Evidence map›Paper›PMID 25172148›Full record

ArticleBioorganic & medicinal chemistry2014

Synthesis of α-L-rhamnosyl ceramide and evaluation of its binding with anti-rhamnose antibodies.

David E Long, Partha Karmakar, Katherine A Wall, Steven J Sucheck

Abstract read
In one paragraph

Article in Bioorganic & medicinal chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

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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.

David E LongDepartment of Chemistry, The University of Toledo, 2801 W. Bancroft Street, MS602, Toledo, OH 43606, United States.
Partha KarmakarDepartment of Chemistry, The University of Toledo, 2801 W. Bancroft Street, MS602, Toledo, OH 43606, United States.
Katherine A WallDepartment of Medicinal and Biological Chemistry, The University of Toledo, 2801 W. Bancroft Street, MS602, Toledo, OH 43606, United States. Electronic address: katherine.wall@utoledo.edu.
Steven J SucheckDepartment of Chemistry, The University of Toledo, 2801 W. Bancroft Street, MS602, Toledo, OH 43606, United States. Electronic address: steve.sucheck@utoledo.edu.

Funding

Synthesis of Glycopeptide-Based Cancer Antigen VaccinesR15GM094734 · NIGMS · UNIVERSITY OF TOLEDO HEALTH SCI CAMPUS · PI WALL, KATHERINE A · 2011 to 2015
$755k
NIGMS NIH HHS GM094734NIGMS NIH HHS R15 GM094734
6 · The paper itself

Abstract

An α-L-rhamnosyl ceramide (1, α-L-RhaCer) has been prepared that was recognized by anti-L-rhamnose (anti-Rha) antibodies. During these studies we explored the use of an α-L-rhamnosyl thioglycoside and a trichloroacetimidate as a glycosyl donors. Subsequently, the acceptors desired for glycosylation, 3-O-benzoylazidosphingosine or 3-O-alloxycarbonylsphingosine, were prepared from D-xylose. The thioglycoside donor, 2,3,4-tri-O-acetyl-1-(4-tolyl)thio-α-L-rhamnopyranoside, and the trichloroacetimidate donor, 2,3,4-tri-O-acetyl-1-(2,2,2-trichloroethanimidate)-α-L-rhamnopyranoside, were synthesized in 50% and 78% yield overall, respectively. The synthesis of the glycosylation acceptor employed an addition-fragmentation olefination that was successfully carried out in 53% yield. With the successful synthesis of key intermediates, α-L-RhaCer (1) was prepared without any insurmountable obstacles. Anti-Rha antibodies were prepared in BALB/c mice by immunizing them with rhamnose-ovalbumin (Rha-Ova) with Sigma Adjuvant System (SAS) and the anti-L-Rha antibodies were isolated from the blood sera. Liposomes and EL4 tumor cells were used as model systems to demonstrate the ability of 1 to insert into a lipid bilayer. The interaction of the liposomes or the EL4 cells with α-L-RhaCer (1) and anti-Rha antibodies were investigated by fluorescence microscopy and flow cytometry, respectively, to confirm the ability of glycolipid 1 to be displayed on the tumor cell surface as well as the ability to be recognized by anti-Rha antibodies.

Indexed as

AnimalsAntibodiesBinding SitesCell Line, TumorLymphomaMannoseMiceMolecular StructureRhamnosealpha-L-rhamnosyl ceramideAntibodiesMannoseRhamnoseAnti-cancer vaccineAnti-rhamnose antibodyGlycolipidRhamnosyl-ceramide

Identifiers

PMID25172148
PMCPMC4172545

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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.