Evidence map›Paper›PMID 10631247›Full record

ArticlePlant physiology2000

Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis.

U Klahre, E Friederich, B Kost, D Louvard, N H Chua

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
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  9. Molecular and Functional Characterization ofFrontiers in plant science · 2020
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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

5 authors at 1 institution in 1 country.

U KlahreLaboratory of Plant Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, New York 10021, USA.
E Friederich
B Kost
D Louvard
N H Chua
Rockefeller University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In an attempt to elucidate the biological function of villin-like actin-binding proteins in plants we have cloned several genes encoding Arabidopsis proteins with high homology to animal villin. We found that Arabidopsis contains at least four villin-like genes (AtVLNs) encoding four different VLN isoforms. Two AtVLN isoforms are more closely related to mammalian villin in their primary structure and are also antigenically related, whereas the other two contain significant changes in the C-terminal headpiece domain. RNA and promoter/beta-glucuronidase expression studies demonstrated that AtVLN genes are expressed in all organs, with elevated expression levels in certain types of cells. These results suggest that AtVLNs have less-specialized functions than mammalian villin, which is found only in the microvilli of brush border cells. Immunoblot experiments using a monoclonal antibody against pig villin showed that AtVLNs are widely distributed in a variety of plant tissues. Green fluorescent protein fused to full-length AtVLN and individual AtVLN headpiece domains can bind to both animal and plant actin filaments in vivo.

Indexed as

Amino Acid SequenceAnimalsArabidopsisCarrier ProteinsChlorocebus aethiopsMicrofilament ProteinsMicroscopy, ConfocalMolecular Sequence DataNicotianaPlant ProteinsPlants, ToxicSequence Homology, Amino AcidVero CellsCarrier ProteinsMicrofilament ProteinsPlant Proteinsvillin

Identifiers

PMID10631247
PMCPMC58842
OpenAlexW2090287625

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.