Evidence map›Paper›PMID 30850498›Full record

ArticleJournal of nuclear medicine : official publication, Society of Nuclear Medicine2019

Riikka Siitonen, Emilia Peuhu, Anu Autio, Heidi Liljenbäck, Elina Mattila, Olli Metsälä, Meeri Käkelä, Tiina Saanijoki, Ingrid Dijkgraaf, Sirpa Jalkanen and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of nuclear medicine : official publication, Society of Nuclear Medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. The role and regulation of integrins in cell migration and invasion.Nature reviews. Molecular cell biology · 2025
    Review
  2. Review
  3. Review
  4. [Frontiers in immunology · 2022
    Article
  5. Review
  6. Review
  7. Evaluation of [Frontiers in medicine · 2021
    Article
  8. 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

12 authors at 5 institutions in 2 countries.

Riikka SiitonenTurku PET Centre, University of Turku, Turku, Finland.
Emilia PeuhuTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland.
Anu AutioTurku PET Centre, University of Turku, Turku, Finland.
Heidi LiljenbäckTurku PET Centre, University of Turku, Turku, Finland.
Elina MattilaTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland.
Olli MetsäläTurku PET Centre, University of Turku, Turku, Finland.
Meeri KäkeläTurku PET Centre, University of Turku, Turku, Finland.
Tiina SaanijokiTurku PET Centre, University of Turku, Turku, Finland.
Ingrid DijkgraafDepartment of Biochemistry, University of Maastricht, Maastricht, the Netherlands.
Sirpa JalkanenMediCity Research Laboratory, University of Turku, Turku, Finland.
Johanna IvaskaTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland.
Anne RoivainenTurku PET Centre, University of Turku, Turku, Finland anne.roivainen@utu.fi.
Turku PET Centre · FIUniversity of Turku · FITurku Centre for Biotechnology · FIÅbo Akademi University · FIMaastricht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Shank-associated RH domain-interacting protein (SHARPIN) is a cytosolic protein that plays a key role in activation of nuclear factor κ-light-chain enhancer of activated B cells and regulation of inflammation. Furthermore, SHARPIN controls integrin-dependent cell adhesion and migration in several normal and malignant cell types, and loss of SHARPIN correlates with increased integrin activity in mice. Arginyl-glycyl-aspartic acid (RGD), a cell adhesion tripeptide motif, is an integrin recognition sequence that facilitates PET imaging of integrin upregulation during tumor angiogenesis. We hypothesized that increased integrin activity due to loss of SHARPIN protein would affect the uptake of α

Indexed as

Amino Acid MotifsAnimalsCell AdhesionCell MovementCoordination ComplexesDermatitisFemaleImmunohistochemistryInflammationIntegrin alphaVbeta3Intracellular Signaling Peptides and ProteinsMaleMelanomaMelanoma, ExperimentalMiceMice, Inbred C57BL68Ga-DOTA-E-(c(RGDfK))2Coordination Complexescyclic arginine-glycine-aspartic acid peptideIntegrin alphaVbeta3Intracellular Signaling Peptides and ProteinsPeptides, CyclicSipl1 protein, mousemelanomaPETRGDSHARPINαvβ3 integrin

Identifiers

PMID30850498
PMCPMC6785786
OpenAlexW2921409025

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.