Abstract: The present invention concerns antigen binding proteins and fragments thereof which specifically bind Oncostatin M (OSM), particularly human OSM (hOSM) and which inhibit the binding of OSM to the gp130 receptor but does not directly interact with site II residues. The invention also concerns a method of humanising antibodies. Further disclosed are pharmaceutical compositions, screening and medical treatment methods.

Abstract: The present invention concerns antigen binding proteins and fragments thereof which specifically bind Oncostatin M (OSM), particularly human OSM (hOSM) and which inhibit the binding of OSM to the gp130 receptor but does not directly interact with site II residues. The invention also concerns a method of humanizing antibodies. Further disclosed are pharmaceutical compositions, screening and medical treatment methods.

Abstract: The present disclosure relates to TSLP binding proteins that interact with particular residues of human full length TSLP, or contact particular regions of human full length TSLP. The invention also includes pharmaceutical compositions and medical uses of these TSLP binding proteins.

Abstract: A process for the identification of compounds with a molecular weight in the range 100 to 750 which inhibit the binding of the first and/or second bromodomains of human BRD-2 to 4 to acetylated lysine residues of their physiological partner proteins which comprises selecting those compounds which are able to: a) form a hydrogen bonding interaction in which the compound accepts a hydrogen bond from the sidechain NH2 group of the asparagine residue found at: BRD-2 BRD-2 BRD-3 BRD-3 BRD-4 BRD-4 BD1 BD2 BD1 BD2 BD1 BD2 ASN156 ASN429 ASN116 ASN391 ASN140 ASN433 or b) accept a water-mediated hydrogen bond in which the compound accepts a hydrogen bond from a water that is itself hydrogen-bonded to the sidechain hydroxyl of the tyrosine residue found at BRD-2 BRD-2 BRD-3 BRD-3 BRD-4 BRD-4 BD1 BD2 BD1 BD2 BD1 BD2 TYR113 TYR386 TYR73 TYR348 TYR97 TYR390 and c) which are also able to form a Van der Waals interaction with a lipophi

Abstract: The present invention concerns antigen binding proteins and fragments thereof which specifically bind Oncostatin M (OSM), particularly human OSM (hOSM) and which inhibit the binding of OSM to the gp130 receptor but does not directly interact with site II residues. The invention also concerns a method of humanising antibodies. Further disclosed are pharmaceutical compositions, screening and medical treatment methods.

Abstract: The present invention concerns antigen binding proteins and fragments thereof which specifically bind Oncostatin M (OSM), particularly human OSM (hOSM) and which inhibit the binding of OSM to the gp130 receptor but does not directly interact with site II residues. The invention also concerns a method of humanizing antibodies. Further disclosed are pharmaceutical compositions, screening and medical treatment methods.

Abstract: A process for the identification of compounds with a molecular weight in the range 100 to 750 which inhibit the binding of the first and/or second bromodomains of human BRD-2 to 4 to acetylated lysine residues of their physiological partner proteins which comprises selecting those compounds which are able to: a) form a hydrogen bonding interaction in which the compound accepts a hydrogen bond from the sidechain NH2 group of the asparagine residue found at: BRD-2 BRD-2 BRD-3 BRD-3 BRD-4 BRD-4 BD1 BD2 BD1 BD2 BD1 BD2 ASN156 ASN429 ASN116 ASN391 ASN140 ASN433 or b) accept a water-mediated hydrogen bond in which the compound accepts a hydrogen bond from a water that is itself hydrogen-bonded to the sidechain hydroxyl of the tyrosine residue found at BRD-2 BRD-2 BRD-3 BRD-3 BRD-4 BRD-4 BD1 BD2 BD1 BD2 BD1 BD2 TYR113 TYR386 TYR73 TYR348 TYR97 TYR390 and c) which are also able to form a Van der Waals interaction with a lipophi

Abstract: A process for the identification of compounds with a molecular weight in the range 100 to 750 which inhibit the binding of the first and/or second bromodomains of human BRD-2 to 4 to acetylated lysine residues of their physiological partner proteins which comprises selecting those compounds which are able to: a) form a hydrogen bonding interaction in which the compound accepts a hydrogen bond from the sidechain NH2 group of the asparagine residue found at: BRD-2 BRD-2 BRD-3 BRD-4 BRD-4 BD1 BD2 BD1 BRD-3 BD2 BD1 BD2 ASN156 ASN429 ASN116 ASN391 ASN140 ASN433 or b) accept a water-mediated hydrogen bond in which the compound accepts a hydrogen bond from a water that is itself hydrogen-bonded to the sidechain hydroxyl of the tyrosine residue found at BRD-2 BRD-3 BRD-4 BD1 BRD-2 BD2 BD1 BRD-3 BD2 BD1 BRD-4 BD2 TYR113 TYR386 TYR73 TYR348 TYR97 TYR390 and c) which are also able to form a Van der Waals interaction with a lipophilic

Abstract: The use of compounds in the treatment of autoimmune and inflammatory diseases or conditions, pharmaceutical compositions containing such compounds and to methods for identifying compounds for use in the treatment of such diseases or conditions.

Abstract: The present invention concerns antigen binding proteins and fragments thereof which specifically bind Oncostatin M (OSM), particularly human OSM (hOSM) and which inhibit the binding of OSM to the gp130 receptor but does not directly interact with site II residues. The invention also concerns a method of humanising antibodies. Further disclosed are pharmaceutical compositions, screening and medical treatment methods.

Abstract: The present invention concerns antigen binding proteins and fragments thereof which specifically bind Oncostatin M (OSM), particularly human OSM (hOSM) and which inhibit the binding of OSM to the gp130 receptor but does not directly interact with site II residues. The invention also concerns a method of humanizing antibodies. Further disclosed are pharmaceutical compositions, screening and medical treatment methods.

Abstract: The present invention concerns antigen binding proteins and fragments thereof which specifically bind Oncostatin M (OSM), particularly human OSM (hOSM) and which inhibit the binding of OSM to the gp130 receptor but does not directly interact with site II residues. The invention also concerns a method of humanising antibodies. Further disclosed are pharmaceutical compositions, screening and medical treatment methods.

Abstract: A process for the identification of compounds with a molecular weight in the range 100 to 750 which inhibit the binding of the first and/or second bromodomains of human BRD-2 to 4 to acetylated lysine residues of their physiological partner proteins which comprises selecting those compounds which are able to: a) form a hydrogen bonding interaction in which the compound accepts a hydrogen bond from the sidechain NH2 group of the asparagine residue found at: BRD-2 BRD-2 BRD-3 BRD-4 BRD-4 BD1 BD2 BD1 BRD-3 BD2 BD1 BD2 ASN156 ASN429 ASN116 ASN391 ASN140 ASN433 or b) accept a water-mediated hydrogen bond in which the compound accepts a hydrogen bond from a water that is itself hydrogen-bonded to the sidechain hydroxyl of the tyrosine residue found at BRD-2 BRD-3 BRD-4 BD1 BRD-2 BD2 BD1 BRD-3 BD2 BD1 BRD-4 BD2 TYR113 TYR386 TYR73 TYR348 TYR97 TYR390 and c) which are also able to form a Van der Waals interaction with a lipophilic

Abstract: The use of compounds in the treatment of autoimmune and inflammatory diseases or conditions, pharmaceutical compositions containing such compounds and to methods for identifying compounds for use in the treatment of such diseases or conditions.