The present invention relates to fusion proteins for the expression of G-protein coupled receptor proteins (GPCR) with the fusion partners, as inserted fragments, from mammalian cells. The fusion partners are from a fragment of APJ protein (the APJ protein fragment) or a fragment with homology of more than 90% similarity to the APJ protein fragment; or a fragment of RGS16 protein (the RGS16 protein fragment) or a fragment with homology of more than 90% similarity to the RGS16 protein fragment; or the fragment of DNJ protein (the DNJ protein fragment) or a fragment with homology of more than 90% similarity to DNJ protein fragment. The fusion expression of GPCR with the above mentioned fusion partners can improve the protein yield and stability when purified from cells. Therefore, these fusion protein partners can be widely used for the study of GPCR proteins.

HNOX proteins are mutated to exhibit improved or optimal kinetic and thermodynamic properties for blood gas O.sub.2 delivery. The engineered HNOX proteins comprise mutations that impart altered O.sub.2 or NO ligand-binding relative to the corresponding wild-type HNOX domain, and are operative as physiologically compatible mammalian blood O.sub.2 gas carriers. The invention also provides pharmaceutical compositions, kits, and methods that use wild-type or mutant HNOX proteins for the treatment of any condition for which delivery of O.sub.2 is beneficial.

The present invention relates to fusion proteins for the expression of G-protein coupled receptor proteins (GPCR) with the fusion partners, as inserted fragments, from mammalian cells. The fusion partners are from a fragment of APJ protein (the APJ protein fragment) or a fragment with homology of more than 90% similarity to the APJ protein fragment; or a fragment of RGS16 protein (the RGS16 protein fragment) or a fragment with homology of more than 90% similarity to the RGS16 protein fragment; or the fragment of DNJ protein (the DNJ protein fragment) or a fragment with homology of more than 90% similarity to DNJ protein fragment. The fusion expression of GPCR with the above mentioned fusion partners can improve the protein yield and stability when purified from cells. Therefore, these fusion protein partners can be widely used for the study of GPCR proteins.

The present invention relates to fusion proteins for the expression of G-protein coupled receptor proteins (GPCR) with the fusion partners, as inserted fragments, from mammalian cells. The fusion partners are from a fragment of APJ protein (the APJ protein fragment) or a fragment with homology of more than 90% similarity to the APJ protein fragment; or a fragment of RGS16 protein (the RGS16 protein fragment) or a fragment with homology of more than 90% similarity to the RGS16 protein fragment; or the fragment of DNJ protein (the DNJ protein fragment) or a fragment with homology of more than 90% similarity to DNJ protein fragment. The fusion expression of GPCR with the above mentioned fusion partners can improve the protein yield and stability when purified from cells. Therefore, these fusion protein partners can be widely used for the study of GPCR proteins.

The present invention relates to fusion proteins for the expression of G-protein coupled receptor proteins (GPCR) with the fusion partners, as inserted fragments, from mammalian cells. The fusion partners are from a fragment of APJ protein (the APJ protein fragment) or a fragment with homology of more than 90% similarity to the APJ protein fragment; or a fragment of RGS16 protein (the RGS16 protein fragment) or a fragment with homology of more than 90% similarity to the RGS16 protein fragment; or the fragment of DNJ protein (the DNJ protein fragment) or a fragment with homology of more than 90% similarity to DNJ protein fragment. The fusion expression of GPCR with the above mentioned fusion partners can improve the protein yield and stability when purified from cells. Therefore, these fusion protein partners can be widely used for the study of GPCR proteins.

A novel class of transporter protein, referred to as SWEET, GLUE or Gl, is disclosed. These transporters provide a novel system for the transportation of sugars across membranes within a cell and between the inside and outside of a cell. Such transporters are useful for understanding and altering the sugar concentration within certain organs of an organism, and within certain organelles within the cell. These transporters are also useful in protecting plants from a pathogen attack.

A recombinant polypeptide is described which comprises at least one PUF RNA-binding domain capable of specifically binding to a cytosine RNA base. The PUF RNA-binding domain of the polypeptide comprises at least one RNA base-binding motif of the general formula X.sub.1X.sub.2X.sub.3X.sub.4X.sub.5X.sub.6X.sub.7X.sub.8X.sub.9X.sub.10X.sub.11 wherein X.sub.1 is selected from the group including glutamine (Q), valine (V), methionine (M), proline (P), glutamic acid (E), and lysine (K); X.sub.2 is selected from the group including histidine (H), phenylalanine (F), tyrosine (Y), and asparagine (N); X.sub.3 is selected from the group including glycine (G) and alanine (A); X.sub.4 is selected from the group including glycine (G), alanine (A), serine (S), threonine (T) and cysteine (C); X.sub.5 is selected from the group including arginine (R), tyrosine (Y), histidine (H), and asparagine (N); X.sub.6 is selected from the group including phenylalanine (F), leucine (L), and valine (V); X.sub.7 is selected from the group including isoleucine (I), leucine (L), and valine (V); X.sub.8 is arginine (R); X.sub.9 is selected from the group including leucine (L), lysine (K), arginine (R), glutamine (Q), and histidine (H); X.sub.10 is selected from the group including lysine (K), phenylalanine (F), alanine (A), cysteine (C), isoleucine (I), valine (V), leucine (L), and methionine (M); and X.sub.11 is selected from the group including leucine (L), phenylalanine (F), isoleucine (I), and valine (V); and wherein the RNA base-binding motif is operably capable of specifically binding to a cytosine RNA base.

Described herein are compositions including filamentous fungal cells, such as Trichoderma fungal cells, having reduced protease activity and expressing fucosylation pathway. Further described herein are methods for producing a glycoprotein having fucosylated N-glycan, using genetically modified filamentous fungal cells, for example, Trichoderma fungal cells, as the expression system.

The present invention relates to fusion proteins for the expression of G-protein coupled receptor proteins (GPCR) with the fusion partners, as inserted fragments, from mammalian cells. The fusion partners are from a fragment of APJ protein (the APJ protein fragment) or a fragment with homology of more than 90% similarity to the APJ protein fragment; or a fragment of RGS16 protein (the RGS16 protein fragment) or a fragment with homology of more than 90% similarity to the RGS16 protein fragment; or the fragment of DNJ protein (the DNJ protein fragment) or a fragment with homology of more than 90% similarity to DNJ protein fragment. The fusion expression of GPCR with the above mentioned fusion partners can improve the protein yield and stability when purified from cells. Therefore, these fusion protein partners can be widely used for the study of GPCR proteins.

There are provided methods and compositions useful in cell-cell fusion using Fusion Family (FF) proteins of nematode origin. There are further provided antinematodal methods and compositions, utilizing fusogenic proteins of the nematode Fusion Family.