Description     Claims     Drawing  

WO9641624A   [0002]  [0017]  [0017]  [0017]  [0020]  [0020]  [0022]  [0024]  [0024]  [0026] 
US5011912A   [0022] 
US5594106A   [0035] 
WO9535367A   [0038]  [0045] 
WO9715588A   [0038]  [0045] 
EP646599A2   [0038] 
GB2306961A   [0038]  [0045] 
WO9708300A   [0038]  [0046] 
WO9507619A   [0053] 
US9902185W   [0111] 
US60117476B   [0111] 
US09050083B   [0111] 
US60073709B   [0111] 

Tumor Necrosis Factor: Function, Release and Clearance   [0001] 
A metalloproteinase disintigrin that releases tumor-necrosis factor-α from cells   [0002] 
Cloning of a disintigrin metalloproteinase that processes precursor tumor-necrosis factor-α   [0002] 
Inhibition of Matrix Metalloproteinases: Structure Based Design   [0003] 
SETOR: Hardware Lighted Three-Dimensional Solid Model Representations of Macromolecules   [0015] 
Protein Engineering   [0016] 
A Metalloproteinase disintigrin that releases tumour-necrosis factor-α from cells   [0018]  [0078] 
Bio/Technology   [0024] 
Cell   [0024] 
Selection and coamplification of heterologous genes in mammalian cells   [0025] 
Molecular Modeling Software and Methods for Medicinal Chemistry   [0052] 
The Use of Structural Information in Drug Design   [0052] 
Three-dimensional structure of echistatin, the smallest active RGD protein   [0059] 
Astacins. serralysins, snake venom and matrix metalloproteinases exhibit identical zinc binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins   [0060] 
he metzincins: Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases   [0060] 
X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors: Implications for substrate binding and rational drug design   [0060] 
Relaxed specificity of matrix metalloproteinases (MMPs) and TIMP intensity of tumor necrosis factor-α (TNF-α) production suggest the major TNF-α converting enzyme is not an MMP   [0062] 
Human pro-tumor necrosis factor is a homotrimer   [0062] 
Length of the linking domain of human pro-tumor necrosis factor determines the cleavage processing   [0062] 
Biochem.   [0062] 
Biochem.   [0062] 
Structure of tumor necrosis factor   [0062] 
Astacins, serralysins, snake venom and matmrix metalloproteinases exhibit identical zinc binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins   [0063] 
The metzincins: Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases   [0063] 
First structure of a snake venom metalloproteinase: prototype for matrix metalloproteinases/collagenases   [0063] 
Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d   [0063] 
Crystal structure of H2-proteinase from the venom of Trimeresurus flavoviridis   [0063] 
ADAMs in Fertilization and Development   [0065] 
Purification of ADAM 10 from bovine spleen as a TNFα convertase   [0065] 
Science   [0065] 
Refined 2.0 A crystal structure of snake venom zinc endopeptidase adamalysin II   [0065] 
Anti-arthritic activity of hydroxamic acid-based pseudopeptide inhibitors of matrix metalloproteinases and TNFα processing   [0066] 
Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1   [0066]