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The Journal of Biological Chemistry|April 20, 2001
Distinction between major and minor Bacillus signal peptidases based on phylogenetic and structural criteriaM L van Roosmalen, J D Jongbloed, J Y Dubois, et al.
Molecular Microbiology|August 1, 1995
The endogenous Bacillus subtilis (natto) plasmids pTA1015 and pTA1040 contain signal peptidase-encoding genes: identification of a new structural module on cryptic plasmidsW J Meijer, A de Jong, G Bea, et al.
Applied and Environmental Microbiology|July 2, 1999
Evaluation of bottlenecks in the late stages of protein secretion in Bacillus subtilisA Bolhuis, H Tjalsma, H E Smith, et al.
Letters in Applied Microbiology|June 11, 2004
The Bacillus secretion stress response is an indicator for alpha-amylase production levelsH Westers, E Darmon, G Zanen, et al.
The Journal of Biological Chemistry|January 9, 1999
The role of lipoprotein processing by signal peptidase II in the Gram-positive eubacterium bacillus subtilis. Signal peptidase II is required for the efficient secretion of alpha-amylase, a non-lipoproteinH Tjalsma, V P Kontinen, Z Prágai, et al.
The Journal of Biological Chemistry|September 29, 2000
TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathwayJ D Jongbloed, U Martin, H Antelmann, et al.
Euro Surveillance : Bulletin Europeen Sur Les Maladies Transmissibles = European Communicable Disease Bulletin|February 2, 2013
Overview of molecular typing methods for outbreak detection and epidemiological surveillanceA J Sabat, A Budimir, D Nashev, et al.
The Journal of Biological Chemistry|August 8, 1998
SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteinsA Bolhuis, C P Broekhuizen, A Sorokin, et al.
Molecular Microbiology|November 1, 1996
Bacillus subtilis can modulate its capacity and specificity for protein secretion through temporally controlled expression of the sipS gene for signal peptidase IA Bolhuis, A Sorokin, V Azevedo, et al.
Antimicrobial Agents and Chemotherapy|August 19, 2015
The phosphoenolpyruvate:sugar phosphotransferase system is involved in sensitivity to the glucosylated bacteriocin sublancinC V Garcia De Gonzalo, E L Denham, R A T Mars, et al.
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