Inhibition of matrix metalloproteinases in rheumatoid arthritis and the crystallographic binding mode of a peptide inhibitor.
Tschesche
H
H
Lehrstuhl für Biochemie, Fakultät für Chemie, Universität Bielefeld, Germany.
Bläser
J
J
Kleine
T
T
Schnierer
S
S
Reinemer
P
P
Bode
W
W
Maasjoshusmann
U
U
Fricke
C
C
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