Evidence map›Paper›PMID 27412675›Full record

ArticleJournal of lipid research2016

Synthesis of a novel photoactivatable glucosylceramide cross-linker.

Monique Budani, Murugesapillai Mylvaganam, Beth Binnington, Clifford Lingwood

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of lipid research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 28% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Central Roles of Glucosylceramide in Driving Cancer Pathogenesis.International journal of molecular sciences · 2025
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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

4 authors at 2 institutions in 1 country.

Monique BudaniDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada Division of Molecular Structure and Function, Peter Gilgan Centre for Research and Learning, Research Institute, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada.
Murugesapillai MylvaganamDivision of Molecular Structure and Function, Peter Gilgan Centre for Research and Learning, Research Institute, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada.
Beth BinningtonDivision of Molecular Structure and Function, Peter Gilgan Centre for Research and Learning, Research Institute, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada.
Clifford LingwoodDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada Division of Molecular Structure and Function, Peter Gilgan Centre for Research and Learning, Research Institute, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Hospital for Sick Children · CAUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biosynthesis of glucosylceramide (GlcCer) is a key rate-limiting step in complex glycosphingolipid (GSL) biosynthesis. To further define interacting partners of GlcCer, we have made a cleavable, biotinylated, photoreactive GlcCer analog in which the reactive nitrene is closely apposed to the GlcCer head group, by substituting the native fatty acid with d, l-2-aminohexadecanoic acid. Two amino-GlcCer diastereomer cross-linkers (XLA and XLB) were generated. XLB proved an effective lactosylceramide (LacCer) synthase substrate while XLA was inhibitory. Both probes specifically bound and cross-linked the GlcCer binding protein, glycolipid transfer protein (GLTP), but not other GSL binding proteins (Shiga toxin and cholera toxin). GlcCer inhibited GLTP cross-linking. Both GlcCer cross-linkers competed with microsomal nitrobenzoxadiazole (NBD)-GlcCer anabolism to NBD-LacCer. GLTP showed marked, ATP-dependent enhancement of cell-free intact microsomal LacCer synthesis from endogenous or exogenous liposomal GlcCer, supporting a role in the transport/membrane translocation of cytosolic and extra-Golgi GlcCer. GLTP was specifically labeled by either XLA or XLB GlcCer cross-linker during this process, together with a (the same) small subset of microsomal proteins. These cross-linkers will serve to probe physiologically relevant GlcCer-interacting cellular proteins.

Indexed as

Carrier ProteinsCell Line, TumorCross-Linking ReagentsFatty AcidsGangliosidesGlucosylceramidesGlycolipidsGlycosphingolipidsGolgi ApparatusHumansIminesCarrier ProteinsCross-Linking ReagentsFatty AcidsGangliosidesGLTP protein, humanGlucosylceramidesGlycolipidsGlycosphingolipidsImineslipid transfer proteinphenylnitreneflippasegangliosidesglycolipidsglycolipid transportglycosphingolipid anabolismGolgi apparatuslipids/chemistrylipid transfer proteins

Identifiers

PMID27412675
PMCPMC5003150
OpenAlexW2467275376

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.