ArticleAMB Express2016
A single-domain antibody-linked Fab bispecific antibody Her2-S-Fab has potent cytotoxicity against Her2-expressing tumor cells.
Article in AMB Express, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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.
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.
Who cites it
19 citing papers in PubMed, 25 citations in OpenAlex.
- Unveiling the Synergistic Potential: Bispecific Antibodies in Conjunction with Chemotherapy for Advanced Non-Small-Cell Lung Cancer Treatment.Current oncology (Toronto, Ont.) · 2025Review
- Understanding the role of TNFR2 signaling in the tumor microenvironment of breast cancer.Journal of experimental & clinical cancer research : CR · 2024Review
- Modular design of bi- and multi-specific knob domain fusions.Frontiers in immunology · 2024Article
- Reviving a Classic Antigen with a Cutting-Edge Approach: Nanobodies for HER2+ Breast Cancer.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Review
- Nanobodies: Next Generation of Cancer Diagnostics and Therapeutics.Frontiers in oncology · 2020Review
- Bp-Bs, a Novel T-cell Engaging Bispecific Antibody with Biparatopic Her2 Binding, Has Potent Anti-tumor Activities.Molecular therapy oncolytics · 2019Article
- Nanobody Engineering: Toward Next Generation Immunotherapies and Immunoimaging of Cancer.Antibodies (Basel, Switzerland) · 2019Review
- Bispecific light T-cell engagers for gene-based immunotherapy of epidermal growth factor receptor (EGFR)-positive malignancies.Cancer immunology, immunotherapy : CII · 2018Article
- A GPC3-targeting Bispecific Antibody, GPC3-S-Fab, with Potent Cytotoxicity.Journal of visualized experiments : JoVE · 2018Article
- A HER2 bispecific antibody can be efficiently expressed inOncology letters · 2018Article
- A Single Domain-Based Anti-Her2 Antibody Has Potent Antitumor Activities.Translational oncology · 2018Article
- Brief introduction of current technologies in isolation of broadly neutralizing HIV-1 antibodies.Virus research · 2018Review
- Site-specific PEGylation of an anti-CEA/CD3 bispecific antibody improves its antitumor efficacy.International journal of nanomedicine · 2018Article
- Single-Domain Antibodies and the Promise of Modular Targeting in Cancer Imaging and Treatment.Frontiers in immunology · 2018Review
- Article
- BiHC, a T-Cell-Engaging Bispecific Recombinant Antibody, Has Potent Cytotoxic Activity Against Her2 Tumor Cells.Translational oncology · 2017Article
- Bispecific Antibodies as a Development Platform for New Concepts and Treatment Strategies.International journal of molecular sciences · 2016Review
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Her2, which is frequently overexpressed in breast cancer, is one of the most studied tumor-associated antigens for cancer therapy. Anti-HER2 monoclonal antibody, trastuzumab, has achieved significant clinical benefits in metastatic breast cancer. In this study, we describe a novel bispecific antibody Her2-S-Fab targeting Her2 by linking a single domain anti-CD16 VHH to the trastuzumab Fab. The Her2-S-Fab antibody can be efficiently expressed and purified from Escherichia coli, and drive potent cancer cell killing in HER2-overexpressing cancer cells. In xenograft model, the Her2-S-Fab suppresses tumor growth in the presence of human immune cells. Our results suggest that the bispecific Her2-S-Fab may provide a valid alternative to Her2 positive cancer therapy.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.