Evidence map›Paper›PMID 33680037›Full record

ArticleIranian journal of pharmaceutical research : IJPR2020

Synthesis of Novel Peptides Using Unusual Amino Acids.

Bahareh Talaei, Vaezeh Fathi Vavsari, Saeed Balalaie, Armin Arabanian, Hamid Reza Bijanzadeh

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Iranian journal of pharmaceutical research : IJPR, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 52% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Review
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 at 2 institutions in 1 country.

Bahareh TalaeiPeptide Chemistry Research Institute, K. N. Toosi University of Technology, P.O. Box 15875-4416 Tehran, Iran.
Vaezeh Fathi VavsariPeptide Chemistry Research Institute, K. N. Toosi University of Technology, P.O. Box 15875-4416 Tehran, Iran.
Saeed BalalaiePeptide Chemistry Research Institute, K. N. Toosi University of Technology, P.O. Box 15875-4416 Tehran, Iran.
Armin ArabanianPeptide Chemistry Research Institute, K. N. Toosi University of Technology, P.O. Box 15875-4416 Tehran, Iran.
Hamid Reza BijanzadehDepartment of Environmental Sciences, Faculty of Natural Resources and Marine Sciences, Tarbiat Modares University, Tehran, Iran.
K.N.Toosi University of Technology · IRTarbiat Modares University · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small peptides are valuable peptides due to their extended biological activities. Their activities could be categorized according to their low antigenicity, osmotic pressure, and also because of their astonishing bioactivities. For example, the aggression of Phe-Phe fibers via self-assembly and intermolecular hydrogen bonding is the main reason for the formation of Alzheimer's β-amyloid fibrils. Hydrogen bonding is the main intramolecular interaction in peptides, while the presence of aromatic ring leads to the π-π stacking and affects the self-assembly and aggression. Thus, insertion of an unusual amino acid into peptide sequence facilitates the formation of intramolecular bonds, lipophilicity and its conformation. To design new small peptides with remarkable lipophilicity, it is an idea to employ

Indexed as

and tetra- peptidesBaclofenGabapentinHydrogen bondingPhenylalanineSynthesis of di-tri-Unusual amino acids

Identifiers

PMID33680037
PMCPMC7757983
OpenAlexW3121245498

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.