Evidence map›Paper›PMID 17379573›Full record

ArticleBiomolecular engineering2007

Metabolic biotinylation of recombinant antibody by biotin ligase retained in the endoplasmic reticulum.

Bhaswati Barat, Anna M Wu

Open access · greenAbstract read
In one paragraph

Article in Biomolecular engineering, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

27 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
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  8. Reporter gene systems: A powerful tool forCurrent research in microbial sciences · 2022
    Article
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  16. Detection of electrophile-sensitive proteins.Biochimica et biophysica acta · 2014
    Review
  17. Article
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

Bhaswati BaratCrump Institute for Molecular Imaging, Department of Molecular & Medical Pharmacology, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.
Anna M Wu
Institute for Molecular Medicine · US

Funding

Women's CancersP30CA016042 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Samuel Wheeler French · 1985 to 2026
$134.5M
RECOMBINANT ANTI-CEA ANTIBODIESP01CA043904 · NCI · CITY OF HOPE NATIONAL MEDICAL CENTER · PI RAUBITSCHEK, ANDREW A. · 1988 to 2012
$30.2M
Transductionally Redirected /Transcriptionally RestricteP50CA086306 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HERSCHMAN, HARVEY R. · 2000 to 2014
$29.0M
Stanford Nanocharacterization LaboratoryU54CA119367 · NCI · STANFORD UNIVERSITY · PI GAMBHIR, SANJIV S · 2006 to 2010
$19.8M
NCI NIH HHS CA16042NCI NIH HHS P01 CA043904NCI NIH HHS P01 CA43904NCI NIH HHS P30 CA016042NCI NIH HHS P50 CA086306NCI NIH HHS P50 CA86306NCI NIH HHS U54 CA119367
6 · The paper itself

Abstract

Due to its strength and specificity, the interaction between avidin and biotin has been used in a variety of scientific and medical applications ranging from immunohistochemistry to drug targeting. The present study describes two methods for biotinylation of proteins secreted from eukaryotic cells using the Escherichia coli biotin protein ligase. In one system the biotin ligase was co-secreted from the cells along with substrate protein enabling extracellular biotinylation of the tagged protein. In the other system, biotin ligase was engineered to be retained in the endoplasmic reticulum (ER) and metabolically biotinylates the secretory protein as it passes through the ER. An engineered antibody fragment, a diabody with specificity for carcinoembryonic antigen (CEA) was fused to the biotin acceptor domain (123 amino acid) of Propionibacterium shermanii. Coexpression of the fusion protein with ER retained biotin ligase showed higher biotinylation efficiency than biotinylation by co-secreted ligase. Biotinylation of the anti-CEA diabody tagged with a short (15 amino acid, Biotin Avitag) biotin acceptor peptide was also successful. Utilization of ER retained biotin ligase for biotinylation of protein is an attractive alternative for efficiently producing uniformly biotinylated recombinant proteins for a variety of avidin-biotin technologies.

Indexed as

Antibodies, MonoclonalBiotinylationCarbon-Nitrogen LigasesEndoplasmic ReticulumEscherichia coliEscherichia coli ProteinsProtein EngineeringRecombinant Fusion ProteinsRepressor ProteinsTranscription FactorsAntibodies, MonoclonalbirA protein, E coliCarbon-Nitrogen LigasesEscherichia coli ProteinsRecombinant Fusion ProteinsRepressor ProteinsTranscription Factors

Identifiers

PMID17379573
PMCPMC2682619
OpenAlexW2024781125

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.