyloid beta-protein (1-42)BoronGraphiteIntrinsically Disordered ProteinsNitrogenPeptide FragmentsPeptidespolyglutamineboronic grapheneinplane heterostructuremolecular dynamics simulationnitrogenized grapheneprotein stretch and confinement

Identifiers

PMID34944399
PMCPMC8698321

What OpenQuestion holds

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Registered trials

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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.