Evidence map›Paper›PMID 25797198›Full record

ArticleQuarterly reviews of biophysics2015

Sphingolipid transfer proteins defined by the GLTP-fold.

Lucy Malinina, Dhirendra K Simanshu, Xiuhong Zhai, Valeria R Samygina, RaviKanth Kamlekar, Roopa Kenoth, Borja Ochoa-Lizarralde, Margarita L Malakhova, Julian G Molotkovsky, Dinshaw J Patel and 1 more

Open access · greenAbstract read
In one paragraph

Article in Quarterly reviews of biophysics, 2015. 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
1.7field-weighted citation impact, top 16% 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, 36 citations in OpenAlex.

  1. Article
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  10. Review
  11. Article
  12. Review
  13. Article
  14. Sphingolipid-Transporting Proteins as Cancer Therapeutic Targets.International journal of molecular sciences · 2019
    Review
  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
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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

11 authors at 1 institution in 1 country.

Lucy MalininaThe Hormel Institute, University of Minnesota,Austin,MN 55912,USA.
Dhirendra K SimanshuStructural Biology Program,Memorial Sloan-Kettering Cancer Center,New York,NY 10065,USA.
Xiuhong ZhaiThe Hormel Institute, University of Minnesota,Austin,MN 55912,USA.
Valeria R SamyginaStructural Biology Unit,CICbioGUNE, Technology Park of Bizkaia,48160 Derio-Bilbao,Spain.
RaviKanth KamlekarThe Hormel Institute, University of Minnesota,Austin,MN 55912,USA.
Roopa KenothThe Hormel Institute, University of Minnesota,Austin,MN 55912,USA.
Borja Ochoa-LizarraldeStructural Biology Unit,CICbioGUNE, Technology Park of Bizkaia,48160 Derio-Bilbao,Spain.
Margarita L MalakhovaThe Hormel Institute, University of Minnesota,Austin,MN 55912,USA.
Julian G MolotkovskyShemyakin-Ovchinnikov Institute of Bioorganic Chemistry,Russian Academy of Sciences,Moscow,Russia.
Dinshaw J PatelStructural Biology Program,Memorial Sloan-Kettering Cancer Center,New York,NY 10065,USA.
Rhoderick E BrownThe Hormel Institute, University of Minnesota,Austin,MN 55912,USA.
Institute of Bioorganic Chemistry · RU

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
GLYCOLIPID TRANSFER--REGULATION BY MEMBRANE INTERFACESR01GM045928 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI BROWN, RHODERICK E · 1992 to 2014
$4.8M
The functional role of the cPLA2alpha/C1P interaction in sepsis resolutionR01HL125353 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI BROWN, RHODERICK E, CHALFANT, CHARLES E. · 2014 to 2018
$4.0M
MOLECULAR BASIS OF GLYCOSPHINGOLIPID BINDING SPECIFICITYR01CA121493 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI PATEL, DINSHAW J · 2006 to 2010
$1.2M
NCI NIH HHS P30 CA008748NCI NIH HHS R01 CA121493NHLBI NIH HHS R01 HL125353NIGMS NIH HHS GM45928NIGMS NIH HHS R01 GM045928
6 · The paper itself

Abstract

Glycolipid transfer proteins (GLTPs) originally were identified as small (~24 kDa), soluble, amphitropic proteins that specifically accelerate the intermembrane transfer of glycolipids. GLTPs and related homologs now are known to adopt a unique, helically dominated, two-layer 'sandwich' architecture defined as the GLTP-fold that provides the structural underpinning for the eukaryotic GLTP superfamily. Recent advances now provide exquisite insights into structural features responsible for lipid headgroup selectivity as well as the adaptability of the hydrophobic compartment for accommodating hydrocarbon chains of differing length and unsaturation. A new understanding of the structural versatility and evolutionary premium placed on the GLTP motif has emerged. Human GLTP-motifs have evolved to function not only as glucosylceramide binding/transferring domains for phosphoinositol 4-phosphate adaptor protein-2 during glycosphingolipid biosynthesis but also as selective binding/transfer proteins for ceramide-1-phosphate. The latter, known as ceramide-1-phosphate transfer protein, recently has been shown to form GLTP-fold while critically regulating Group-IV cytoplasmic phospholipase A2 activity and pro-inflammatory eicosanoid production.

Indexed as

Carrier ProteinsGlycolipidsProtein FoldingSphingolipidsCarrier ProteinsGlycolipidsSphingolipids

Identifiers

PMID25797198
PMCPMC4691851
OpenAlexW2046407639

What OpenQuestion holds

Textmetadata
LicenceTDM
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.