Cyclic-GMP-AMP synthase (cGAS) and cyclic-GMP-AMP (cGAMP), including 23-cGAMP, 22-cGAMP, 32-cGAMP and 33-GAMP, are used in pharmaceutical formulations (including vaccine adjuvants), drug screens, therapies, and diagnostics.

Cyclic-GMP-AMP synthase (cGAS) and cyclic-GMP-AMP (cGAMP), including 23-cGAMP, 22-cGAMP, 32-cGAMP and 33-GAMP, are used in pharmaceutical formulations (including vaccine adjuvants), drug screens, therapies, and diagnostics.

This disclosure provides systems and methods for sequencing nucleic acids using nucleotide analogues and translocation of tags from incorporated nucleotide analogues through a nanopore. In aspects, this disclosure is related to composition, method, and system for sequencing a nucleic acid using tag molecules and detection of translocation through a nanopore of tags released from incorporation of the molecule.

Cyclic-GMP-AMP synthase (cGAS) and cyclic-GMP-AMP (cGAMP), including 23-cGAMP, 22-cGAMP, 32-cGAMP and 33-GAMP, are used in pharmaceutical formulations (including vaccine adjuvants), drug screens, therapies, and diagnostics.

Provided are SpdE polypeptides and variants and nucleic acids encoding the SpdE polypeptides and variants. Also provided are vectors including one or more nucleic acids encoding a SpdE polypeptide or variant and cells including a nucleic acid encoding the SpdE polypeptide or variant, as well as cells expressing a SpdE polypeptide or variant and compositions including such cells and a pharmaceutically acceptable carrier. Finally, methods of detecting presence and/or amount of one or more amino acids in a sample are provided. The methods include contacting the sample with a SpdE protein, measuring diguanylate cyclase activity of the SpdE protein; and comparing the diguanylate cyclase activity of the SpdE protein to a control. The methods can utilize isolated SpdE protein or a cell expressing a SpdE protein.

Cyclic-GMP-AMP synthase (cGAS) and cyclic-GMP-AMP (cGAMP), including 23-cGAMP, 22-cGAMP, 32-cGAMP and 33-GAMP, are used in pharmaceutical formulations (including vaccine adjuvants), drug screens, therapies and diagnostics.

The present invention relates to a fusion protein consisting of a C2 domain and an Akt protein fragment, particularly the fragment consisting of the amino acid residues ranging from the 111.sup.th to the 480.sup.th amino acids from the N-terminus of the Akt protein, and a use of the said fusion protein. More specifically, the fusion protein of the present invention increases the Akt protein activity even under the condition of high calcium concentration, reduces body weight and fat in an animal model treated with a high fat diet infected with adenovirus containing the fusion protein above, improves insulin resistance and improves fatty liver, so that the fusion protein comprising the C2 domain and the fragment consisting of the amino acid residues ranging from the 111.sup.th to 480.sup.th amino acids from the N-terminus of Akt protein can be effectively used for the treatment of metabolic disease.

A transgenic knockout non-human animal is described whose genome includes a heterozygous disruption of the expression of at least one endogenous gene encoding zinc-finger, CCHC domain-containing protein 6 (ZCCHC6). The transgenic animal model can be used to study bone disease or development by determining differences in bone characteristics, protein expression, or cytokine expression in the animal model in comparison to a corresponding wild-type non-human animal.

This disclosure provides systems and methods for sequencing nucleic acids using nucleotide analogues and translocation of tags from incorporated nucleotide analogues through a nanopore. In aspects, this disclosure is related to composition, method, and system for sequencing a nucleic acid using tag molecules and detection of translocation through a nanopore of tags released from incorporation of the molecule.

The present invention provides an in vitro method for monitoring interphase nuclear envelope rupture events in a eukaryotic cell or screening or identifying compound capable of increasing or decreasing the intensity and/or frequency of interphase nuclear envelope rupture events in a eukaryotic cell. These methods relate on a protein having a cytosolic non-nuclear localization in interphase and a non-sequence specific DNA binding activity. Interphase nuclear envelope rupture events are characterized by the presence of the protein of the invention in the nucleus of the eukaryotic cell.