Evidence map›Paper›PMID 34947648›Full record

ArticleNanomaterials (Basel, Switzerland)2021

Quantitative Assessment of Chirality of Protein Secondary Structures and Phenylalanine Peptide Nanotubes.

Alla Sidorova, Vladimir Bystrov, Aleksey Lutsenko, Denis Shpigun, Ekaterina Belova, Ilya Likhachev

Abstract read
In one paragraph

Article in Nanomaterials (Basel, Switzerland), 2021. 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
–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

5 citing papers in PubMed.

  1. Advances in Alzheimer's Disease-Associated Aβ Therapy Based on Peptide.International journal of molecular sciences · 2023
    Review
  2. Article
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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

6 authors.

Alla SidorovaFaculty of Physics, Lomonosov Moscow State University, 119991 Moscow, Russia.
Vladimir BystrovInstitute of Mathematical Problems of Biology, The Branch of Keldysh Institute of Applied Mathematics, RAS, 142290 Pushchino, Russia.ORCID 0000-0003-1487-9469
Aleksey LutsenkoFaculty of Physics, Lomonosov Moscow State University, 119991 Moscow, Russia.
Denis ShpigunFaculty of Physics, Lomonosov Moscow State University, 119991 Moscow, Russia.
Ekaterina BelovaFaculty of Physics, Lomonosov Moscow State University, 119991 Moscow, Russia.ORCID 0000-0002-7701-8765
Ilya LikhachevInstitute of Mathematical Problems of Biology, The Branch of Keldysh Institute of Applied Mathematics, RAS, 142290 Pushchino, Russia.

Funding

Russian Foundation for Basic Research 20-51-53014_GFEN_a
6 · The paper itself

Abstract

In this study we consider the features of spatial-structure formation in proteins and their application in bioengineering. Methods for the quantitative assessment of the chirality of regular helical and irregular structures of proteins are presented. The features of self-assembly of phenylalanine (F) into peptide nanotubes (PNT), which form helices of different chirality, are also analyzed. A method is proposed for calculating the magnitude and sign of the chirality of helix-like peptide nanotubes using a sequence of vectors for the dipole moments of individual peptides.

Indexed as

chiralitydipole momentshelical structuresmolecular modelingpeptide nanotubesphenylalaninepolarizationprotein secondary structureself-assembly

Identifiers

PMID34947648
PMCPMC8707344

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.