Evidence map›Paper›PMID 25121619›Full record

ArticleBioconjugate chemistry2014

Optimization of photoactive protein Z for fast and efficient site-specific conjugation of native IgG.

James Z Hui, Andrew Tsourkas

Abstract read
In one paragraph

Article in Bioconjugate chemistry, 2014. 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
3.0field-weighted citation impact, top 9% 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, 42 citations in OpenAlex.

  1. Review
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  6. Nanomaterial-based contrast agents.Nature reviews. Methods primers · 2023
    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.

James Z HuiDepartment of Bioengineering, University of Pennsylvania , 210 South 33rd Street, 240 Skirkanich Hall, Philadelphia, Pennsylvania 19104, United States.
Andrew Tsourkas
University of Pennsylvania · US

Funding

Bridging multiple scales in modeling targeted drug nanocarrier deliveryU01EB016027 · NIBIB · UNIVERSITY OF PENNSYLVANIA · PI ECKMANN, DAVID M, RADHAKRISHNAN, RAVI · 2013 to 2017
$2.7M
Highly Paramagnetic, Biodegradable Nanoclusters for Imaging Prostate CancerR01CA157766 · NCI · UNIVERSITY OF PENNSYLVANIA · PI TSOURKAS, ANDREW · 2011 to 2015
$1.6M
Imaging B Cells with Gd-Labeled Dendrimer NanoclustersR01EB012065 · NIBIB · UNIVERSITY OF PENNSYLVANIA · PI TSOURKAS, ANDREW · 2010 to 2013
$1.4M
A facile method for producing bispecific antibodies from full-length IgGR21CA187657 · NCI · UNIVERSITY OF PENNSYLVANIA · PI TSOURKAS, ANDREW · 2014 to 2015
$383k
NCI NIH HHS R01CA15766NCI NIH HHS R01 CA157766NCI NIH HHS R21 CA187657NCI NIH HHS R21CA187657NIBIB NIH HHS R01 EB012065NIBIB NIH HHS R01EB012065NIBIB NIH HHS U01 EB016027
6 · The paper itself

Abstract

Antibody conjugates have been used in a variety of applications from immunoassays to drug conjugates. However, it is becoming increasingly clear that in order to maximize an antibody's antigen binding ability and to produce homogeneous antibody-conjugates, the conjugated molecule should be attached onto IgG site-specifically. We previously developed a facile method for the site-specific modification of full length, native IgGs by engineering a recombinant Protein Z that forms a covalent link to the Fc domain of IgG upon exposure to long wavelength UV light. To further improve the efficiency of Protein Z production and IgG conjugation, we constructed a panel of 13 different Protein Z variants with the UV-active amino acid benzoylphenylalanine (BPA) in different locations. By using this panel of Protein Z to cross-link a range of IgGs from different hosts, including human, mouse, and rat, we discovered two previously unknown Protein Z variants, L17BPA and K35BPA, that are capable of cross-linking many commonly used IgG isotypes with efficiencies ranging from 60% to 95% after only 1 h of UV exposure. When compared to existing site-specific methods, which often require cloning or enzymatic reactions, the Protein Z-based method described here, utilizing the L17BPA, K35BPA, and the previously described Q32BPA variants, represents a vastly more accessible and efficient approach that is compatible with nearly all native IgGs, thus making site-specific conjugation more accessible to the general research community.

Indexed as

AnimalsBinding SitesBlood ProteinsHumansImmunoglobulin GKineticsMiceModels, MolecularMutationPhenylalanineProtein ConformationRatsSubstrate SpecificitybenzoylphenylalanineBlood ProteinsImmunoglobulin GPhenylalanineplasma protein Z

Identifiers

PMID25121619
PMCPMC4166039
OpenAlexW2321496780

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.