Evidence map›Paper›PMID 33411018›Full record

ArticleJournal of molecular modeling2021

Microcanonical insights into the physicochemical stability of the coformulation of insulin with amylin analogues.

Rafael B Frigori, Fabio Rodrigues

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of molecular modeling, 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
0.2field-weighted citation impact, top 53% 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

0 citing papers in PubMed, 3 citations in OpenAlex.

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

2 authors at 1 institution in 1 country.

Rafael B FrigoriUniversidade Tecnológica Federal do Paraná, Rua Cristo Rei 19, 85902-490, Toledo, PR, Brazil. frigori@utfpr.edu.br.ORCID http://orcid.org/0000-0002-4861-7240
Fabio RodriguesUniversidade Tecnológica Federal do Paraná, Rua Cristo Rei 19, 85902-490, Toledo, PR, Brazil.
Universidade Tecnológica Federal do Paraná · BR

Funding

Laboratório Nacional de Computação Científica PHAST2
6 · The paper itself

Abstract

Injections of insulin are the main treatment for diabetes, but in the long run this therapy can induce serious drawbacks. This has inspired new drugs able to decrease insulin requirements. For instance, human amylin (hIAPP) is a small hormone cosecreted by pancreatic β-cells with insulin to which is a synergistic partner. However, the high amyloidogenicity of hIAPP precluded it as a therapeutics and led to the design of pramlintide (sIAPP), a chimeric analogue with substitutions (A25P, S28P, and S29P) inherited from the aggregation-resistant rat isoform (rIAPP). Despite sIAPP advantages, it still shares with hIAPP a poorly soluble profile at physiological pH that hampers its mixture with insulin. Recent improvements, as charge-enhanced mutants, have been proposed. For instance, sIAPP

Indexed as

Chemical PhenomenaDrug CompoundingAnimalsHumansInsulinIslet Amyloid PolypeptideProtein MultimerizationRatsThermodynamicsInsulinIslet Amyloid PolypeptideAggregationAmylinDiabetesInsulin coformulationsMonte CarloProtein-protein interactionsRational drug design

Identifiers

PMID33411018
OpenAlexW3121054107

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.