Evidence map›Paper›PMID 30063825›Full record

ArticleBioconjugate chemistry2018

Efficient Assembly of Quantum Dots with Homogenous Glycans Derived from Natural N-Linked Glycoproteins.

Valle Palomo, Philip A Cistrone, Naiqian Zhan, Goutam Palui, Hedi Mattoussi, Philip E Dawson

Open access · greenAbstract read
In one paragraph

Article in Bioconjugate chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Glycan Nanobiosensors.Nanomaterials (Basel, Switzerland) · 2020
    Review
  3. Quantum Dot Labelling of Tepary Bean (Molecules (Basel, Switzerland) · 2020
    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

6 authors at 2 institutions in 1 country.

Valle PalomoDepartment of Chemistry , The Scripps Research Institute , La Jolla , California 92037 , United States.ORCID 0000-0002-1473-4086
Philip A CistroneDepartment of Chemistry , The Scripps Research Institute , La Jolla , California 92037 , United States.
Naiqian ZhanDepartment of Chemistry and Biochemistry , Florida State University , Tallahassee , Florida 32306 , United States.
Goutam PaluiDepartment of Chemistry and Biochemistry , Florida State University , Tallahassee , Florida 32306 , United States.
Hedi MattoussiDepartment of Chemistry and Biochemistry , Florida State University , Tallahassee , Florida 32306 , United States.ORCID 0000-0002-6511-9323
Philip E DawsonDepartment of Chemistry , The Scripps Research Institute , La Jolla , California 92037 , United States.ORCID 0000-0002-2538-603X
Florida State University · USScripps Research Institute · US

Funding

Cyclic EphA4 peptide antagonists for neuroprotection in ALSR01NS087070 · NINDS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI PASQUALE, ELENA B · 2014 to 2018
$3.5M
NINDS NIH HHS R01 NS087070
6 · The paper itself

Abstract

Coating inorganic nanoparticles with polyethylene glycol (PEG)-appended ligands, as means to preserve their physical characteristics and promote steric interactions with biological systems, including enhanced aqueous solubility and reduced immunogenicity, has been explored by several groups. Conversely, macromolecules present in the human serum and on the surface of cells are densely coated with hydrophilic glycans that act to reduce nonspecific interactions, while facilitating specific binding and interactions. In particular, N-linked glycans are abundant on the surface of most serum proteins and are composed of a branched architecture that is typically characterized by a significant level of molecular heterogeneity. Here we provide two distinct methodologies, covalent bioconjugation and self-assembly, to functionalize two types of Quantum Dots with a homogeneous, complex-type N-linked glycan terminated with a sialic acid moiety. A detailed physical and functional characterization of these glycan-coated nanoparticles has been performed. Our findings support the potential use of such fluorescent platforms to sense glycan-involved biological processes, such as lectin recognition and sialidase-mediated hydrolysis.

Indexed as

Quantum DotsElectrophoretic Mobility Shift AssayGlycoproteinsHydrophobic and Hydrophilic InteractionsPolyethylene GlycolsPolysaccharidesGlycoproteinsPolyethylene GlycolsPolysaccharides

Identifiers

PMID30063825
PMCPMC8524201
OpenAlexW2887183961

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.