GPRC5D-targeting bispecifics bridge myeloma cells and T-cells, resolving specificity gaps in existing therapies.
A miRNA expression construct uses a 50-nucleotide spacer to enhance DROSHA processing and mature miRNA production.
Tandemly repeated antibody-binding proteins increase capture antibody loading on solid supports, resolving limited binding site availability in immunoassays.
Mutated carbonic anhydrases replace energy-intensive MEA scrubbing, enabling efficient CO2 capture with reduced thermal degradation.
A cyclic cell-penetrating peptide conjugated with an endosomal escape vehicle enables intracellular delivery of antisense compounds.
Segmented antibody structures with modified Fc regions extend half-lives while protease cleavage sites prevent lymphopenia.
Expressing human LAG-3 in animal models resolves species differences that cause high failure rates in traditional drug development pipelines.
Chimeric antigen receptors target Sialyl Tn glycan to inhibit tumor growth while sparing normal tissues with low antigen expression.
Virus-like nanoparticles display SARS-CoV-2 spike protein domains to induce high-titer neutralizing antibody responses.
A segmented polypeptide inhibitor disrupts transcription factor binding to nuclear speckles.
Genetically modified T cells use chimeric antigen receptors to target SSEA4, overcoming chemotherapy resistance in ovarian cancer.
A PDGFR-VEGFR fusion protein acts as a decoy receptor to bind VEGF and PDGF simultaneously.
Engineered T cells express chimeric antigen receptors only in hypoxic tumor environments to target CD138-positive cancer cells.
RSPO3-binding agents inhibit tumor growth by blocking RSPO3-LGR interactions, reducing cancer stem cell frequency and angiogenesis.
Engineered fully human T-cell receptors redirect CD4 and CD8 T-cells to recognize hTERT peptides presented by Class II MHC molecules.
Segmenting the CAR into distinct antigen binding domains resolves the contradiction between long-term maintenance and solid tumor efficacy.
Masked EpCAM trispecific proteins reduce off-target side effects by requiring tumor-associated protease cleavage for selective cancer cell targeting.
Antibodies target MUC16 peptide backbone to resolve low sensitivity and specificity limits in current cancer screening methods.