Abstract: Peptides of Formula I are useful for therapeutic purposes, among others.

Abstract: A method is described for inhibiting urokinase plasminogen activator in a human or animal patient.

Abstract: A method is described for inhibiting urokinase plasminogen activator in a human or animal patient.

Abstract: A tumor necrosis factor-? converting enzyme (TACE) is produced, purified, and crystallized. The three-dimensional coordinates of the crystal are obtained by X-ray diffraction. The coordinates can be recorded on a computer readable medium, or are part of a video memory, where they can be used as part of a system for studying for studying TACE. The coordinates are also used in designing, screening, and developing compounds that associate with TACE.

Abstract: The invention relates to novel selective inhibitors of the urokinase plasminogen activator (uPA, EC 3.4.21.31), of the arylguanidine type.

Abstract: A tumor necrosis factor-&agr; converting enzyme (TACE) is produced, purified, and crystallized. The three-dimensional coordinates of the crystal are obtained by X-ray diffraction. The coordinates can be recorded on a computer readable medium, or are part of a video memory, where they can be used as part of a system for studying for studying TACE. The coordinates are also used in designing, screening, and developing compounds that associate with TACE.

Abstract: Peptides of Formula I are useful for therapeutic purposes, among others.

Abstract: A chimeric serine protease whose protease domain is composed of two domain halves (half-sides) with a &bgr;-folded sheet structure, wherein the first domain half corresponds to the first domain half of a first serine protease and the second domain half corresponds to the second domain half of a second serine protease, has improved properties and can be readily crystallized.

Abstract: A process for the recombinant production of a protease is characterized by a) transforming a host cell with a recombinant nucleic acid which codes for a zymogenic precursor of a protease containing an autocatalytic cleavage site which does not occur naturally, wherein the active form of the said protease recognizes this cleavage site and cleaves the precursor to form the active protease, b) culturing the host cell in such a way that the zymogenic precursor of the protease is formed in the host cell in the form of inclusion bodies, c) isolating the inclusion bodies and renaturation under such conditions that the protease part of the zymogenic precursor is formed in its natural conformation and d) autocatalytic cleavage of the renatured zymogenic precursor to produce the active protease. This process is suitable for providing recombinant proteases in a simple manner and in large amounts.

Abstract: The invention relates to bifunctional tryptase inhibitors of formula (I) wherein H1 and H2 comprise a Q group and L is a linker of formula and the conformation of the H1, H2 and L groups is such that the groups are separated by a distance of from 20 to 45 Å. Pharmaceutical compositions and crystal forms of the compounds are described in addition to methods for producing and identifying such compounds, as well as the use of such compounds in methods of treating allergic and inflammatory diseases.

Abstract: The invention relates to novel selective inhibitors of the urokinase plasminogen activator (uPA, EC 3.4.21.31), of the arylguanidine type.

Abstract: A tumor necrosis factor-&agr; converting enzyme (TACE) is produced, purified, and crystallized. The three-dimensional coordinates of the crystal are obtained by X-ray diffraction. The coordinates can be recorded on a computer readable medium, or are part of a video memory, where they can be used as part of a system for studying for studying TACE. The coordinates are also used in designing, screening, and developing compounds that associate with TACE.

Abstract: A method for producing biologically active serine proteases, isolated serine protease domains and their amino acid variants in a prokaryotic host is disclosed. The method comprises an N-terminal addition of a helper sequence consisting of a dipeptide which is suitable for degradation by a dipeptidyl amino peptidase, by the expression of the serine protease(s) and/or its (their) fragments containing the N-terminal dipeptide helper sequence, optionally as inclusion bodies, and by the renaturation of the expressed proteins and the activation of the serine protease(s) and/or serine protease domains by splitting off the helper sequence using an exopeptidase.

Abstract: The invention relates to novel inhibitors of human tryptase which are used in the pharmaceutical industry for the production of medicaments.

Abstract: The invention provides spatial structures and crystal forms of polypeptides comprising at least one subdomain of a protein from the family of proteins that includes calcium-activated cystein proteinases (calpains). Also provided are methods of preparing these crystal forms, and methods of modeling calpains using the coordinates derived from the disclosed crystal forms. The invention further provides compounds that act as ligands for calpains, methods for identifying such ligands, and methods for using such ligands as inhibitors or activators of calpain activity.

Abstract: A tumor necrosis factor-&agr; converting enzyme (TACE) is produced, purified, and crystallized. The three-dimensional coordinates of the crystal are obtained by X-ray diffraction. The coordinates can be recorded on a computer readable medium, or are part of a video memory, where they can be used as part of a system for studying for studying TACE. The coordinates are also used in designing, screening, and developing compounds that associate with TACE.

Abstract: There is described the use of a compound represented by general formulae (I), (II) or (III), for the inhibition of matrix metalloproteinases (MMP), wherein X1 is oxygen or sulfur, R1 is OH, SH, CH2OH, CH2SH or NHOH, R2 is a residue of 2 to 10 hydrocarbon backbone atoms, which binds to the amino acid 161 of HNC, said residue being saturated or unsaturated, linear or branched, and contains preferably homocyclic or heterocyclic structures, X2 is oxygen or sulfur and binds as hydrogen acceptor on amino acid 160 of HNC, Y is a residue which binds to the S1′ pocket of HNC and consists of at least 4 backbone atoms Z1-Z2-Z3-Z4-R3, and R3 is n-propyl, isopropyl, isobutyl or a residue with at least 4 backbone atoms, which is not larger than a tricyclic ring system. These compounds bind to MMPs in a manner different from the mode of binding of the inhibitors of the state of the art.

Abstract: A chimeric serine protease whose protease domain is composeD. of two domain halves (half-sides) with a &bgr;-folded sheet structure, wherein the first domain half corresponds to the first domain half of a first serine protease and the second domain half corresponds to the second domain half of a second serine protease, has improved properties and can be readily crystallized.

Abstract: A chimeric serine protease whose protease domain is composed of two domain halves (half-sides) with a .beta.-folded sheet structure, wherein the first domain half corresponds to the first domain half of a first serine protease and the second domain half corresponds to the second domain half of a second serine protease, has improved properties and can be readily crystallized.