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A Rietsch

Showing results (1-10 of 7) with videos related to

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FEMS Microbiology Letters|February 15, 1993
Non-specific hole formation in the Escherichia coli inner membrane by lambda S proteins in independent of cellular secY and secA functions and of the proportion of membrane acidic phospholipidsA Rietsch, U Bläsi
Annual Review of Genetics|February 3, 1999
The genetics of disulfide bond metabolismA Rietsch, J Beckwith
FEMS Microbiology Letters|August 15, 1997
The hydrophilic C-terminal part of the lambda S holin is non-essential for intermolecular interactionsA Rietsch, P Fraisl, A Graschopf, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 12, 1996
An in vivo pathway for disulfide bond isomerization in Escherichia coliA Rietsch, D Belin, N Martin, et al.
Journal of Bacteriology|November 14, 1997
Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxinA Rietsch, P Bessette, G Georgiou, et al.
Virology|April 1, 1993
Lambda kil-mediated lysis requires the phage contextG R Reisinger, A Rietsch, W Lubitz, et al.
The Journal of Biological Chemistry|August 28, 1999
Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coliE Mössner, M Huber-Wunderlich, A Rietsch, et al.
Pageof 1

Showing results (1-10 of 7) with videos related to

Sort By:
Pageof 1
FEMS Microbiology Letters|February 15, 1993
Non-specific hole formation in the Escherichia coli inner membrane by lambda S proteins in independent of cellular secY and secA functions and of the proportion of membrane acidic phospholipidsA Rietsch, U Bläsi
Annual Review of Genetics|February 3, 1999
The genetics of disulfide bond metabolismA Rietsch, J Beckwith
FEMS Microbiology Letters|August 15, 1997
The hydrophilic C-terminal part of the lambda S holin is non-essential for intermolecular interactionsA Rietsch, P Fraisl, A Graschopf, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 12, 1996
An in vivo pathway for disulfide bond isomerization in Escherichia coliA Rietsch, D Belin, N Martin, et al.
Journal of Bacteriology|November 14, 1997
Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxinA Rietsch, P Bessette, G Georgiou, et al.
Virology|April 1, 1993
Lambda kil-mediated lysis requires the phage contextG R Reisinger, A Rietsch, W Lubitz, et al.
The Journal of Biological Chemistry|August 28, 1999
Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coliE Mössner, M Huber-Wunderlich, A Rietsch, et al.
Pageof 1