Compositions and methods are provided for genetically modifying cells to guide in situ chemical synthesis of electroactive, conductive, or insulating polymers on plasma membranes, organelle membranes, or subcellular surfaces of cells. In particular, compositions and methods are provided for genetically modifying excitable cells such as neurons, muscle cells, and endocrine cells to guide in situ chemical synthesis of polymers on the extracellular side of the plasma membrane. The subject methods can be used in various applications, for example, to assemble polymers in vivo at targeted locations to modulate electrical conduction and create new electrical conduction pathways, allow cell-type-specific neuromodulation, provide a conductive structure on cells for connection to electrodes, sensors, or other external electronic and electrochemical devices, and create a durable structure to replace damaged tissue for use in regenerative medicine.

Provided are recombinant plasmids containing the gene of the heterodimeric snake venom protein Agkisacutacin A chain and Agkisacutacin B chain, cell strains containing the recombinant plasmids, and a method for expressing the heterodimeric snake venom protein Agkisacutacin. The expression level of Agkisacutacin in the present method exceeds 10 mg/L, and the purity level can reach more than 95% by means of two steps of purification.

Provided are recombinant plasmids containing the gene of the heterodimeric snake venom protein Agkisacutacin A chain and Agkisacutacin B chain, cell strains containing the recombinant plasmids, and a method for expressing the heterodimeric snake venom protein Agkisacutacin. The expression level of Agkisacutacin in the present method exceeds 10 mg/L, and the purity level can reach more than 95% by means of two steps of purification.

The present application provides fibers made from recombinant hagfish intermediate filament proteins. Methods of expressing and purifying the proteins, and methods of creating the fibers, are likewise disclosed. The method of purifying protein yields larger quantities of hagfish protein than have been previously achieved, and the fibers have the highest mechanical properties yet recorded for recombinant hagfish protein fibers.

The present invention provides a chimeric cytokine receptor (CCR) comprising: (i) an exodomain which binds to a ligand selected from a tumour secreted factor, a chemokine and a cell-surface antigen; and (ii) a cytokine receptor endodomain.

The present invention provides a chimeric cytokine receptor (CCR) comprising: (i) an exodomain which binds to a ligand selected from a tumour secreted factor, a chemokine and a cell-surface antigen; and (ii) a cytokine receptor endodomain.

Provided herein, in some embodiments, are engineered phagemids that comprise at least one synthetic genetic circuit, wherein the at least one synthetic genetic circuit comprises gene sequences encoding at least one non-lytic antimicrobial peptides (AMPs) and/or antibacterial toxin proteins, a stable origin of replication, and a bacteriophage-packaging signal, wherein the engineered phagemid does not comprise some or all gene sequences encoding bacteriophage proteins required for assembly of a bacteriophage particle.

The present invention provides a recombinant sequence information of a key host factor ANP32A/B which is necessary for the replication of influenza virus in a host. More specifically, the present invention relates to a 129-130 motif and a 149 site of the host factor ANP32A/B protein, which are key active sites for exerting its ability to promote the replication of influenza virus, and are also potential targeting sites of anti-influenza drugs.

Fusion proteins containing a half-life extension protein, a linker, and a GDF15 protein are described. Also described are nucleic acids encoding the fusion proteins, recombinant cells thereof, compositions comprising the fusion proteins, and methods of using the fusion proteins for treating or preventing metabolic diseases, disorders or conditions.

This disclosure features structurally-stabilized oncolytic peptides and related compositions and methods of making same. Also disclosed are methods of using such structurally-stabilized peptides in the treatment of cancer, e.g., a hematological cancer, e.g., a leukemia, a lymphoma, or multiple myeloma, and/or in the inhibition of proliferation of a cancer cell, e.g., a hematological cancer, e.g., a leukemia and/or a lymphoma and/or a multiple myeloma cell. Also disclosed are methods of using such structurally-stabilized peptides for killing cancer cells or dual-killing cancer cell and micro-organisms, and thus providing therapeutics to treat cancer with or without simultaneously preventing or treating infection, while avoiding toxicity to normal, non-cancerous cells.