Evidence map›Paper›PMID 39858499›Full record

ArticleBiomolecules2025

Functional Characterization of the SHIP1-Domains Regarding Their Contribution to Inositol 5-Phosphatase Activity.

Spike Murphy Müller, Nina Nelson, Manfred Jücker

Abstract read
In one paragraph

Article in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Genome-Wide Identification of theInternational journal of molecular sciences · 2026
    Article
  6. Article
  7. Review
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.

Spike Murphy MüllerInstitute of Biochemistry and Signal Transduction, University Medical Center Hamburg-Eppendorf, 20246 Hamburg, Germany.ORCID 0009-0003-3561-7991
Nina NelsonInstitute of Biochemistry and Signal Transduction, University Medical Center Hamburg-Eppendorf, 20246 Hamburg, Germany.ORCID 0000-0002-7551-030X
Manfred JückerInstitute of Biochemistry and Signal Transduction, University Medical Center Hamburg-Eppendorf, 20246 Hamburg, Germany.ORCID 0000-0003-2176-6526

Funding

Erich Und Gertrud Roggenbuck Stiftung 0424/109
6 · The paper itself

Abstract

The Src homology 2 domain-containing inositol 5-phosphatase 1 (SHIP1) is a multidomain protein consisting of two protein-protein interaction domains, the Src homology 2 (SH2) domain, and the proline-rich region (PRR), as well as three phosphoinositide-binding domains, the pleckstrin homology-like (PHL) domain, the 5-phosphatase (5PPase) domain, and the C2 domain. SHIP1 is commonly known for its involvement in the regulation of the PI3K/AKT signaling pathway by dephosphorylation of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P

Indexed as

Phosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesHumansInositol Polyphosphate 5-PhosphatasesPhosphatidylinositol PhosphatesProtein Domainssrc Homology DomainsInositol Polyphosphate 5-PhosphatasesINPP5D protein, humanINPPL1 protein, humanPhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphatidylinositol PhosphatesAKT (=PKB)allosteric regulationcloningenzyme catalysisenzyme kineticsenzyme regulationphosphatase activityphosphatidylinositide 3-kinase (PI 3-kinase)phosphatidylinositol phosphatasePI3K/AKT signaling pathwaypolymerase chain reaction (PCR)protein expressionSHIP1Western blot

Identifiers

PMID39858499
PMCPMC11763786

What Socratic holds

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LicenceCC BY
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 Socratic graph.