Evidence map›Paper›PMID 18426242›Full record

ReviewBiotechnology progress

Site-specific linking of biomolecules via glycan residues using glycosyltransferases.

Pradman K Qasba, Elizabeth Boeggeman, Boopathy Ramakrishnan

Open access · bronzeAbstract readReview
In one paragraph

Review in Biotechnology progress. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

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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

3 authors at 2 institutions in 1 country.

Pradman K QasbaStructural Glycobiology Section, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, Center for Cancer Research, NCI-Frederick, Frederick, Maryland 21702, USA. qasba@helix.nih.gov
Elizabeth Boeggeman
Boopathy Ramakrishnan
Center for Cancer Research · USScience Applications International Corporation (United States) · US

Funding

Utilizing Glycosyltransferases for BioconjugationZIABC010742 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI QASBA, PRADMAN K · 2009 to 2013
$1.1M
Utilizing Glycosyltransferases for BioconjugationZ01BC010742 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI QASBA, PRADMAN K · 2006 to 2008
$678k
Structure-Function Studies and Design of Novel GlycosyltransferasesZ01BC009304 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI QASBA, PRADMAN K · 1996 to 2008
$631k
Using Glycosyltransferases for Conjugation of Single-Chain Antibodies and LipidsZIABC010805 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI QASBA, PRADMAN K · 2009 to 2010
$509k
Oligosaccharide substrate interactions with beta-1,4-GalZ01BC010041 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI QASBA, PRADMAN K · 1996 to 2008
$216k
Intramural NIH HHS Z01 BC009304Intramural NIH HHS Z01 BC010742NCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400
6 · The paper itself

Abstract

The structural information on glycosyltransferases has revealed that the sugar-donor specificity of these enzymes can be broadened to include modified sugars with a chemical handle that can be utilized for conjugation chemistry. Substitution of Tyr289 to Leu in the catalytic pocket of bovine beta-1,4-galactosyltransferase generates a novel glycosyltransferase that can transfer not only Gal but also GalNAc or a C2-modified galactose that has a chemical handle, from the corresponding UDP-derivatives, to the non-reducing end GlcNAc residue of a glycoconjugate. Similarly, the wild-type polypeptide-N-acetyl-galactosaminyltransferase, which naturally transfers GalNAc from UDP-GalNAc, can also transfer C2-modified galactose with a chemical handle from its UDP-derivative to the Ser/Thr residue of a polypeptide acceptor substrate that is tagged as a fusion peptide to a non-glycoprotein. The potential of wild-type and mutant glycosyltransferases to produce glycoconjugates carrying sugar moieties with chemical handle makes it possible to conjugate biomolecules with orthogonal reacting groups at specific sites. This methodology assists in the assembly of bio-nanoparticles that are useful for developing targeted drug-delivery systems and contrast agents for magnetic resonance imaging.

Indexed as

Drug DesignBinding SitesBiopolymersCatalysisCross-Linking ReagentsGlycosyltransferasesPolysaccharidesBiopolymersCross-Linking ReagentsGlycosyltransferasesPolysaccharides

Identifiers

PMID18426242
PMCPMC2435414
OpenAlexW2035590565

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.