Evidence map›Paper›PMID 17105344›Full record

ArticlePLoS biology2006

The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure.

Lucy Malinina, Margarita L Malakhova, Alex T Kanack, Min Lu, Ruben Abagyan, Rhoderick E Brown, Dinshaw J Patel

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

36 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. 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
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Sphingolipid transfer proteins defined by the GLTP-fold.Quarterly reviews of biophysics · 2015
    Article
  15. Article
  16. Structural insights into lipid-dependent reversible dimerization of human GLTP.Acta crystallographica. Section D, Biological crystallography · 2013
    Article
  17. Article
  18. Sphingolipid homeostasis in the endoplasmic reticulum and beyond.Cold Spring Harbor perspectives in biology · 2013
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 1 country.

Lucy MalininaStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, United States of America.
Margarita L Malakhova
Alex T Kanack
Min Lu
Ruben Abagyan
Rhoderick E Brown
Dinshaw J Patel
University of Minnesota · USMemorial Sloan Kettering Cancer Center · USCornell University · USScripps Research Institute · US

Funding

GLYCOLIPID TRANSFER--REGULATION BY MEMBRANE INTERFACESR01GM045928 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI BROWN, RHODERICK E · 1992 to 2014
$4.8M
MOLECULAR BASIS OF GLYCOSPHINGOLIPID BINDING SPECIFICITYR01CA121493 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI PATEL, DINSHAW J · 2006 to 2010
$1.2M
NCI NIH HHS CA121493NCI NIH HHS R01 CA121493NIGMS NIH HHS GM45928NIGMS NIH HHS R01 GM045928
6 · The paper itself

Abstract

Glycosphingolipids (GSLs) play major roles in cellular growth and development. Mammalian glycolipid transfer proteins (GLTPs) are potential regulators of cell processes mediated by GSLs and display a unique architecture among lipid binding/transfer proteins. The GLTP fold represents a novel membrane targeting/interaction domain among peripheral proteins. Here we report crystal structures of human GLTP bound to GSLs of diverse acyl chain length, unsaturation, and sugar composition. Structural comparisons show a highly conserved anchoring of galactosyl- and lactosyl-amide headgroups by the GLTP recognition center. By contrast, acyl chain chemical structure and occupancy of the hydrophobic tunnel dictate partitioning between sphingosine-in and newly-observed sphingosine-out ligand-binding modes. The structural insights, combined with computed interaction propensity distributions, suggest a concerted sequence of events mediated by GLTP conformational changes during GSL transfer to and/or from membranes, as well as during GSL presentation and/or transfer to other proteins.

Indexed as

Base SequenceBinding SitesCarrier ProteinsCrystallography, X-RayGlycolipidsHumansLigandsModels, ChemicalMolecular Sequence DataProtein Structure, SecondarySphingosineStructure-Activity RelationshipCarrier ProteinsGlycolipidsLigandslipid transfer proteinSphingosine

Identifiers

PMID17105344
PMCPMC1618416
OpenAlexW2052081608

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.