Evidence map›Paper›PMID 16258848›Full record

ArticleNeurochemical research2005

Glutamate decarboxylase: loss of N-terminal segment does not affect homodimerization and determination of the oxidation state of cysteine residues.

Gino Battaglioli, Hongcheng Liu, Charles R Hauer, David L Martin

Abstract read
PubMed Publisher
In one paragraph

Article in Neurochemical research, 2005. 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
0.8field-weighted citation impact, top 35% 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, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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

4 authors at 2 institutions in 1 country.

Gino BattaglioliNew State Department of Health, Wadsworth Center, PO Box 509, Albany, New York 12201, USA. battagli@wadsworth.org
Hongcheng Liu
Charles R Hauer
David L Martin
Albany State University · USUnited States Department of State · US

Funding

CONTROL OF GAMMA-AMINOBUTYRIC ACID SYNTHESISR01MH035664 · NIMH · WADSWORTH CENTER · PI MARTIN, DAVID L · 1985 to 1988
–
CONTROL OF GAMMA-AMINOBUTYRIC ACID SYNTHESISR37MH035664 · NIMH · WADSWORTH CENTER · PI MARTIN, DAVID L · 1989 to 1998
–
NIMH NIH HHS MH 35664NINDS NIH HHS NS38413
6 · The paper itself

Abstract

Glutamate decarboxylase (GAD) produces GABA, the main inhibitory neurotransmitter in adult mammalian brain. The physical characteristics of GAD were studied using mass spectrometry and partial protein digests. The N-termini of the two main isoforms, GAD65 and GAD67, were processed by removal of the initial methionine residues and acetylation of the penultimate alanines. Native recombinant GAD65 and GAD67 exist as homodimers that can be dissociated with non-reducing methods, indicating that homodimerization does not involve intermolecular disulfide bonds. Truncation of the N-terminal segment with trypsin digestion did not affect homodimerization but increased activity by decreasing the Km of GAD67 and increasing the Vmax of both isoforms. Of the 15 cysteines in GAD65, the six found in the N-terminal segment can form disulfide bonds and of the 13 cysteines in GAD67, cysteines 32 and 38 can form a disulfide bond. The in vitro formation of disulfide bonds in the N-termini, and the removal of the termini with relatively low amounts of trypsin, indicate that the N-terminal segments of GAD65 and GAD67 are exposed and flexible. The formation of a disulfide bridge between cysteines 30 and 45 of GAD65 suggests that alteration of normal redox conditions could affect GAD targeting.

Indexed as

Amino Acid SequenceAnimalsCysteineDimerizationDisulfidesElectrophoresis, Polyacrylamide GelGlutamate DecarboxylaseIsoenzymesKineticsMolecular Sequence DataMolecular WeightOxidation-ReductionProtein ConformationProtein DenaturationRatsRecombinant ProteinsCysteineDisulfidesGlutamate Decarboxylaseglutamate decarboxylase 1glutamate decarboxylase 2IsoenzymesRecombinant Proteins

Identifiers

PMID16258848
OpenAlexW2041821988

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.