Ramifications of kinetic partitioning on usher-mediated pilus biogenesis.

Por Saulino, E T, Thanassi, D G, Pinkner, J S, Hultgren, S J
Publicado em 1998

Interactive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly.

Por Slonim, L N, Pinkner, J S, Brändén, C I, Hultgren, S J
Publicado em 1992

Molecular basis of two subfamilies of immunoglobulin-like chaperones.

Por Hung, D L, Knight, S D, Woods, R M, Pinkner, J S, Hultgren, S J
Publicado em 1996

The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems.

Por Jones, C H, Danese, P N, Pinkner, J S, Silhavy, T J, Hultgren, S J
Publicado em 1997

PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA.

Por Jacob-Dubuisson, F, Pinkner, J, Xu, Z, Striker, R, Padmanhaban, A, Hultgren, S J
Publicado em 1994

FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria.

Por Jones, C H, Pinkner, J S, Nicholes, A V, Slonim, L N, Abraham, S N, Hultgren, S J
Publicado em 1993

FimH adhesin of type 1 pili is assembled into a fibrillar tip structure in the Enterobacteriaceae.

Por Jones, C H, Pinkner, J S, Roth, R, Heuser, J, Nicholes, A V, Abraham, S N, Hultgren, S J
Publicado em 1995

Haemophilus influenzae pili are composite structures assembled via the HifB chaperone.

Por St Geme, J W, Pinkner, J S, Krasan, G P, Heuser, J, Bullitt, E, Smith, A L, Hultgren, S J
Publicado em 1996