Evidence map›Paper›PMID 12226497›Full record

ArticlePlant physiology2002

Isolation and characterization of a novel ribosome-inactivating protein from root cultures of pokeweed and its mechanism of secretion from roots.

Sang-Wook Park, Christopher B Lawrence, James C Linden, Jorge M Vivanco

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Frontiers in plant science · 2019
    Article
  3. Purification of a ribosome-inactivating protein with antioxidation and root developer potencies fromPhysiology and molecular biology of plants : an international journal of functional plant biology · 2019
    Article
  4. Toxic proteins in plants.Phytochemistry · 2015
    Review
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  8. Article
  9. Targeting an antimicrobial effector function in insect immunity as a pest control strategy.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
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  11. 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

4 authors at 2 institutions in 2 countries.

Sang-Wook ParkDepartment of Horticulture and Landscape Architecture, Colorado State University, Fort Collins, Colorado 80523-1173, USA.
Christopher B Lawrence
James C Linden
Jorge M Vivanco
Landscape Institute · GBMicrobiology Society · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosome-inactivating proteins are N-glycosidases that remove a specific adenine from the sarcin/ricin loop of the large rRNA, thus arresting protein synthesis at the translocation step. In the present study, a novel type I ribosome-inactivating protein, termed PAP-H, was purified from Agrobacterium rhizogenes-transformed hairy roots of pokeweed (Phytolacca americana). The protein was purified by anion- and cation-exchange chromatography. PAP-H has a molecular mass of 29.5 kD as detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its isoelectric point was determined to be 7.8. Yeast (Saccharomyces cerevisiae) ribosomes incubated with PAP-H released the 360-nucleotide diagnostic fragment from the 26S rRNA upon aniline treatment, an indication of its ribosome-inactivating activity. Using immunofluorescence microscopy, PAP-H was found to be located in the cell walls of hairy roots and root border cells. PAP-H was determined to be constitutively secreted as part of the root exudates, with its secretion enhanced by a mechanism mediated by ethylene induction. Purified PAP-H did not show in vitro antifungal activity against soil-borne fungi. In contrast, root exudates containing PAP-H as well as additional chitinase, beta-1,3-glucanase, and protease activities did inhibit the growth of soil-borne fungi. We found that PAP-H depurinates fungal ribosomes in vitro and in vivo, suggesting an additive mechanism that enables PAP-H to penetrate fungal cells.

Indexed as

Amino Acid SequenceAntifungal AgentsBase Sequencebeta-GlucosidaseCells, CulturedCell Surface ExtensionsCell WallChitinasesCloning, MolecularDNA, ComplementaryEndopeptidasesEthylenesGlucan 1,3-beta-GlucosidaseMicroscopyMolecular Sequence DataPancreatitis-Associated ProteinsAntifungal Agentsbeta-GlucosidaseChitinasesDNA, ComplementaryEndopeptidasesethyleneEthylenesGlucan 1,3-beta-GlucosidasePancreatitis-Associated ProteinsPlant ProteinsREG3A protein, human

Identifiers

PMID12226497
PMCPMC166550
OpenAlexW2064380866

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.