Evidence map›Paper›PMID 19270338›Full record

ArticleThe Journal of biological chemistry2009

Glycolipid acquisition by human glycolipid transfer protein dramatically alters intrinsic tryptophan fluorescence: insights into glycolipid binding affinity.

Xiuhong Zhai, Margarita L Malakhova, Helen M Pike, Linda M Benson, H Robert Bergen, István P Sugár, Lucy Malinina, Dinshaw J Patel, Rhoderick E Brown

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Sphingolipid-Transporting Proteins as Cancer Therapeutic Targets.International journal of molecular sciences · 2019
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Sphingolipid transfer proteins defined by the GLTP-fold.Quarterly reviews of biophysics · 2015
    Article
  11. Article
  12. Article
  13. Article
  14. Structural insights into lipid-dependent reversible dimerization of human GLTP.Acta crystallographica. Section D, Biological crystallography · 2013
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

9 authors at 5 institutions in 1 country.

Xiuhong ZhaiThe Hormel Institute, University of Minnesota, Austin, Minnesota 55912.
Margarita L MalakhovaThe Hormel Institute, University of Minnesota, Austin, Minnesota 55912.
Helen M PikeThe Hormel Institute, University of Minnesota, Austin, Minnesota 55912.
Linda M BensonMayo Proteomics Research Center, Mayo Clinic College of Medicine, Rochester, Minnesota 55905.
H Robert BergenMayo Proteomics Research Center, Mayo Clinic College of Medicine, Rochester, Minnesota 55905.
István P SugárDepartment of Neurology, Mount Sinai School of Medicine, New York, New York 10029.
Lucy MalininaStructural Biology, CIC bioGUNE, Parque Tecnológico de Vizcaya, Ed. 800, Derio 48160, Spain. Electronic address: lucy@cicbiogune.es.
Dinshaw J PatelStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065. Electronic address: pateld@mskcc.org.
Rhoderick E BrownThe Hormel Institute, University of Minnesota, Austin, Minnesota 55912. Electronic address: reb@umn.edu.
Hormel (United States) · USMayo Clinic · USUniversity of Minnesota · USIcahn School of Medicine at Mount Sinai · USMemorial Sloan Kettering Cancer Center · 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 CA121493NIGMS NIH HHS GM45928NIGMS NIH HHS R01 GM045928
6 · The paper itself

Abstract

Glycolipid transfer proteins (GLTPs) are small, soluble proteins that selectively accelerate the intermembrane transfer of glycolipids. The GLTP fold is conformationally unique among lipid binding/transfer proteins and serves as the prototype and founding member of the new GLTP superfamily. In the present study, changes in human GLTP tryptophan fluorescence, induced by membrane vesicles containing glycolipid, are shown to reflect glycolipid binding when vesicle concentrations are low. Characterization of the glycolipid-induced "signature response," i.e. approximately 40% decrease in Trp intensity and approximately 12-nm blue shift in emission wavelength maximum, involved various modes of glycolipid presentation, i.e. microinjection/dilution of lipid-ethanol solutions or phosphatidylcholine vesicles, prepared by sonication or extrusion and containing embedded glycolipids. High resolution x-ray structures of apo- and holo-GLTP indicate that major conformational alterations are not responsible for the glycolipid-induced GLTP signature response. Instead, glycolipid binding alters the local environment of Trp-96, which accounts for approximately 70% of total emission intensity of three Trp residues in GLTP and provides a stacking platform that aids formation of a hydrogen bond network with the ceramide-linked sugar of the glycolipid headgroup. The changes in Trp signal were used to quantitatively assess human GLTP binding affinity for various lipids including glycolipids containing different sugar headgroups and homogenous acyl chains. The presence of the glycolipid acyl chain and at least one sugar were essential for achieving a low-to-submicromolar dissociation constant that was only slightly altered by increased sugar headgroup complexity.

Indexed as

Carrier ProteinsFluorescenceGlycolipidsHumansHydrogen BondingProtein BindingTryptophanCarrier ProteinsGLTP protein, humanGlycolipidsTryptophan

Identifiers

PMID19270338
PMCPMC2679463
OpenAlexW2034784128

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.