Evidence map›Paper›PMID 32824918›Full record

ArticleBiomolecules2020

Lipid Modulation in the Formation of β-Sheet Structures. Implications for De Novo Design of Human Islet Amyloid Polypeptide and the Impact on β-Cell Homeostasis.

Israel Martínez-Navarro, Raúl Díaz-Molina, Angel Pulido-Capiz, Jaime Mas-Oliva, Ismael Luna-Reyes, Eustolia Rodríguez-Velázquez, Ignacio A Rivero, Marco A Ramos-Ibarra, Manuel Alatorre-Meda, Victor García-González

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 38% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
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  5. Review
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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

10 authors at 3 institutions in 1 country.

Israel Martínez-NavarroDepartamento de Bioquímica, Facultad de Medicina Mexicali, Universidad Autónoma de Baja California, Mexicali 21000, Baja California, Mexico.
Raúl Díaz-MolinaDepartamento de Bioquímica, Facultad de Medicina Mexicali, Universidad Autónoma de Baja California, Mexicali 21000, Baja California, Mexico.ORCID 0000-0002-9400-5683
Angel Pulido-CapizDepartamento de Bioquímica, Facultad de Medicina Mexicali, Universidad Autónoma de Baja California, Mexicali 21000, Baja California, Mexico.
Jaime Mas-OlivaInstituto de Fisiología Celular, Universidad Nacional Autónoma de México, Ciudad de Mexico 04510, Mexico.ORCID 0000-0001-8007-6993
Ismael Luna-ReyesInstituto de Fisiología Celular, Universidad Nacional Autónoma de México, Ciudad de Mexico 04510, Mexico.
Eustolia Rodríguez-VelázquezFacultad de Odontología, Universidad Autónoma de Baja California, Tijuana 22390, Mexico.
Ignacio A RiveroTecnológico Nacional de México/Instituto Tecnológico de Tijuana, Centro de Graduados e Investigación en Química, Tijuana 22510, Baja California, Mexico.
Marco A Ramos-IbarraFacultad de Ciencias Químicas e Ingeniería, Universidad Autónoma de Baja California, Tijuana 22390, Baja California, Mexico.ORCID 0000-0002-8950-2079
Manuel Alatorre-MedaCátedras CONACyT- Tecnológico Nacional de México/I.T. Tijuana, Centro de Graduados e Investigación en Química-Grupo de Biomateriales y Nanomedicina, Tijuana 22510, Mexico.ORCID 0000-0002-3301-9619
Victor García-GonzálezDepartamento de Bioquímica, Facultad de Medicina Mexicali, Universidad Autónoma de Baja California, Mexicali 21000, Baja California, Mexico.ORCID 0000-0002-9421-3730
Universidad Autónoma de Baja California · MXTecnológico Nacional de México · MXUniversidad Nacional Autónoma de México · MX

Funding

21a. Convocatoria Interna de Apoyo a Proyectos de Investigación Coordinación General de Investigación y Posgrado/UABCCoordinación de Posgrado e Investigación-UABC 106/2/N/57/1 (1983)DGTIC-UNAM (supercomputing cluster MIZTLI) LANCAD-UNAM-DGTIC-352Fondo Sectorial de Investigación para la Educación CB 2017-2018 A1-S-28653/SEP/CONACYT
6 · The paper itself

Abstract

Human islet amyloid polypeptide (hIAPP) corresponds to a 37-residue hormone present in insulin granules that maintains a high propensity to form β-sheet structures during co-secretion with insulin. Previously, employing a biomimetic approach, we proposed a panel of optimized IAPP sequences with only one residue substitution that shows the capability to reduce amyloidogenesis. Taking into account that specific membrane lipids have been considered as a key factor in the induction of cytotoxicity, in this study, following the same design strategy, we characterize the effect of a series of lipids upon several polypeptide domains that show the highest aggregation propensity. The characterization of the C-native segment of hIAPP (residues F

Indexed as

HomeostasisHumansInsulin-Secreting CellsIslet Amyloid PolypeptideLipidsProtein Conformation, beta-StrandIslet Amyloid PolypeptideLipidsamyloidogenesisanionic lipidsendoplasmic reticulumF23R varianthIAPPinsulin granulesunfolded protein responseβ-cell cytotoxicityβ-sheet transitions

Identifiers

PMID32824918
PMCPMC7563882
OpenAlexW3073221348

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.