The NMR structure of the NIPP1 FHA domain.

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.

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.

Who cites it

4 citing papers in PubMed.

1. A substrate-trapping strategy for protein phosphatase PP1 holoenzymes using hypoactive subunit fusions.The Journal of biological chemistry · 2018
   Article
2. NIPP1 maintains EZH2 phosphorylation and promoter occupancy at proliferation-related target genes.Nucleic acids research · 2013
   Article
3. Structure and interactions of the cytoplasmic domain of the Yersinia type III secretion protein YscD.Journal of bacteriology · 2012
   Article
4. The molecular basis for substrate specificity of the nuclear NIPP1:PP1 holoenzyme.Structure (London, England : 1993) · 2012
   Article

Corrections and comments

• Erratum issued
  Tanuma, Kiminobu [corrected to Tanuma, Nobuhiro]

Authors and funding

8 authors.

Funding

No grant is acknowledged in the PubMed record.

Abstract

PubMed holds no abstract for this paper.

Indexed as