Evidence map›Paper›PMID 31814256›Full record

ArticleChembiochem : a European journal of chemical biology2020

A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes.

Łukasz Syga, Reinder H de Vries, Hugo van Oosterhout, Rianne Bartelds, Arnold J Boersma, Gerard Roelfes, Bert Poolman

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 51% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

7 authors at 2 institutions in 2 countries.

Łukasz SygaDepartment of Biochemistry, Groningen Biomolecular Sciences and, Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
Reinder H de VriesDepartment of Biomolecular Chemistry and Catalysis, Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
Hugo van OosterhoutDepartment of Biomolecular Chemistry and Catalysis, Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
Rianne BarteldsDepartment of Biochemistry, Groningen Biomolecular Sciences and, Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
Arnold J BoersmaDWI Leibniz Institute for Interactive Materials, Forckenbeckstrasse 50, 52074, Aachen, Germany.
Gerard RoelfesDepartment of Biomolecular Chemistry and Catalysis, Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
Bert PoolmanDepartment of Biochemistry, Groningen Biomolecular Sciences and, Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.ORCID 0000-0002-1455-531X
University of Groningen · NLDWI – Leibniz Institute for Interactive Materials · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Attachment of lipophilic groups is an important post-translational modification of proteins, which involves the coupling of one or more anchors such as fatty acids, isoprenoids, phospholipids, or glycosylphosphatidyl inositols. To study its impact on the membrane partitioning of hydrophobic peptides or proteins, we designed a tyrosine-based trifunctional linker. The linker allows the facile incorporation of two different functionalities at a cysteine residue in a single step. We determined the effect of the lipid modification on the membrane partitioning of the synthetic α-helical model peptide WALP with or without here and in all cases below; palmitoyl groups in giant unilamellar vesicles that contain a liquid-ordered (L

Indexed as

Cell MembraneHumansLipid BilayersLipoylationMembrane MicrodomainsPalmitic AcidPeptide FragmentsProtein Processing, Post-TranslationalProteinsTyrosineUnilamellar LiposomesLipid BilayersPalmitic AcidPeptide FragmentsProteinsTyrosineUnilamellar Liposomesbiological membraneslipid phase separationmembrane partitioningpalmitoylationtrifunctional linker

Identifiers

PMID31814256
PMCPMC7317724
OpenAlexW2993304937

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.