Evidence map›Paper›PMID 9223293›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Nuclear localization of basonuclin in human keratinocytes and the role of phosphorylation.

S Iuchi, H Green

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. 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
0.9field-weighted citation impact, top 28% 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, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Basonuclins 1 and 2, whose genes share a common origin, are proteins with widely different properties and functions.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  7. Review
  8. Basonuclin 2: an extremely conserved homolog of the zinc finger protein basonuclin.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  9. Marker succession during the development of keratinocytes from cultured human embryonic stem cells.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  10. Article
  11. Basonuclin, a zinc finger protein of keratinocytes and reproductive germ cells, binds to the rRNA gene promoter.Proceedings of the National Academy of Sciences of the United States of America · 1999
    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

2 authors at 1 institution in 1 country.

S IuchiDepartment of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston MA 02115, USA.
H Green
Harvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Basonuclin is a zinc-finger protein found in basal cells of the epidermis. In human keratinocyte cultures, basonuclin is susceptible to serine-phosphorylation and the addition of the phosphatase inhibitor, okadaic acid, promotes accumulation of basonuclin in the cytoplasm. The region of basonuclin containing the nuclear localization signal of basonuclin is necessary for nuclear localization of the protein and Ser-541, located immediately C-terminal to the nuclear localization signal, is the principal phosphorylation site in vitro. A nearly complete basonuclin transiently expressed in cultured keratinocytes localizes predominantly in the nucleus, but substitution of aspartic acid for Ser-541 promotes cytoplasmic localization. The same substitution of Ser-537 has a similar but weaker effect. Substitution of both serine residues by alanine leads to nuclear localization. These results show that nuclear localization of basonuclin depends on serine dephosphorylation, primarily of Ser-541. Different subcellular locations of basonuclin in different keratinocyte subtypes are therefore most likely to be controlled by the state of phosphorylation of Ser-541.

Indexed as

3T3 CellsAnimalsCell NucleusCytoplasmDNA-Binding ProteinsHumansKeratinocytesMiceMutagenesisPhosphoproteinsPhosphorylationProtein Processing, Post-TranslationalProteinsSerineSubcellular FractionsTranscription FactorsBNC1 protein, humanBnc1 protein, mouseDNA-Binding ProteinsPhosphoproteinsProteinsSerineTranscription Factors

Identifiers

PMID9223293
PMCPMC21535
OpenAlexW2012302802

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.