Cleavage of the intermediate filament subunit protein vimentin by HIV-1 protease: utilization of a novel cleavage site and identification of higher order polymers of pepstatin A.
Shoeman
R L
RL
Max-Planck-Institut für Zellbiologie, Ladenburg/Heidelberg, Federal Republic of Germany.
Höner
B
B
Stoller
T J
TJ
Mothes
E
E
Kesselmeier
C
C
Traub
P
P
Graves
M C
MC
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D016333:HIV Protease / Q000378:metabolism*; D066298:In Vitro Techniques; D051379:Mice; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D010436:Pepstatins / Q000378:metabolism; D011108:Polymers / Q000378:metabolism; D014746:Vimentin / Q000737:chemistry / Q000378:metabolism*
D009842:Oligopeptides; D010436:Pepstatins; D011108:Polymers; D014746:Vimentin; C014195:Streptomyces pepsin inhibitor; D016333:HIV Protease; C031375:pepstatin