Abstract: The present disclosure provides for use of variants of C-type natriuretic peptide (CNP), for the treatment of skeletal dysplasias in children, and improvement in one or more symptoms of skeletal dysplasias, such as long bone growth or growth velocity, and use in other disorders having a skeletal dysplasia and/or CNP-associated symptom or component.

Abstract: treatment of skeletal dysplasias in children, and improvement in one or more symptoms of skeletal dysplasias, such as long bone growth or growth velocity, by administering variants of C-type natriuretic peptide (CNP) is described.

Abstract: Provided herein are compounds having the formula D1-L-D2, wherein D1 is a processable group, L is a linker, and D2 is a drug. Also described herein are pharmaceutical compositions comprising said compounds and methods for the treatment of ocular diseases or disorders including glaucoma, ocular hypertension, ocular inflammation, diabetic macular edema, posterior inflammation, anterior inflammation, macular degeneration, post-cataract surgery and retinal vein occlusion.

Abstract: The present disclosure relates, in general, to measures of efficacy in patients receiving C-type natriuretic peptide (CNP) therapy to treat a skeletal dysplasia, short stature or bone-related disorders.

Abstract: The present disclosure provides for use of variants of C-type natriuretic peptide (CNP), for the treatment of skeletal dysplasias in children, and improvement in one or more symptoms of skeletal dysplasias, such as long bone growth or growth velocity, and use in other disorders having a skeletal dysplasia and/or CNP-associated symptom or component.

Abstract: A method and apparatus for generating a presentation including a device demonstration including a user interface for receiving a first user command defining a parent record including a presentation element, a first client record including the first device, and the first input, and a second client record including the second device and the second input; the user input further configured for receiving a first display command and a second display command, and a processor for generating a user interface having a first view configured including the first video content within a first graphic associated with the first device and the presentation element and coupling the first view to a display device, the processor further configured for generating a second view including the second video content within a second graphic associated with the second external device and coupling the second view to the display device.

Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).

Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).

Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming intramolecular bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, acylation, alkylation, substitution of carboxy terminal amino acids, C-terminal truncation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).

Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).

Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming intramolecular bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, acylation, alkylation, substitution of carboxy terminal amino acids, C-terminal truncation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).

Abstract: A glove or partial glove comprising a palmar portion and a dorsal portion comprising one or more finger/thumb extensions, the portions joined together at a sealed seam, the seam positioned such that the seam on each of the finger/thumb extensions is positioned adjacent the dorsal aspect of the user's finger/thumb with the palmar aspect extending over the fingertip in a hood-like configuration. The glove portions may comprise a shear-thickening-fluid (STF) treated textile base, including a multi-ply construction in which each ply comprises an STF-treated textile base. The glove may comprise an integral pathogen barrier, such as a coating that is impervious to blood and bloodborne pathogens, and may have one or more features that aids donning and/or provides an adjustable fit. The glove or partial glove may be a first glove in a glove system including at least a second, latex glove to be worn over the first glove.

Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (K-RNRNNIA) and SEQ ID NO: 28 (KRNR).

Abstract: Modified glucagon peptides are disclosed having improved solubility and/or half-life while retaining glucagon agonist activity. The glycogen peptides have been modified by substitution of native amino acids with, and/or addition of, charged amino acids to the carboxy terminus of the peptide. The modified glucagon agonists can be further modified by pegylation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 23, or both to further enhance the solubility of the glucagon agonist analogs.

Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming intramolecular bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, acylation, alkylation, substitution of carboxy terminal amino acids, C-terminal truncation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).

Abstract: Glucagon peptides with increased GIP activity are provided, optionally with GLP-I and/or glucagon activity. In some embodiments, C-terminally extended glucagon peptides comprising an amino acid sequence substantially similar to native glucagon are provided herein.

Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming intramolecular bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, acylation, alkylation, substitution of carboxy terminal amino acids, C-terminal truncation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).

Abstract: Modified glucagon peptides are disclosed having improved solubility and/or half-life while retaining glucagon agonist activity. The glycogen peptides have been modified by substitution of native amino acids with, and/or addition of, charged amino acids to the carboxy terminus of the peptide. The modified glucagon agonists can be further modified by pegylation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 23, or both to further enhance the solubility of the glucagon agonist analogs.

Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (K-RNRNNIA) and SEQ ID NO: 28 (KRNR).

Abstract: A glove comprises a hand portion and a wrist portion extending from the hand portion and terminates in a hand insertion opening. The wrist portion includes anti-roll down/anti-rucking means in the form of a band of friction enhancing material provided on a surface which, in use, will form the inside of the glove, whereby, in use, the friction enhancing portion contacts the sleeve of a garment worn by the user so as to increase friction against the wrist portion of the glove, thereby preventing roll-down/rucking of the glove. The friction enhancing material is applied prior to any finishing operation(s) which reduce(s) the residual tack of the glove material and is selected from a group of materials whose tack is substantially unaffected by the finishing operation.