Evidence map›Paper›PMID 28554774›Full record

ReviewBiochimica et biophysica acta. Molecular cell research2017

Tubular lipid binding proteins (TULIPs) growing everywhere.

Louise H Wong, Tim P Levine

Open access · hybridAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular cell research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. LYVAC/PDZD8 is a lysosomal vacuolator.Science (New York, N.Y.) · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. The Intimate Connection Between Lipids and Hedgehog Signaling.Frontiers in cell and developmental biology · 2022
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. 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

2 authors at 1 institution in 1 country.

Louise H WongUCL Institute of Ophthalmology, 11-43 Bath Street, London EC1V 9EL, UK.
Tim P LevineUCL Institute of Ophthalmology, 11-43 Bath Street, London EC1V 9EL, UK. Electronic address: tim.levine@ucl.ac.uk.
University College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M011801/1
6 · The paper itself

Abstract

Tubular lipid binding proteins (TULIPs) have become a focus of interest in the cell biology of lipid signalling, lipid traffic and membrane contact sites. Each tubular domain has an internal pocket with a hydrophobic lining that can bind a hydrophobic molecule such as a lipid. This allows TULIP proteins to carry lipids through the aqueous phase. TULIP domains were first found in a large family of extracellular proteins related to the bacterial permeability-inducing protein (BPI) and cholesterol ester transfer protein (CETP). Since then, the same fold and lipid transfer capacity have been found in SMP domains (so-called for their occurrence in synaptotagmin, mitochondrial and lipid binding proteins), which localise to intracellular membrane contact sites. Here the methods for identifying known TULIPs are described, and used to find previously unreported TULIPs, one in the silk polymer and another in prokaryotes illustrated by the E. coli protein YceB. The bacterial TULIP alters views on the likely evolution of the domain, suggesting its presence in the last universal common ancestor. The major function of TULIPs is to handle lipids, but we still do not know how they work in detail, or how many more remain to be discovered. This article is part of a Special Issue entitled: Membrane Contact Sites edited by Christian Ungermann and Benoit Kornmann.

Indexed as

AnimalsBacterial ProteinsBinding SitesCholesterol Ester Transfer ProteinsEvolution, MolecularHumansLipid MetabolismPhospholipid Transfer ProteinsProtein BindingBacterial ProteinsCholesterol Ester Transfer ProteinsPhospholipid Transfer ProteinsAnacetrapibCystic fibrosis transmembrane conductance regulator (CFTR)Endoplasmic reticulum-mitochondria encounter structure (ERMES)Extended-synaptotagmin (E-Syt)Lipid trafficLipopolysaccharide (LPS)PDZK8Tether

Identifiers

PMID28554774
PMCPMC5507252
OpenAlexW2619431296

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.