Evidence map›Paper›PMID 9004547›Full record

ArticlePlanta1996

Processing in vitro of pronapin, the 2S storage-protein precursor of Brassica napus produced in a baculovirus expression system.

E Murén, L Rask

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

5 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Deposition of storage proteins.Plant molecular biology · 1998
    Review
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.

E MurénUppsala Genetic Center, Department of Cell Research, Swedish University of Agricultural Sciences, Sweden. eva.muren@cellfo.slu.se
L Rask
Swedish University of Agricultural Sciences · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The maturation of the 2S albumin, napin, in Brassica napus L. involves removal of an amino-terminal and an internal propeptide. Pulse-chase experiments with B. napus embryos showed that intermediates are detectable during the pronapin processing. Intact pronapin was expressed by baculovirus in Spodoptera frugiperda insect cells in order to obtain substrate for studying the processing event. Processing of pronapin with a crude B. napus embryo protein extract resulted in several fragments of similar sizes to those of napin heavy and light chains. The character of the major processing activity in the B. napus extract suggested that it was due to an aspartic proteinase. A secondary activity indicated an additional endoproteinase involved in the pronapin processing. Limited proteolysis of pronapin with a purified aspartic proteinase from Hordeum vulgare showed that cleavage occurred exclusively in the prosequences. The cleavage products formed in-vitro requires additional trimming of the propeptides in order to obtain the subunits of mature napin.

Indexed as

Protein Processing, Post-Translational2S Albumins, PlantAmino Acid SequenceAnimalsBaculoviridaeBrassicaCell LineGenetic VectorsMolecular Sequence DataPlant ExtractsPlant ProteinsProtein PrecursorsRecombinant Fusion ProteinsSpodoptera2S Albumins, Plantnapin protein, Brassica napusPlant ExtractsPlant ProteinsProtein PrecursorsRecombinant Fusion Proteins

Identifiers

PMID9004547
OpenAlexW2090035800

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.