Evidence map›Paper›PMID 29495576›Full record

ArticleInternational journal of molecular sciences2018

Biochemical and MALDI-TOF Mass Spectrometric Characterization of a Novel Native and Recombinant Cystine Knot Miniprotein from Solanum tuberosum subsp. andigenum cv. Churqueña.

Juliana Cotabarren, Mariana Edith Tellechea, Sebastián Martín Tanco, Julia Lorenzo, Javier Garcia-Pardo, Francesc Xavier Avilés, Walter David Obregón

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2018. 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
–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

1 citing paper in PubMed.

  1. Article
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

7 authors.

Juliana CotabarrenCentro de Investigación de Proteínas Vegetales (CIPROVE), Departamento de Ciencias Biológicas, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, 47 y 115 s/N, La Plata B1900AVW, Argentina. cotabarren.juliana@biol.unlp.edu.ar.
Mariana Edith TellecheaCentro de Investigación de Proteínas Vegetales (CIPROVE), Departamento de Ciencias Biológicas, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, 47 y 115 s/N, La Plata B1900AVW, Argentina. mariana.edith.tellechea@gmail.com.
Sebastián Martín TancoInstitut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Campus Universitari, Bellaterra, Cerdanyola del Vallès, 08193 Barcelona, Spain. sebastiantanco@gmail.com.
Julia LorenzoInstitut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Campus Universitari, Bellaterra, Cerdanyola del Vallès, 08193 Barcelona, Spain. julia.lorenzo@uab.es.ORCID 0000-0001-5659-6008
Javier Garcia-PardoCatalan Institute of Nanoscience and Nanotechnology (ICN2), CSIC and The Barcelona Institute of Science and Technology, Campus UAB, Bellaterra, 08193 Barcelona, Spain. javiergarciapardo@msn.com.
Francesc Xavier AvilésInstitut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Campus Universitari, Bellaterra, Cerdanyola del Vallès, 08193 Barcelona, Spain. FrancescXavier.Aviles@uab.cat.
Walter David ObregónCentro de Investigación de Proteínas Vegetales (CIPROVE), Departamento de Ciencias Biológicas, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, 47 y 115 s/N, La Plata B1900AVW, Argentina. davidobregon@biol.unlp.edu.ar.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cystine-knot miniproteins (CKMPs) are an intriguing group of cysteine-rich molecules that combine the characteristics of proteins and peptides. Typically, CKMPs are fewer than 50 residues in length and share a characteristic knotted scaffold characterized by the presence of three intramolecular disulfide bonds that form the singular knotted structure. The knot scaffold confers on these proteins remarkable chemical, thermal, and proteolytic stability. Recently, CKMPs have emerged as a novel class of natural molecules with interesting pharmacological properties. In the present work, a novel cystine-knot metallocarboxypeptidase inhibitor (chuPCI) was isolated from tubers of

Indexed as

ProteomicsRecombinant ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAmino Acid SequenceAnimalsCarboxypeptidasesCattleCloning, MolecularCystine-Knot MiniproteinsEnzyme ActivationKineticsPlant ProteinsProtease InhibitorsSequence Analysis, DNASolanum tuberosumSwineCarboxypeptidasesCystine-Knot MiniproteinsPlant ProteinsProtease InhibitorsRecombinant ProteinsAndean potatoescarboxypeptidase inhibitorcystine-knot miniproteinsplant inhibitorproteaseSolanum tuberosum

Identifiers

PMID29495576
PMCPMC5877539

What OpenQuestion holds

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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.