Inhibition of matrix metalloproteinases in rheumatoid arthritis and the crystallographic binding mode of a peptide inhibitor.
Lehrstuhl für Biochemie, Fakultät für Chemie, Universität Bielefeld, Germany.
H
H
Tschesche
J
J
Bläser
T
T
Kleine
S
S
Schnierer
P
P
Reinemer
W
W
Bode
U
U
Maasjoshusmann
C
C
Fricke
D001172:Arthritis, Rheumatoid / Q000201:enzymology* / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D005109:Extracellular Matrix / Q000201:enzymology*; D006801:Humans; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D008961:Models, Structural; D009842:Oligopeptides / Q000378:metabolism; D011487:Protein Conformation; D013582:Synovial Fluid / Q000201:enzymology* / Q000378:metabolism
D009842:Oligopeptides; C090221:prolyl-leucyl-glycine hydroxamate; D008666:Metalloendopeptidases