Evidence map›Paper›PMID 9495318›Full record

ArticleGene expression1997

C/EBP proteins contain nuclear localization signals imbedded in their basic regions.

S C Williams, N D Angerer, P F Johnson

Abstract read
In one paragraph

Article in Gene expression, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.6field-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

23 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. C/EBPα in normal and malignant myelopoiesis.International journal of hematology · 2015
    Review
  8. Article
  9. Ubiquitin tagged dominant negative induces degradation of B-ZIP proteins.Biochemical and biophysical research communications · 2012
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Dominant-negative C/EBP disrupts mitotic clonal expansion and differentiation of 3T3-L1 preadipocytes.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  18. Article
  19. Interaction of HCF-1 with a cellular nuclear export factor.The Journal of biological chemistry · 2002
    Article
  20. 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

3 authors at 1 institution in 1 country.

S C WilliamsDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock 79430, USA.
N D Angerer
P F Johnson
Texas Tech University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The C/EBP-related proteins (C/EBPalpha, CRP1, C/EBPbeta, and C/EBPdelta) form a subfamily of bZIP (basic region/leucine zipper) transcription factors that display sequence homology within the bZIP domain. The conserved basic region contains two motifs that exhibit significant homology to the bipartite nuclear localization signal (NLS) first described in nucleoplasmin. CRP1 and C/EBPbeta proteins bearing deletions of the basic region accumulate in the cytoplasm, in contrast to their normal nuclear location. Analysis of chimeric proteins consisting of CRP1 basic region sequences fused to beta-galactosidase revealed that the CRP1 basic region contains a single NLS that differs from conventional bipartite signals in two ways. First, mutation of a pair of arginine residues at the N-terminus of the proposed NLS does not disrupt its function. Second, the CRP1 NLS requires additional nonbasic residues at its C-terminus. A basic residue within the CRP1 NLS that is not conserved within the C/EBP family is occupied instead by an uncharged residue in C/EBPalpha and C/EBPbeta. When this nonconserved arginine residue was changed to alanine the CRP1 NLS behaved as a classical bipartite signal, suggesting that bipartite NLSs are present in all family members but that NLSs of the individual members differ slightly. Additionally, mutation of critical NLS residues in the intact CRP1 and C/EBPbeta proteins showed that these elements exhibit more bipartite-like characteristics when present in their normal sequence context. Finally, we observed that a C/EBPbeta protein lacking its NLS can be localized to the nucleus when coexpressed with C/EBPalpha, indicating that a single NLS is sufficient to promote nuclear transport of a bZIP dimer.

Indexed as

Amino Acid SequenceArginineCCAAT-Enhancer-Binding ProteinsCell NucleusCytoplasmDNA-Binding ProteinsHeLa CellsHumansLysineMolecular Sequence DataMutationNuclear Localization SignalsNuclear ProteinsRecombinant Fusion ProteinsSequence DeletionSequence Homology, Amino AcidArginineCCAAT-Enhancer-Binding ProteinsCEBPE protein, humanDNA-Binding ProteinsLysineNuclear Localization SignalsNuclear ProteinsRecombinant Fusion ProteinsTranscription Factors

Identifiers

PMID9495318
PMCPMC6148256
OpenAlexW131517112

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.