Evidence map›Paper›PMID 15287756›Full record

ArticleBiochemistry2004

Human glycolipid transfer protein: probing conformation using fluorescence spectroscopy.

Xin-Min Li, Margarita L Malakhova, Xin Lin, Helen M Pike, Taeowan Chung, Julian G Molotkovsky, Rhoderick E Brown

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.2field-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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
  5. Article
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  7. Article
  8. Article
  9. Sphingolipid transfer proteins defined by the GLTP-fold.Quarterly reviews of biophysics · 2015
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Glycolipid transfer proteins.Biochimica et biophysica acta · 2007
    Review
  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

7 authors at 4 institutions in 3 countries.

Xin-Min LiThe Hormel Institute, University of Minnesota, 801 16th Avenue NE, Austin, Minnesota 55912-3698, USA.
Margarita L Malakhova
Xin Lin
Helen M Pike
Taeowan Chung
Julian G Molotkovsky
Rhoderick E Brown
Hormel (United States) · USInstitute of Bioorganic Chemistry · RURussian Academy of Sciences · RUYeungnam University · KR

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 GM45928NIGMS NIH HHS R01 GM045928
6 · The paper itself

Abstract

Glycolipid transfer protein (GLTP) is a soluble 24 kDa protein that selectively accelerates the intermembrane transfer of glycolipids in vitro. Little is known about the GLTP structure and dynamics. Here, we report the cloning of human GLTP and characterize the environment of the three tryptophans (Trps) of the protein using fluorescence spectroscopy. Excitation at 295 nm yielded an emission maximum (lambda(max)) near 347 nm, indicating a relatively polar average environment for emitting Trps. Quenching with acrylamide at physiological ionic strength or with potassium iodide resulted in linear Stern-Volmer plots, suggesting accessibility of emitting Trps to soluble quenchers. Insights into reversible conformational changes accompanying changes in GLTP activity were provided by addition and rapid dilution of urea while monitoring changes in Trp or 1-anilinonaphthalene-8-sulfonic acid fluorescence. Incubation of GLTP with glycolipid liposomes caused a blue shift in the Trp emission maximum but diminished the fluorescence intensity. The blue-shifted emission maximum, centered near 335 nm, persisted after separation of glycolipid liposomes from GLTP, consistent with formation of a GLTP-glycolipid complex at a glycolipid-liganding site containing Trp. The results provide the first insights into human GLTP structural dynamics by fluorescence spectroscopy, including global conformational changes that accompany GLTP folding into an active conformational state as well as more subtle conformational changes that play a role in GLTP-mediated transfer of glycolipids between membranes, and establish a foundation for future studies of membrane rafts using GLTP.

Indexed as

Amino Acid SequenceAnimalsCarrier ProteinsCattleCloning, MolecularGlycolipidsHumansLiposomesMiceMolecular Sequence DataProtein ConformationProtein DenaturationProtein FoldingRecombinant ProteinsSpectrometry, FluorescenceSwineCarrier ProteinsGLTP protein, humanGltp protein, mouseGlycolipidslipid transfer proteinLiposomesRecombinant ProteinsTryptophanUrea

Identifiers

PMID15287756
PMCPMC2593833
OpenAlexW2008171714

What OpenQuestion holds

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Registered trials

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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.