Evidence map›Paper›PMID 27778107›Full record

ArticlePlanta2017

A Bowman-Birk protease inhibitor purified, cloned, sequenced and characterized from the seeds of Maclura pomifera (Raf.) Schneid.

Martín Indarte, Cristian M Lazza, Diego Assis, Néstor O Caffini, María A Juliano, Francesc X Avilés, Xavier Daura, Laura M I López, Sebastián A Trejo

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Planta, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 28% 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

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
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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

9 authors at 5 institutions in 3 countries.

Martín IndartePHusisTherapeutics, 3210 Merryfield Row, San Diego, CA, 92121, USA.
Cristian M LazzaCentro de Investigación de Proteínas Vegetales, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, 1900, La Plata, Argentina.
Diego AssisDepartamento de Biofisica, Universidade Federal de São Paulo, Vila Clementino, São Paulo, 04044-020, Brazil.
Néstor O CaffiniCentro de Investigación de Proteínas Vegetales, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, 1900, La Plata, Argentina.
María A JulianoDepartamento de Biofisica, Universidade Federal de São Paulo, Vila Clementino, São Paulo, 04044-020, Brazil.
Francesc X AvilésInstitut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona, Bellaterra, 08193, Barcelona, Spain.
Xavier DauraInstitut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona, Bellaterra, 08193, Barcelona, Spain.
Laura M I LópezInstituto de Ciencias de la Salud, Universidad Nacional Arturo Jauretche, 1888 Florencio Varela, Buenos Aires, Argentina. lmilopez@biol.unlp.edu.ar.
Sebastián A TrejoLaboratorio de Neurofisiología del Instituto Multidisciplinar de Biología Celular (IMBICE), La Plata, B1906APO, Buenos Aires, Argentina. strejo@imbice.gov.ar.
Universidade Federal de São Paulo · BRUniversidad Nacional de La Plata · ARUniversitat Autònoma de Barcelona · ESInstituto Multidisciplinario de Biología Celular · ARUniversidad Nacional Arturo Jauretche · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MAIN

conclusionA new BBI-type protease inhibitor with remarkable structural characteristics was purified, cloned, and sequenced from seeds of Maclura pomifera , a dicotyledonous plant belonging to the Moraceae family. In this work, we report a Bowman-Birk inhibitor (BBI) isolated, purified, cloned, and characterized from Maclura pomifera seeds (MpBBI), the first of this type from a species belonging to Moraceae family. MpBBI was purified to homogeneity by RP-HPLC, total RNA was extracted from seeds of M. pomifera, and the 3'RACE-PCR method was applied to obtain the cDNA, which was cloned and sequenced. Peptide mass fingerprinting (PMF) analysis showed correspondence between the in silico-translated protein and MpBBI, confirming that it corresponds to a new plant protease inhibitor. The obtained cDNA encoded a polypeptide of 65 residues and possesses 10 cysteine residues, with molecular mass of 7379.27, pI 6.10, and extinction molar coefficient of 9105 M

Indexed as

Cloning, MolecularMacluraModels, MolecularPeptide MappingPlant ProteinsProtein ConformationSeedsSequence Homology, Amino AcidTrypsinTrypsin Inhibitor, Bowman-Birk SoybeanTrypsin InhibitorsPlant ProteinsTrypsinTrypsin Inhibitor, Bowman-Birk SoybeanTrypsin InhibitorsBBI-type protease inhibitorCloningHomology modelingLoopThree-dimensional structureTrypsin inhibition

Identifiers

PMID27778107
OpenAlexW2538721134

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.