Abstract: In an example embodiment, a selection of an image in a user interface is received. Then information about the image is received. Then a look is identified for the image, wherein the look is a category for the image based at least in part on one or more visual attributes of the image as shown in the image The identified look is then compared with one or more item listings stored in a database to identify one or more matching item listings, the one or more matching item listings containing associated images that correspond to the look. Finally, the one or more matching item listings are displayed in the user interface.

Abstract: In an example embodiment, a selection of an image in a user interface is received. Then information about the image is received. Then a look is identified for the image, wherein the look is a category for the image based at least in part on one or more visual attributes of the image as shown in the image The identified look is then compared with one or more item listings stored in a database to identify one or more matching item listings, the one or more matching item listings containing associated images that correspond to the look. Finally, the one or more matching item listings are displayed in the user interface.

Abstract: In an example embodiment, a selection of an image in a user interface is received. Then information about the image is received. Then a look is identified for the image, wherein the look is a category for the image based at least in part on one or more visual attributes of the image as shown in the image The identified look is then compared with one or more item listings stored in a database to identify one or more matching item listings, the one or more matching item listings containing associated images that correspond to the look. Finally, the one or more matching item listings are displayed in the user interface.

Abstract: The crystal structure at 2.16 ? resolution of the full-length bacterial bifunctional transglycosylase penicillin-binding protein 1b (PBP1b) from Escherichia coli, in complex with its inhibitor moenomycin, is provided. The atomic coordinates of the complex as well as the moenomycin binding site are provided. Three dimensional structures of amino acid residues involved in moenomycin binding and transglycosylation activity are identified. Binding site for peptidoglycan synthesis inhibitors comprising inhibitor-binding site comprises amino acid residues from at least one of transglycosylase (TG), UvrB domain 2 homolog (UB2H) and transmembrane (TM) domains of PBP1b are identified at an atomic level of resolution. Methods for rational drug design based on the atomic coordinates are provided. Methods for screening for antibiotics based on anisotropic binding assay and transglycosylase inhibitor assays are provided. Novel antibiotics based on the screening assays of the invention are disclosed.

Abstract: A Schottky source-gated thin film transistor is provided including: a drain contact; an insulating substrate; a source contact made of a Schottky metal; a channel connecting the buried source contact to the drain, the channel made of ZnO; and a Schottky source barrier formed between the source contact and the channel; and a gate; wherein the source contact is positioned below the channel.

Abstract: A Schottky source-gated thin film transistor is provided including: a drain contact; an insulating substrate; a source contact made of a Schottky metal; a channel connecting the buried source contact to the drain, the channel made of ZnO; and a Schottky source barrier formed between the source contact and the channel; and a gate; wherein the source contact is positioned below the channel.

Abstract: The crystal structure at 2.16 ? resolution of the full-length bacterial bifunctional transglycosylase penicillin-binding protein 1b (PBP1b) from Escherichia coli, in complex with its inhibitor moenomycin, is provided. The atomic coordinates of the complex as well as the moenomycin binding site are provided. Three dimensional structures of amino acid residues involved in moenomycin binding and transglycosylation activity are identified. Binding site for peptidoglycan synthesis inhibitors comprising inhibitor-binding site comprises amino acid residues from at least one of transglycosylase (TG), UvrB domain 2 homolog (UB2H) and transmembrane (TM) domains of PBP1b are identified at an atomic level of resolution. Methods for rational drug design based on the atomic coordinates are provided. Methods for screening for antibiotics based on anisotropic binding assay and transglycosylase inhibitor assays are provided. Novel antibiotics based on the screening assays of the invention are disclosed.

Abstract: In an example embodiment, a selection of an image in a user interface is received. Then information about the image is received. Then a look is identified for the image, wherein the look is a category for the image based at least in part on one or more visual attributes of the image as shown in the image The identified look is then compared with one or more item listings stored in a database to identify one or more matching item listings, the one or more matching item listings containing associated images that correspond to the look. Finally, the one or more matching item listings are displayed in the user interface.

Abstract: Moenomycin inhibits bacterial growth by clocking the transglycosylase activity of class A penicillin-binding proteins (PBPs), which are key enzymes in bacterial cell wall synthesis. The binding affinities of moenomycin A with various truncated PBPs were compared showing that the transmembrane domain is important for moenomycin binding. Full-length class-A PBPs from 16 bacterial species were produced, and their binding activities showed a correlation with the antimicrobial activity of moenomycin against Enterococcus faecalis and Staphylococcus aureus. Moreover, a fluorescence anisotropy-based high-throughput assay was developed and used successfully for identification of transglycosylase inhibitors.

Abstract: Crystal structure at 2.16 ? resolution of full-length Escherichia coli penicillin-binding protein 1b (PBP1b) in complex with its inhibitor moenomycin, is provided. 3D structures of amino acid residues involved in moenomycin binding and transglycosylation activity are identified. Binding sites for peptidoglycan synthesis inhibitors comprising amino acid residues from transglycosylase (TG), UvrB domain 2 homolog (UB2H) and transmembrane (TM) domains of PBP1b are identified at atomic level resolution. Rational drug design, based on the atomic coordinates, are disclosed. Methods for screening for antibiotics using anisotropic binding and transglycosylase inhibitor assays and novel antibiotics based on the screening assays are provided.

Abstract: Moenomycin inhibits bacterial growth by clocking the transglycosylase activity of class A penicillin-binding proteins (PBPs), which are key enzymes in bacterial cell wall synthesis. The binding affinities of moenomycin A with various truncated PBPs were compared showing that the transmembrane domain is important for moenomycin binding. Full-length class-A PBPs from 16 bacterial species were produced, and their binding activities showed a correlation with the antimicrobial activity of moenomycin against Enterococcus faecalis and Staphylococcus aureus. Moreover, a fluorescence anisotropy-based high-throughput assay was developed and used successfully for identification of transglycosylase inhibitors.

Abstract: The crystal structure at 2.16 ? resolution of the full-length bacterial bifunctional transglycosylase penicillin-binding protein 1b (PBP1b) from Escherichia coli, in complex with its inhibitor moenomycin, is provided. The atomic coordinates of the complex as well as the moenomycin binding site are provided. Three dimensional structures of amino acid residues involved in moenomycin binding and transglycosylation activity are identified. Binding site for peptidoglycan synthesis inhibitors comprising inhibitor-binding site comprises amino acid residues from at least one of transglycosylase (TG), UvrB domain 2 homolog (UB2H) and transmembrane (TM) domains of PBP1b are identified at an atomic level of resolution. Methods for rational drug design based on the atomic coordinates are provided. Methods for screening for antibiotics based on anisotropic binding assay and transglycosylase inhibitor assays are provided. Novel antibiotics based on the screening assays of the invention are disclosed.

Abstract: Moenomycin inhibits bacterial growth by clocking the transglycosylase activity of class A penicillin-binding proteins (PBPs), which are key enzymes in bacterial cell wall synthesis. The binding affinities of moenomycin A with various truncated PBPs were compared showing that the transmembrane domain is important for moenomycin binding. Full-length class-A PBPs from 16 bacterial species were produced, and their binding activities showed a correlation with the antimicrobial activity of moenomycin against Enterococcus faecalis and Staphylococcus aureus. Moreover, a fluorescence anisotropy-based high-throughput assay was developed and used successfully for identification of transglycosylase inhibitors.