Evidence map›Paper›PMID 28202413›Full record

ArticleBiochemical and biophysical research communications2017

Engineered antibody CH2 domains binding to nucleolin: Isolation, characterization and improvement of aggregation.

Dezhi Li, Rui Gong, Jun Zheng, Xihai Chen, Dimiter S Dimitrov, Qi Zhao

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
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  4. The reduced form of the antibody CH2 domain.Protein science : a publication of the Protein Society · 2021
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  5. Review
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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

6 authors at 5 institutions in 3 countries.

Dezhi LiCollege of Life Science, Xiamen University, Xiamen, Fujian, China.
Rui GongCAS Key Laboratory of Special Pathogens and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.
Jun ZhengFaculty of Health Sciences, University of Macau, Taipa, Macau, China.
Xihai ChenDepartment of General Surgery, The Fourth Affiliated Hospital, Harbin Medical University, Harbin, Heilongjiang, China. Electronic address: maronghai@163.com.
Dimiter S DimitrovProtein Interaction Section, Cancer Inflammation Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.
Qi ZhaoFaculty of Health Sciences, University of Macau, Taipa, Macau, China. Electronic address: zhaoqi@alumni.cuhk.net.
University of Macau · MOChinese Academy of Sciences · CNHarbin Medical University · CNNational Institutes of Health · USXiamen University · CN

Funding

Human Monoclonal Antibodies Against CancerZIABC010701 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DIMITROV, DIMITER S · 2009 to 2017
$6.9M
Human Monoclonal Antibodies and Antibody-Guided NanoparticlesZ01BC010701 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DIMITROV, DIMITER S · 2006 to 2008
$2.6M
Viral Envelope Glycoprotein Interactions with ReceptorsZ01BC010257 · BC · BASIC SCIENCES · PI DIMITROV, DIMTER S. · 1996 to 2005
–
Intramural NIH HHS Z01 BC010257Intramural NIH HHS Z01 BC010701
6 · The paper itself

Abstract

Smaller recombinant antibody fragments are now emerging as alternatives of conventional antibodies. Especially, immunoglobulin (Ig) constant CH2 domain and engineered CH2 with improved stability are promising as scaffolds for selection of specific binders to various antigens. We constructed a yeast display library based on an engineered human IgG1 CH2 scaffold with diversified loop regions. A group of CH2 binders were isolated from this yeast display library by panning against nucleolin, which is a tumor-associated antigen involved in cell proliferation, tumor cell growth and angiogenesis. Out of 20 mutants, we selected 3 clones exhibiting relatively high affinities to nucleolin on yeasts. However, recombinant CH2 mutants aggregated when they were expressed. To find the mechanism of the aggregation, we employed computational prediction approaches through structural homology models of CH2 binders. The analysis of potential aggregation prone regions (APRs) and solvent accessible surface areas (ASAs) indicated two hydrophobic residues, Val

Indexed as

Amino Acid SequenceAntigensBinding SitesComputational BiologyHumansImmunoglobulin Constant RegionsImmunoglobulin GModels, MolecularMutationNucleolinPeptide LibraryPhosphoproteinsProtein AggregatesProtein BindingProtein DomainsProtein EngineeringAntigensImmunoglobulin Constant RegionsImmunoglobulin GNucleolinPeptide LibraryPhosphoproteinsProtein AggregatesRecombinant ProteinsRNA-Binding ProteinsAggregation prone regionAntibody domainCH2Monoclonal antibodyNucleolinYeast display

Identifiers

PMID28202413
PMCPMC6957259
OpenAlexW2588089162

What OpenQuestion holds

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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.