Evidence map›Paper›PMID 28510001›Full record

ReviewBiophysical reviews2012

Proteoliposomes in nanobiotechnology.

P Ciancaglini, A M S Simão, M Bolean, J L Millán, C F Rigos, J S Yoneda, M C Colhone, R G Stabeli

Open access · bronzeAbstract readReview
In one paragraph

Review in Biophysical reviews, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

26 citing papers in PubMed, 54 citations in OpenAlex.

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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

8 authors at 4 institutions in 2 countries.

P CiancagliniDepartamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto da (FFCLRP), Universidade de São Paulo - USP, 14040-901, Ribeirão Preto, SP, Brazil. pietro@ffclrp.usp.br.
A M S SimãoDepartamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto da (FFCLRP), Universidade de São Paulo - USP, 14040-901, Ribeirão Preto, SP, Brazil.
M BoleanDepartamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto da (FFCLRP), Universidade de São Paulo - USP, 14040-901, Ribeirão Preto, SP, Brazil.
J L MillánSanford Children's Health Research Center, Sanford - Burnham Medical Research Institute, La Jolla, CA, USA.
C F RigosDepartamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto da (FFCLRP), Universidade de São Paulo - USP, 14040-901, Ribeirão Preto, SP, Brazil.
J S YonedaDepartamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto da (FFCLRP), Universidade de São Paulo - USP, 14040-901, Ribeirão Preto, SP, Brazil.
M C ColhoneDepartamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto da (FFCLRP), Universidade de São Paulo - USP, 14040-901, Ribeirão Preto, SP, Brazil.
R G StabeliCentro de Estudos de Biomoléculas Aplicadas a Medicina, Núcleo de Saúde (NUSAU), Universidade Federal de Rondônia (UNIR), 76800-000, Porto Velho, RO, Brazil.
Universidade de São Paulo · BRUniversidade de Ribeirão Preto · BRSanford Burnham Prebys Medical Discovery Institute · USUniversidade Federal de Rondônia · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteoliposomes are systems that mimic lipid membranes (liposomes) to which a protein has been incorporated or inserted. During the last decade, these systems have gained prominence as tools for biophysical studies on lipid-protein interactions as well as for their biotechnological applications. Proteoliposomes have a major advantage when compared with natural membrane systems, since they can be obtained with a smaller number of lipidic (and protein) components, facilitating the design and interpretation of certain experiments. However, they have the disadvantage of requiring methodological standardization for incorporation of each specific protein, and the need to verify that the reconstitution procedure has yielded the correct orientation of the protein in the proteoliposome system with recovery of its functional activity. In this review, we chose two proteins under study in our laboratory to exemplify the steps necessary for the standardization of the reconstitution of membrane proteins in liposome systems: (1) alkaline phosphatase, a protein with a glycosylphosphatidylinositol anchor, and (2) Na,K-ATPase, an integral membrane protein. In these examples, we focus on the production of the specific proteoliposomes, as well as on their biochemical and biophysical characterization, with emphasis on studies of lipid-protein interactions. We conclude the chapter by highlighting current prospects of this technology for biotechnological applications, including the construction of nanosensors and of a multi-protein nanovesicular biomimetic to study the processes of initiation of skeletal mineralization.

Indexed as

Alkaline phosphataseBiomineralizationBiotechnologyLeishmaniasisNa,K-ATPaseNanosensorProteoliposomes

Identifiers

PMID28510001
PMCPMC5418368
OpenAlexW2042585338

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.