Evidence map›Paper›PMID 15329726›Full record

ArticleNature2004

Structural basis for glycosphingolipid transfer specificity.

Lucy Malinina, Margarita L Malakhova, Alexei Teplov, Rhoderick E Brown, Dinshaw J Patel

Open access · greenAbstract read
In one paragraph

Article in Nature, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

62 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
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  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Sphingolipid-Transporting Proteins as Cancer Therapeutic Targets.International journal of molecular sciences · 2019
    Review
  14. Article
  15. Upregulation of human glycolipid transfer protein (GLTP) induces necroptosis in colon carcinoma cells.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2019
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

2 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 1 country.

Lucy MalininaStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
Margarita L Malakhova
Alexei Teplov
Rhoderick E Brown
Dinshaw J Patel
Memorial Sloan Kettering Cancer Center · USHormel (United States) · USUniversity of Minnesota · US

Funding

GLYCOLIPID TRANSFER--REGULATION BY MEMBRANE INTERFACESR01GM045928 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI BROWN, RHODERICK E · 1992 to 2014
$4.8M
NIGMS NIH HHS R01 GM045928
6 · The paper itself

Abstract

Lipid transfer proteins are important in membrane vesicle biogenesis and trafficking, signal transduction and immunological presentation processes. The conserved and ubiquitous mammalian glycolipid transfer proteins (GLTPs) serve as potential regulators of cell processes mediated by glycosphingolipids, ranging from differentiation and proliferation to invasive adhesion, neurodegeneration and apoptosis. Here we report crystal structures of apo-GLTP (1.65 A resolution) and lactosylceramide-bound (1.95 A) GLTP, in which the bound glycosphingolipid is sandwiched, after adaptive recognition, within a previously unknown two-layer all-alpha-helical topology. Glycosphingolipid binding specificity is achieved through recognition and anchoring of the sugar-amide headgroup to the GLTP recognition centre by hydrogen bond networks and hydrophobic contacts, and encapsulation of both lipid chains, in a precisely oriented manner within a 'moulded-to-fit' hydrophobic tunnel. A cleft-like conformational gating mechanism, involving two interhelical loops and one alpha-helix of GLTP, could enable the glycolipid chains to enter and leave the tunnel in the membrane-associated state. Mutation and functional analyses of residues in the glycolipid recognition centre and within the hydrophobic tunnel support a framework for understanding how GLTPs acquire and release glycosphingolipids during lipid intermembrane transfer and presentation processes.

Indexed as

Antigens, CDApoproteinsApoptosisCarrier ProteinsCrystallography, X-RayHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsLactosylceramidesModels, MolecularMutationProtein Structure, SecondaryStructure-Activity RelationshipSubstrate SpecificityAntigens, CDApoproteinsCarrier ProteinsCDw17 antigenGLTP protein, humanLactosylceramideslipid transfer protein

Identifiers

PMID15329726
PMCPMC2640488
OpenAlexW2129019768

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.