Abstract: Systems, devices, and methods are operable to track usage of a surgical instrument and modify the performance of the surgical instrument based on the prior usage of the surgical instrument. Some surgical instruments are designed to have a limited service life beginning at their first use, or a limit to their overall usage in order to ensure safe use of the sensitive instruments. However, a lack of ability to track usage characteristics when the instrument is separated from an external power supply allows for user abuse and avoidance of such safety mechanisms. Adding a battery or capacitor to the instrument may allow for an ability to track usage when the instrument is separated from an external power supply. Implementing special user prompts, device use ratios, and device use half-life upon powering down of an instrument may additionally be used to prevent circumvention of safety features.

Abstract: The present invention relates to the photoredox-mediated functionalization of proteins with chemical groups via radical generated C—C bond formation, by using specific boronate and sulfone precursor compounds. The present invention also relates to functionalized proteins that can be generated via this method and to the specific boronate and sulfone precursor compounds themselves.

Abstract: Described herein are antibody conjugates and methods of making antibody conjugates.

Abstract: A process for the production of a glycoconjugate by N-glycosylation of a protein or peptide comprising the sequence D/E-X-N-X-S/T (SEQ ID NO:1), wherein each X is the same or different and is any natural amino acid other than proline, wherein the process comprises reacting the protein or peptide with a polyisoprenyl pyrophosphate of formula (I), or a salt thereof, in the presence of PglB: to produce the glycoconjugate comprising the protein or peptide having a saccharide [S1] linked to the asparagine in the sequence D/E-X-N-X-S/T (SEQ ID NO:1). Polyisoprenylpyrophosphates used as substrates in the biocatalytic process are also provided, as well as certain glycoconjugates.

Abstract: Compounds which inhibit Wza-mcdiated polysaccharide transport are useful in the prevention or treatment of bacterial infection, in particular of E. coli infection. The compounds are typically cyclic oligosaccharides such as cyclodextrins, which bear positively charged functional groups at the primary carbon position.

Abstract: Described herein are antibody conjugates and methods of making antibody conjugates.

Abstract: A process for the production of a glycoconjugate by N-glycosylation of a protein or peptide comprising the sequence D/E-X—N—X—S/T, wherein each X is the same or different and is any natural amino acid other than proline, wherein the process comprises reacting the protein or peptide with a polyisoprenyl pyrophosphate of formula (I), or a salt thereof, in the presence of PglB: (I) to produce the glycoconjugate comprising the protein or peptide having a saccharide [SI] linked to the asparagine in the sequence D/E-X—N—X—S/T. Polyisoprenylpyrophosphates used as substrates in the biocatalytic process are also provided, as well as certain glycoconjugates.

Abstract: Compounds which are trehalose-6-phosphate or trehalose-6-phosphonate precursors of formula (I) or agriculturally acceptable salts thereof are provided: (I) The compounds are useful in increasing starch production in plants.

Abstract: Compounds which inhibit Wza-mcdiated polysaccharide transport are useful in the prevention or treatment of bacterial infection, in particular of E. coli infection. The compounds are typically cyclic oligosaccharides such as cyclodextrins, which bear positively charged functional groups at the primary carbon position.

Abstract: Compounds which are trehalose-6-phosphate or trehalose-6-phosphonate precursors of formula (I) or agriculturally acceptable salts thereof are provided: (I) The compounds are useful in increasing starch production in plants.

Abstract: This invention provides chimeric molecules that are catalytic antagonists of a target molecule. The catalytic antagonists of this invention preferably comprise a targeting moiety attached to an enzyme that degrades the molecule specifically bound by the targeting moiety. The catalytic antagonists of this invention thus bind to a target recognized by the targeting moiety (e.g., a receptor) the enzyme component of the chimera then degrades all or part of the target. This typically results in a reduction or loss of activity of the target and release of the chimeric molecule. The chimeric molecule is then free to attack and degrade another target molecule.

Abstract: This invention provides chimeric molecules that are catalytic antagonists of a target molecule. The catalytic antagonists of this invention preferably comprise a targeting moiety attached to an enzyme that degrades the molecule specifically bound by the targeting moiety. The catalytic antagonists of this invention thus bind to a target recognized by the targeting moiety (e.g., a receptor) the enzyme component of the chimera then degrades all or part of the target. This typically results in a reduction or loss of activity of the target and release of the chimeric molecule. The chimeric molecule is then free to attack and degrade another target molecule.

Abstract: A modified polypeptide having carbohydrate processing enzymatic activity is provided, said polypeptide comprising an amino acid sequence selected from: (a) the amino acid sequence of SEQ ID NO:2 comprising a mutation in at least one of W433, E432 and M439; (b) the amino acid sequence of an enzyme of glycosyl hydrolase family 1, comprising at least one mutation at an amino acid residue equivalent to W433, E432 or M439 of SEQ ID NO:2; and (c) a variant of (a) or (b) having carbohydrate processing enzymatic activity and comprising at least one amino acid mutation at a position equivalent to W433, E432 or M439 of SEQ ID NO:2.

Abstract: A modified polypeptide having carbohydrate processing enzymatic activity is provided, said polypeptide comprising an amino acid sequence selected from: (a) the amino acid sequence of SEQ ID NO:2 comprising a mutation in at least one of W433, E432 and M439; (b) the amino acid sequence of an enzyme of glycosyl hydrolase family 1, comprising at least one mutation at an amino acid residue equivalent to W433, E432 or M439 of SEQ ID NO:2; and (c) a variant of (a) or (b) having carbohydrate processing enzymatic activity and comprising at least one amino acid mutation at a position equivalent to W433, E432 or M439 of SEQ ID NO:2.

Abstract: The present invention is directed to glyodendrimeric proteases, composition with glycodendrimeric proteases and methods for inhibiting adhesion binding in microorganisms by contacting microorganisms with a glycodendrimeric protease or a composition with a glycodendrimeric protease. The invention may be used to treat patients in need of treatment.

Abstract: This invention provides modified enzymes comprising one or more amino acid residues replaced by cysteine residues, where the cysteine residues are modified by replacing the thiol hydrogen in the cysteine residues with a substituent group providing a thiol side chain comprising a multiply charged moiety. The enzymes show improved interaction and/or specificity and/or activity with charged substrates.

Abstract: The present invention relates to a chemically modified mutant protein including a cysteine residue substituted for a residue other than cysteine in a precursor protein, the substituted cysteine residue being subsequently modified by reacting the cysteine residue with a glycosylated thiosulfonate. Also, a method of producing the chemically modified mutant protein is provided. The present invention also relates to a glycosylated methanethiosulfonate. Another aspect of the present invention is a method of modifying the functional characteristics of a protein including providing a protein and reacting the protein with a glycosylated methanethiosulfonate reagent under conditions effective to produce a glycoprotein with altered functional characteristics as compared to the protein. In addition, the present invention relates to methods of determining the structure-function relationships of chemically modified mutant proteins.

Abstract: This invention provides chimeric molecules that are catalytic antagonists of a target molecule. The catalytic antagonists of this invention preferably comprise a targeting moiety attached to an enzyme that degrades the molecule specifically bound by the targeting moiety. The catalytic antagonists of this invention thus bind to a target recognized by the targeting moiety (e.g., a receptor) the enzyme component of the chimera then degrades all or part of the target. This typically results in a reduction or loss of activity of the target and release of the chimeric molecule. The chimeric molecule is then free to attack and degrade another target molecule.

Abstract: The present invention is directed to glyodendrimeric proteases, composition with glycodendrimeric proteases and methods for inhibiting adhesion binding in microorganisms by contacting microorganisms with a glycodendrimeric protease or a composition with a glycodendrimeric protease. The invention may be used to treat patients in need of treatment.

Abstract: The present invention relates to a chemically modified mutant protein including a cysteine residue substituted for a residue other than cysteine n a precursor protein, the substituted cysteine residue being subsequently modified by reacting the cysteine residue with a glycosylated thiosulfonate. Also a method of producing the chemically modified mutant protein is provided. The present invention also relates to a glycosylated methanethiosulfonate. Another aspect of the present invention is a method of modifying the functional characteristics of a protein including providing a protein and reacting the protein with a glycosylated methanethiosulfonate reagent under conditions effective to produce a glycoprotein with altered functional characteristics as compared to the protein. In addition, the present invention relates to methods of determining the structure-function relationships of chemically modified mutant proteins.