Evidence map›Paper›PMID 22039217›Full record

ArticlePlant physiology2012

Mapping, complementation, and targets of the cysteine protease actinidin in kiwifruit.

Niels J Nieuwenhuizen, Ratnasiri Maddumage, Gianna K Tsang, Lena G Fraser, Janine M Cooney, H Nihal De Silva, Sol Green, Kim A Richardson, Ross G Atkinson

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.4field-weighted citation impact, top 9% 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

11 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Cysteine Peptidases ofCurrent protein & peptide science · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Effects of topical Kiwifruit on healing of neuropathic diabetic foot ulcer.Journal of research in medical sciences : the official journal of Isfahan University of Medical Sciences · 2014
    Article
  11. 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

9 authors at 1 institution in 1 country.

Niels J NieuwenhuizenNew Zealand Institute for Plant and Food Research Limited, Mount Albert Research Centre, Auckland 1142, New Zealand.
Ratnasiri Maddumage
Gianna K Tsang
Lena G Fraser
Janine M Cooney
H Nihal De Silva
Sol Green
Kim A Richardson
Ross G Atkinson
Plant & Food Research · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cysteine proteases (CPs) accumulate to high concentration in many fruit, where they are believed to play a role in fungal and insect defense. The fruit of Actinidia species (kiwifruit) exhibit a range of CP activities (e.g. the Actinidia chinensis variety YellowA shows less than 2% of the activity of Actinidia deliciosa variety Hayward). A major quantitative trait locus for CP activity was mapped to linkage group 16 in a segregating population of A. chinensis. This quantitative trait locus colocated with the gene encoding actinidin, the major acidic CP in ripe Hayward fruit encoded by the ACT1A-1 allele. Sequence analysis indicated that the ACT1A locus in the segregating A. chinensis population contained one functional allele (A-2) and three nonfunctional alleles (a-3, a-4, and a-5) each containing a unique frameshift mutation. YellowA kiwifruit contained two further alleles: a-6, which was nonfunctional because of a large insertion, and a-7, which produced an inactive enzyme. Site-directed mutagenesis of the act1a-7 protein revealed a residue that restored CP activity. Expression of the functional ACT1A-1 cDNA in transgenic plants complemented the natural YellowA mutations and partially restored CP activity in fruit. Two consequences of the increase in CP activity were enhanced degradation of gelatin-based jellies in vitro and an increase in the processing of a class IV chitinase in planta. These results provide new insight into key residues required for CP activity and the in vivo protein targets of actinidin.

Indexed as

ActinidiaAllelesChitinasesChromosome MappingCysteine EndopeptidasesDNA, ComplementaryFrameshift MutationGelatinGenetic Complementation TestMolecular Sequence DataMutagenesis, Site-DirectedPlant ProteinsPlants, Genetically ModifiedQuantitative Trait LociSequence Analysis, DNAactinidainChitinasesCysteine EndopeptidasesDNA, ComplementaryGelatinPlant Proteins

Identifiers

PMID22039217
PMCPMC3252086
OpenAlexW2061206290

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.