Evidence map›Paper›PMID 12176927›Full record

ArticleGenome research2002

B-ZIP proteins encoded by the Drosophila genome: evaluation of potential dimerization partners.

Jan Fassler, David Landsman, Asha Acharya, Jonathan R Moll, Maria Bonovich, Charles Vinson

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Genome research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
–field-weighted citation impact
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

48 citing papers in PubMed, 77 citations in OpenAlex.

  1. Developmentally-regulated post-apocrine cell death ofFrontiers in cell and developmental biology · 2026
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  12. Genome-Wide Identification ofInternational journal of genomics · 2017
    Article
  13. Drosophila IRBP bZIP heterodimer binds P-element DNA and affects hybrid dysgenesis.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Stress-MediatedFrontiers in plant science · 2016
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Jan FasslerComputational Biology Branch, National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20814, USA.
David Landsman
Asha Acharya
Jonathan R Moll
Maria Bonovich
Charles Vinson
University of Iowa · US

Funding

Structural And Functional Analysis Of Protein Sequence FamiliesZIALM000071 · NLM · NATIONAL LIBRARY OF MEDICINE · PI LANDSMAN, DAVID · 2009 to 2025
$3.7M
Structural-Functional Analysis-Protein Sequence FamiliesZ01LM000071 · NLM · NATIONAL LIBRARY OF MEDICINE · PI LANDSMAN, DAVID · 1995 to 2008
$140k
6 · The paper itself

Abstract

The basic region-leucine zipper (B-ZIP) (bZIP) protein motif dimerizes to bind specific DNA sequences. We have identified 27 B-ZIP proteins in the recently sequenced Drosophila melanogaster genome. The dimerization specificity of these 27 B-ZIP proteins was evaluated using two structural criteria: (1) the presence of attractive or repulsive interhelical g<-->e' electrostatic interactions and (2) the presence of polar or charged amino acids in the 'a' and 'd' positions of the hydrophobic interface. None of the B-ZIP proteins contain only aliphatic amino acids in the'a' and 'd' position. Only six of the Drosophila B-ZIP proteins contain a "canonical" hydrophobic interface like the yeast GCN4, and the mammalian JUN, ATF2, CREB, C/EBP, and PAR leucine zippers, characterized by asparagine in the second 'a' position. Twelve leucine zippers contain polar amino acids in the first, third, and fourth 'a' positions. Circular dichroism spectroscopy, used to monitor thermal denaturations of a heterodimerizing leucine zipper system containing either valine (V) or asparagine (N) in the 'a' position, indicates that the V-N interaction is 2.3 kcal/mole less stable than an N-N interaction and 5.3 kcal/mole less stable than a V-V interaction. Thus, we propose that the presence of polar amino acids in novel positions of the 'a' position of Drosophila B-ZIP proteins has led to leucine zippers that homodimerize rather than heterodimerize.

Indexed as

GenomeNuclear ProteinsRNA-Binding ProteinsAmino AcidsAmino Acid SequenceAnimalsAsparagineDatabases, ProteinDimerizationDNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsGenes, InsectHumansLeucine ZippersMolecular Sequence DataALYREF protein, humanAmino AcidsAsparagineDNA-Binding ProteinsDrosophila ProteinsNuclear ProteinsRNA-Binding ProteinsTranscription FactorsValine

Identifiers

PMID12176927
PMCPMC186634
OpenAlexW2129567429

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.