Evidence map›Paper›PMID 27283494›Full record

ArticleBiophysical journal2016

Evidence for Surface Recognition by a Cholesterol-Recognition Peptide.

Masaru Mukai, Kerney Jebrell Glover, Steven L Regen

Abstract readLetter
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Analysis of cholesterol-recognition motifs of the plasma membrane CaJournal of bioenergetics and biomembranes · 2024
    Article
  2. Article
  3. Physics of HIV.Journal of physics D: Applied physics · 2018
    Article
  4. 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

3 authors.

Masaru MukaiDepartment of Chemistry, Lehigh University, Bethlehem, Pennsylvania.
Kerney Jebrell GloverDepartment of Chemistry, Lehigh University, Bethlehem, Pennsylvania.
Steven L RegenDepartment of Chemistry, Lehigh University, Bethlehem, Pennsylvania. Electronic address: slr0@lehigh.edu.

Funding

Investigation of Caveolin Structure, Topology, and OligomerizationR01GM093258 · NIGMS · LEHIGH UNIVERSITY · PI GLOVER, KERNEY JEBRELL · 2012 to 2016
$1.7M
NIGMS NIH HHS R01 GM093258
6 · The paper itself

Abstract

Two cholesterol recognition/interaction amino-acid consensus peptides, N-acetyl-LWYIKC-amide, and N-acetyl-CLWYIK-amide, have been coupled to exchangeable mimics of Chol (cholesterol) and Phos (1,2-dipalmitoyl-sn-glycerol-3-phospho-(1'rac-glycerol)) via disulfide bond formation. Equilibration between Chol and Phos via thiolate-disulfide interchange reactions has revealed that both peptides favor Chol as a nearest-neighbor in liquid-disordered (ld) bilayers to the same extent. In contrast, no Chol- or Phos-recognition could be detected by these peptides in analogous liquid-ordered (lo) bilayers. Fluorescence measurements of the tryptophan moiety have shown that both peptides favor the membrane-water interface. Taken together, these results provide strong evidence that the recognition behavior of the LWYIK motif is, fundamentally, a surface phenomenon but that partial penetration into the bilayer is also necessary.

Indexed as

CholesterolLipid BilayersLiposomesMolecular StructurePeptidesPhosphatidylglycerolsProtein MultimerizationSurface PropertiesWater1,2-dipalmitoylphosphatidylglycerolCholesterolLipid BilayersLiposomesPeptidesPhosphatidylglycerolsWater

Identifiers

PMID27283494
PMCPMC4919587

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.