Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Biochemical and biophysical research communications - 1 Apr 2017

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

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antigens
Share to Immunoglobulin Constant Regions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunoglobulin G

Share to Peptide Library

Share to Protein Aggregates

Share to Protein Domains

Share to Protein Engineering

Share to Yeasts

Source

Open in PubMed Open full text

Identifiers

PMID: 28202413
DOI: 10.1016/j.bbrc.2017.02.058
PMCID: PMC6957259

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Engineered antibody CH2 domains binding to nucleolin: Isolation, characterization and improvement of aggregation.PMID 28202413Read ↗

An engineered human IgG1 CH2 domain with decreased aggregation and nonspecific binding.Semantic proximity Read ↗

Expression, purification, and characterization of engineered antibody CH2 and VH domains.Semantic proximity Read ↗

Introducing antigen-binding sites in structural loops of immunoglobulin constant domains: Fc fragments with engineered HER2/neu-binding sites and antibody propertiesSemantic proximity Read ↗

Drug-like antibodies with high affinity, diversity and developability directly from next-generation antibody librariesSemantic proximity Read ↗

Design, construction, and characterization of a large synthetic human antibody phage display librarySemantic proximity Read ↗

NaLi-H1: A universal synthetic library of humanized nanobodies providing highly functional antibodies and intrabodiesSemantic proximity Read ↗

A fluorescent protein scaffold for presenting structurally constrained peptides provides an effective screening system to identify high affinity target-binding peptides.Semantic proximity Read ↗

General strategy for the generation of human antibody variable domains with increased aggregation resistance.Semantic proximity Read ↗

Improving antibody affinity through in vitro mutagenesis in complementarity determining regionsSemantic proximity Read ↗

Design Strategy to Create Antibody Mimetics Harbouring Immobilised Complementarity Determining Region Peptides for Practical UseSemantic proximity Read ↗

A single-domain antibody library based on a stability-engineered human VH3 scaffoldSemantic proximity Read ↗

A Highly Functional Synthetic Phage Display Library Containing over 40 Billion Human Antibody ClonesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.