Results 41 to 50 of about 70,621 (279)

A Case of Corneal Melting in a Patient with HER2-Positive Breast Cancer

open access: yesCase Reports in Ophthalmology, 2022
Trastuzumab is the cornerstone treatment for HER2-positive breast cancer. While ocular side effects are more commonly described after the use of the antibody-drug conjugate ado-trastuzumab emtansine, we here describe corneal melting in a 79-year-old ...
Deborah Peeters   +3 more
doaj   +1 more source

Retracted: Trastuzumab induces PUMA‐dependent apoptosis and inhibits tumor growth in gastric cancer

open access: yesFEBS Open Bio, 2018
Gastric cancer (GC) is one of the most prevalent cancers worldwide. Trastuzumab has been approved for the treatment of metastatic GC, gastroesophageal junction cancer, and breast cancer.
Linghe Luo, Haiyan Liu, Qian Xi
doaj   +1 more source

Trastuzumab Sensitizes Ovarian Cancer Cells to EGFR-targeted Therapeutics

open access: yesJournal of Ovarian Research, 2010
Background Early studies have demonstrated comparable levels of HER2/ErbB2 expression in both breast and ovarian cancer. Trastuzumab (Herceptin), a therapeutic monoclonal antibody directed against HER2, is FDA-approved for the treatment of both early and
Wilken Jason A   +2 more
doaj   +1 more source

Trastuzumab resistance in HER2-positive breast cancer: Mechanisms, emerging biomarkers and targeting agents

open access: yesFrontiers in Oncology, 2022
Trastuzumab is a standard molecular targeted therapy for human epidermal growth factor receptor 2(HER2) -positive breast cancer, which can significantly improve the survival of patients with this molecular subtype of breast cancer.
Zhen-hao Wang   +12 more
doaj   +1 more source

In-Trastuzumab Scintigraphy in HER2-Positive Metastatic Breast Cancer Patients Remains Feasible during Trastuzumab Treatment

open access: yesMolecular Imaging, 2014
Human epidermal growth factor receptor (HER)2 imaging with radiolabeled trastuzumab might support HER2-targeted therapy. It is, however, frequently questioned whether HER2 imaging is also possible during trastuzumab treatment as the receptor might be ...
Sietske B.M. Gaykema   +8 more
doaj   +1 more source

miR-301a-3p induced by endoplasmic reticulum stress mediates the occurrence and transmission of trastuzumab resistance in HER2-positive gastric cancer

open access: yesCell Death and Disease, 2021
Trastuzumab resistance negatively influences the clinical efficacy of the therapy for human epidermal growth factor receptor 2 (HER2) positive gastric cancer (GC), and the underlying mechanisms remain elusive.
Jing Guo   +8 more
doaj   +1 more source

circCDYL2 promotes trastuzumab resistance via sustaining HER2 downstream signaling in breast cancer

open access: yesMolecular Cancer, 2022
Background Approximate 25% HER2-positive (HER2+) breast cancer (BC) patients treated with trastuzumab recurred rapidly. However, the mechanisms underlying trastuzumab resistance remained largely unclear.
Yun Ling   +17 more
doaj   +1 more source

Hippo pathway at the crossroads of stemness and therapeutic resistance in breast cancer

open access: yesMolecular Oncology, EarlyView.
Dysregulation of the Hippo pathway drives nuclear accumulation of YAP/TAZ, activating stemness‐related transcriptional programs that sustain breast cancer stemness and fuel therapeutic resistance across subtypes, underscoring Hippo signaling as a targetable vulnerability. Figure created and edited with BioRender.com.
Giulia Schiavoni   +11 more
wiley   +1 more source

Human Blood Serum Inhibits Ductal Carcinoma Cells BT474 Growth and Modulates Effect of HER2 Inhibition

open access: yesBiomedicines, 2022
Trastuzumab, a HER2-targeted antibody, is widely used for targeted therapy of HER2-positive breast cancer (BC) patients; yet, not all of them respond to this treatment.
Dmitrii Kamashev   +7 more
doaj   +1 more source

Engineering tandem VHHs to target different epitopes to enhance antibody‐dependent cell‐mediated cytotoxicity

open access: yesFEBS Open Bio, EarlyView.
Tandem VHH targeting distinct EGFR epitopes were engineered into a monovalent bispecific antibody (7D12‐EGA1‐Fc) with more potent ADCC without increasing affinity to EGFR. Structural modeling of 7D12‐EGA1‐Fc showed cross‐linking of separate EGFR domains to enhance CD16a engagement on NK cells.
Yuqiang Xu   +5 more
wiley   +1 more source

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