Evidence map›Paper›PMID 36372231›Full record

ArticleThe Journal of biological chemistry2022

Role of the membrane anchor in the regulation of Lck activity.

Nicla Porciello, Deborah Cipria, Giulia Masi, Anna-Lisa Lanz, Edoardo Milanetti, Alessandro Grottesi, Duncan Howie, Steve P Cobbold, Lothar Schermelleh, Hai-Tao He and 4 more

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. T-cell virtuosity in ''knowing thyself".Frontiers in immunology · 2024
    Review
  6. 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

14 authors at 6 institutions in 4 countries.

Nicla PorcielloT Cell Signalling Laboratory, Sir William Dunn School of Pathology, Oxford University, Oxford, United Kingdom.
Deborah CipriaT Cell Signalling Laboratory, Sir William Dunn School of Pathology, Oxford University, Oxford, United Kingdom.
Giulia MasiT Cell Signalling Laboratory, Sir William Dunn School of Pathology, Oxford University, Oxford, United Kingdom.
Anna-Lisa LanzT Cell Signalling Laboratory, Sir William Dunn School of Pathology, Oxford University, Oxford, United Kingdom.
Edoardo MilanettiDepartment of Physics, University of Rome "La Sapienza", Rome, Italy.
Alessandro GrottesiCINECA - Italian Computing Centre (ICC), Rome, Italy.
Duncan HowieSir William Dunn School of Pathology, Oxford University, Oxford, United Kingdom.
Steve P CobboldSir William Dunn School of Pathology, Oxford University, Oxford, United Kingdom.
Lothar SchermellehMicron Advanced Bioimaging Unit, Department of Biochemistry, Oxford University, Oxford, United Kingdom.
Hai-Tao HeAix Marseille Université, CNRS, INSERM, CINL, Marseille, France.
Marco D'AbramoDepartment of Chemistry, University of Rome "La Sapienza", Rome, Italy.
Nicolas DestainvilleLaboratoire de Physique Théorique, Université Paul Sabatier, CNRS, UPS, Toulouse, France. Electronic address: destain@irsamc.ups-tlse.fr.
Oreste AcutoT Cell Signalling Laboratory, Sir William Dunn School of Pathology, Oxford University, Oxford, United Kingdom. Electronic address: oreste.acuto@path.ox.ac.uk.
Konstantina NikaT Cell Signalling Laboratory, Sir William Dunn School of Pathology, Oxford University, Oxford, United Kingdom; Department of Biochemistry, School of Medicine, University of Patras, Patras, Greece. Electronic address: knika@upatras.gr.
University of Oxford · GBCentre National de la Recherche Scientifique · FRBusiness Innovation Centre · ITSapienza University of Rome · ITUniversity of Patras · GRUniversity of Rome Tor Vergata · IT

Funding

Wellcome Trust 091911Wellcome Trust 107457Wellcome Trust 200844/Z/16/ZWellcome Trust GR076558MAWellcome Trust WT094296MA
6 · The paper itself

Abstract

Theoretical work suggests that collective spatiotemporal behavior of integral membrane proteins should be modulated by boundary lipids sheathing their membrane anchors. Here, we show evidence for this prediction while investigating the mechanism for maintaining a steady amount of the active form of integral membrane protein Lck kinase (Lck

Indexed as

Lymphocyte Specific Protein Tyrosine Kinase p56(lck)Protein Processing, Post-TranslationalLeukocyte Common AntigensLipid BilayersPhosphorylationProtein DomainsLeukocyte Common AntigensLipid BilayersLymphocyte Specific Protein Tyrosine Kinase p56(lck)boundary lipidsCD45Lckmembrane anchormembrane lateral organization

Identifiers

PMID36372231
PMCPMC9763865
OpenAlexW4308793356

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.