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

Therapeutic enzyme deimmunization by combinatorial T-cell epitope removal using neutral drift.

Proceedings of the National Academy of Sciences of the United States of America - 25 Jan 2011

Cantor Jason R, Yoo Tae Hyeon, Dixit Aakanksha, Iverson Brent L, Forsthuber Thomas G, Georgiou George

Abstract excerpt

A number of heterologous enzymes have been investigated for cancer treatment and other therapeutic applications; however, immunogenicity issues have limited their clinical utility. Here, a new approach has been created for heterologous enzyme deimmunization whereby combinatorial saturation mutagenesis is coupled with a screening strategy that capitalizes on the evolutionary biology concept of neutral drift, and...

Read the complete abstract on PubMed

Topics

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

Share to Genetic Drift
Share to Asparaginase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Directed Molecular Evolution

Share to Epitopes, T-Lymphocyte

Share to HLA-DRB1 Chains

Share to Immunization

Share to Interferon-gamma

Share to Peptide Library

Source

Open in PubMed Open full text

Identifiers

PMID: 21209329
DOI: 10.1073/pnas.1014739108
PMCID: PMC3029727

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Therapeutic enzyme deimmunization by combinatorial T-cell epitope removal using neutral drift.PMID 21209329Read ↗

Computationally optimized deimmunization libraries yield highly mutated enzymes with low immunogenicity and enhanced activity.Semantic proximity Read ↗

Fluorescence-Activated Cell Sorting of Human l-asparaginase Mutant Libraries for Detecting Enzyme Variants with Enhanced Activity.Semantic proximity Read ↗

Protein deimmunization via structure‐based design enables efficient epitope deletion at high mutational loadsSemantic proximity Read ↗

Enhancing the efficiency of directed evolution in focused enzyme libraries by the adaptive substituent reordering algorithm.Semantic proximity Read ↗

Generation of effective libraries by neutral drift.Semantic proximity Read ↗

Allosteric deimmunisation of a <i>Salmonella</i> phosphatase enhances catalytic functionSemantic proximity Read ↗

<i>In Silico</i> -Driven Engineering of <i>Halomonas elongata</i> L-Asparaginase: Towards Enhanced Proteolytic Resistance in Lymphoblastic LeukemiaSemantic proximity Read ↗

Structural and biophysical studies of new L-asparaginase variants: lessons from random mutagenesis of the prototypic Escherichia coli Ntn-amidohydrolase.Semantic proximity Read ↗

Directed enzyme evolution via small and effective neutral drift libraries.Semantic proximity Read ↗

Directed evolution of angiotensin-converting enzyme 2 (ACE2) peptidase activity profiles for therapeutic applicationsSemantic proximity Read ↗

Studies on Deimmunization of Antileukaemic L-Asparaginase to have Reduced Clinical Immunogenicity--An in silico Approach.Semantic proximity Read ↗

Advances in directed protein evolution by recursive genetic recombination: applications to therapeutic proteins.Semantic proximity Read ↗

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