Evidence map›Paper›PMID 11161058›Full record

ArticlePlant physiology2001

Distinct patterns of expression but similar biochemical properties of protein L-isoaspartyl methyltransferase in higher plants.

N Thapar, A K Kim, S Clarke

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2001. 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
2.9field-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

16 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. The Journal of biological chemistry · 2020
    Article
  4. Article
  5. Article
  6. Article
  7. Enzymatic attributes of an l-isoaspartyl methyltransferase fromBiochemistry and biophysics reports · 2015
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

3 authors at 1 institution in 1 country.

N ThaparDepartment of Chemistry and Biochemistry and the Molecular Biology Institute, Paul D. Boyer Hall, University of California, Los Angeles, California 90095-1569, USA.
A K Kim
S Clarke
University of California, Los Angeles · US

Funding

CONTROL OF EUCARYOTIC FUNCTION BY METHYLATIONR37GM026020 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CLARKE, STEVEN G · 2000 to 2009
$5.0M
CONTROL OF EUKARYOTIC MEMBRANE FUNCTION BY METHYLATIONR01GM026020 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CLARKE, STEVEN G · 1985 to 2013
$2.1M
ENYZMES AFFECTING THE ACCUMULATION OF ALTERED PROTEINSR01AG018000 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CLARKE, STEVEN G · 2000 to 2003
$904k
NIA NIH HHS AG18000NIA NIH HHS R01 AG018000NIGMS NIH HHS GM260NIGMS NIH HHS R01 GM026020NIGMS NIH HHS R37 GM026020
6 · The paper itself

Abstract

Protein L-isoaspartyl methyltransferase is a widely distributed repair enzyme that initiates the conversion of abnormal L-isoaspartyl residues to their normal L-aspartyl forms. Here we show that this activity is expressed in developing corn (Zea mays) and carrot (Daucus carota var. Danvers Half Long) plants in patterns distinct from those previously seen in winter wheat (Triticum aestivum cv Augusta) and thale cress (Arabidopsis thaliana), whereas the pattern of expression observed in rice (Oryza sativa) is similar to that of winter wheat. Although high levels of activity are found in the seeds of all of these plants, relatively high levels of activity in vegetative tissues are only found in corn and carrot. The activity in leaves was found to decrease with aging, an unexpected finding given the postulated role of this enzyme in repairing age-damaged proteins. In contrast with the situation in wheat and Arabidopsis, we found that osmotic or salt stress could increase the methyltransferase activity in newly germinated seeds (but not in seeds or seedlings), whereas abscisic acid had no effect. We found that the corn, rice, and carrot enzymes have comparable affinity for methyl-accepting substrates and similar optimal temperatures for activity of 45 degrees C to 55 degrees C as the wheat and Arabidopsis enzymes. These experiments suggest that this enzyme may have specific roles in different plant tissues despite a common catalytic function.

Indexed as

Daucus carotaGene Expression Regulation, EnzymologicGene Expression Regulation, PlantKineticsOryzaProtein D-Aspartate-L-Isoaspartate MethyltransferaseSeedsTriticumZea maysProtein D-Aspartate-L-Isoaspartate Methyltransferase

Identifiers

PMID11161058
PMCPMC64902
OpenAlexW2005593212

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.