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

A search for synergy in the binding kinetics of Trastuzumab and Pertuzumab whole and F(ab) to Her2

4 Aug 2015

Abstract excerpt

Therapeutic efficacy resulting from combining Trastuzumab and Pertuzumab in the treatment of Her2 overexpressing breast cancer patients has been shown to increase patient survival. This is thought to arise from inhibition of receptor dimerization and the immune tagging of the cancer cells; however, the underlying molecular mechanisms have remained enigmatic. Previously, a molecular modeling study suggested that...

Read the complete abstract on PubMed

Topics

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

Share to Cell Adhesion Molecules Research
Share to HER2/EGFR in Cancer Research
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 28721368
DOI: 10.1038/npjbcancer.2015.12

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A search for synergy in the binding kinetics of Trastuzumab and Pertuzumab whole and F(ab) to Her2PMID 28721368Read ↗

Synergy between trastuzumab and pertuzumab for human epidermal growth factor 2 (Her2) from colocalization: an in silicobased mechanismSemantic proximity Read ↗

Fluorescence cross-correlation spectroscopy quantifies affinity, cooperativity, and kinetic stability in ternary protein complexesSemantic proximity Read ↗

Dynamical rearrangement of human epidermal growth factor receptor 2 upon antibody binding: effects on the dimerizationSemantic proximity Read ↗

Not all therapeutic antibody isotypes are equal: the case of IgM versus IgG in Pertuzumab and TrastuzumabSemantic proximity Read ↗

Cryo-EM Structure of HER2-trastuzumab-pertuzumab complexSemantic proximity Read ↗

Differential and synergistic effects of epidermal growth factor receptor antibodies on unliganded ErbB dimers and oligomers.Semantic proximity Read ↗

Plant-Derived Anti-Human Epidermal Growth Factor Receptor 2 Antibody Suppresses Trastuzumab-Resistant Breast Cancer with Enhanced Nanoscale BindingSemantic proximity Read ↗

EGFR Expression in HER2-Driven Breast Cancer CellsSemantic proximity Read ↗

Prolonged Response to Trastuzumab in a Patient With HER2-Nonamplified Breast Cancer With Elevated HER2 Dimerization Harboring an<i>ERBB2</i>S310F MutationSemantic proximity Read ↗

Analysis of Cell-Surface Receptor Dynamics through Covalent Labeling by Catalyst-Tethered AntibodySemantic proximity Read ↗

Parsing ERK Activation Reveals Quantitatively Equivalent Contributions from Epidermal Growth Factor Receptor and HER2 in Human Mammary Epithelial CellsSemantic proximity Read ↗

Humanization of a recombinant monoclonal antibody to produce a therapeutic HER dimerization inhibitor, pertuzumabSemantic proximity Read ↗

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