Abstract: The invention provides a green process for direct oxidation of a large number of substituted or unsubstituted cinnamaldehydes or cinnamyl alcohols into the corresponding alkyl or aryl cinnamates in one step. The process of the present invention is a convenient and efficient green process for the preparation of various aryl or alkyl cinnamates under conventional, microwave and ultrasound directly from cinnamaldehydes or cinnamyl alcohols in the presence of an oxidizing agent, catalyst and an alcohol, with or without an organic solvent. These esters are immensely important compounds in flavor, perfumery and pharmaceutical industries. There are several prior arts available for the preparation of cinnamic esters, but all of them suffer from deficiencies such as use of expensive reagents and catalysts, harsh reaction conditions, use of toxic chemicals and others.

Abstract: The present invention relates to Nephronophthisis, in particular to the NPHP6 protein (nephrocystin-6) and nucleic acids encoding the NPHP6 protein. The present invention also provides assays for the detection of NPHP6, and assays for detecting NPHP6 polymorphisms and mutations associated with disease states.

Abstract: The present invention relates to Nephronophthisis, in particular to the NPHP5 protein (nephrocystin-5) and nucleic acids encoding the NPHP5 protein. The present invention also provides assays for the detection of NPHP5 polymorphisms and mutations associated with disease states.

Abstract: Cyclic peptide of formula (1) where Xaa1 is selected from L-amino acids selected from Phe, Lys and Arg, D-amino acids selected from Phe and Met, the L- and D-amino acid optionally substituted on its &agr;-carbon or its &agr;-amino group with a C1-4 alkyl group; and Melle; Xaa2, Xaa3 et Xaa4 are respectively Leu, Asp and Val, optionally substituted on their &agr;-carbon or &agr;-amino group with a C1-4 alkyl group; X1 is selected from D-amino acids selected from Ala, Phe, Arg, Lys, Trp, hArg(Et)2, Orn(CHMe2), Orn(Me2), Lys(CHMe2) and Arg(Pmc), optionally substituted on their &agr;-carbon or &agr;-amino group with a C1-4 alkyl group; Formula (II); NH(CH2)5CO; and NH(CH2)2S(CH2)yCO, where y is 1 or 2; X2 is selected from D-amino acids selected from Ala, Arg, Lys, His, hArg(Et)2, Orm(CHMe2), and Om(Me2), optionally substituted on their &agr;-carbon or &agr;-amino group with a C1-4 alkyl group; NH(CH2)SCH2CO; and NH(CH2)xCO, where x is 2 or 3; Xaa5 and Xaa6 are each independently a

Abstract: Cyclic dimeric peptides of formula (I) ##STR1## wherein: peptide 1 and peptide 2 independently represent a tetrapeptide of formula -AA1-AA2-AA3-AA4- juxtaposed in parallel or antiparallel orientation; AA1 is an L or D amino acid selected from Ile, Leu and amino analogues thereof selected from Pro, Gly, Tic and Phe; AA2 is an L amino acid selected from Leu and amino acid analogues thereof selected from Ile, Phe and Val; AA3 is an L amino acid selected from Asp, Glu and amino acid analogues thereof; AA4 is an L amino acid selected from Val and amino acid analogues thereof selected from Leu, Ile, Phe and Cha (cyclohexylalanine); L1 and L2 independently represent linking moieties for linking peptides 1 and 2 to form a cyclic dipeptide; or salts thereof. The cyclic dipeptides inhibit the interaction of vascular cell adhesion molecule-1 and fibronectin with integrin very late antigen 4 and have therapeutic applications such as in rheumatoid arthritis, asthma or multiple sclerosis.

Abstract: Cyclic peptides of formula (1): ##STR1## Wherein: AA1 is an L or D amino acid selected from Ile and Leu or amino acid analogue thereof; AA2 is an L amino acid selected from Leu or amino acids analogue thereof; AA3 is an L amino acid selected from Asp or amino acid analogue thereof containing a carboxy group in its side chain; AA4 is an L amino acid selected from Val or amino acid analogue thereof and; LINKER represents a linking moiety for linking N terminus of AA1 to C terminus of AA4 to form a cyclic peptide containing a heterocyclic ring having 17 to 30 members. The cyclic peptides inhibit the interaction of vascular cell adhesion molecule-1 and fibronectin with integrin very late antigen 4 and have therapeutic applications such as in rheumatoid arthritis or multiple sclerosis.

Abstract: The disclosure relates to novel luliberin analogues which possess luliberin agonist activity, to processes for their manufacture and to compositions containing them. Typical of the peptides disclosed is ##STR1## in which A is D-Phe, D-Tyr(Me) or D-Ser(Bu.sup.t).