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

Improvement of the Pharmacological Properties of Maize RIP by Cysteine-Specific PEGylation.

Toxins - 17 Oct 2016

Au Ka-Yee, Shi Wei-Wei, Qian Shuai, Zuo Zhong, Shaw Pang-Chui

Abstract excerpt

To improve the pharmacological properties of maize ribosome-inactivating protein (maize RIP) for targeting HIV-infected cells, the previously engineered TAT-fused active form of maize RIP (MOD) was further engineered for cysteine-directed PEGylation. In this work, two potential antigenic sites, namely Lys-78 and Lys-264, were identified. They were mutated to cysteine residue and conjugated with PEG5k or PEG20k....

Read the complete abstract on PubMed

Topics

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

Share to Cysteine
Share to Half-Life
Share to Immunoglobulin E

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Immunoglobulin G

Share to Plant Proteins

Share to Polyethylene Glycols

Share to Rats, Sprague-Dawley

Share to Zea mays

Source

Open in PubMed Open full text

Identifiers

PMID: 27763506
DOI: 10.3390/toxins8100298
PMCID: PMC5086658

Genes

TAT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Improvement of the Pharmacological Properties of Maize RIP by Cysteine-Specific PEGylation.PMID 27763506Read ↗

Recent advances in (therapeutic protein) drug developmentSemantic proximity Read ↗

Mapping the antigenic determinants and reducing the immunogenicity of trichosanthin by site-directed mutagenesis.Semantic proximity Read ↗

Expression and glycoengineering of functionally active heteromultimeric IgM in plantsSemantic proximity Read ↗

G196 epitope tag system: a novel monoclonal antibody, G196, recognizes the small, soluble peptide DLVPR with high affinitySemantic proximity Read ↗

A highly expressing, soluble, and stable plant-made IgG fusion vaccine strategy enhances antigen immunogenicity in mice without adjuvantSemantic proximity Read ↗

Regulatory approval and a first-in-human phase I clinical trial of a monoclonal antibody produced in transgenic tobacco plants.Semantic proximity Read ↗

A resource of high-quality and versatile nanobodies for drug deliverySemantic proximity Read ↗

Development of therapeutic proteins: advances and challengesSemantic proximity Read ↗

CHO glycosylation mutants as potential host cells to produce therapeutic proteins with enhanced efficacy.Semantic proximity Read ↗

Rational design of low immunogenic anti CD25 recombinant immunotoxin for T cell malignancies by elimination of T cell epitopes in PE38.Semantic proximity Read ↗

[Transglutaminase-based antibody-drug conjugation: antibody site-specific mutation and identification].Semantic proximity Read ↗

Elimination of N-glycosylation by site mutation further prolongs the half-life of IFN-α/Fc fusion proteins expressed in Pichia pastoris.Semantic proximity Read ↗

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