Activity-Related Conformational Changes in D,D-Carboxypeptidases Revealed by In Vivo Periplasmic Forster Resonance Energy Transfer Assay in Escherichia coli (vol 8, e01089-17, 2017)MBIOIF4.72022-02-220OAAI
Activity-Related Conformational Changes in D, D-Carboxypeptidases Revealed by In Vivo Periplasmic Forster Resonance Energy Transfer Assay in Escherichia coliMBIOIF4.72017-11-0823OAAI
Novel Twin-Arginine Translocation Pathway-Dependent Phenotypes of Bacillus subtilis Unveiled by Quantitative ProteomicsJOURNAL OF PROTEOME RESEARCHIF3.62013-01-1126PREAI
High-Salinity Growth Conditions Promote Tat-Independent Secretion of Tat Substrates in Bacillus subtilisAPPLIED AND ENVIRONMENTAL MICROBIOLOGYIF3.72012-11-0123OA
Specific Targeting of the Metallophosphoesterase YkuE to the Bacillus Cell Wall Requires the Twin-arginine Translocation SystemJOURNAL OF BIOLOGICAL CHEMISTRYIF3.92012-08-0124OAAI
Salt Sensitivity of Minimal Twin Arginine TranslocasesJOURNAL OF BIOLOGICAL CHEMISTRYIF3.92011-12-0123OAAI
Overflow of a hyper-produced secretory protein from the Bacillus Sec pathway into the Tat pathway for protein secretion as revealed by proteogenomicsPROTEOMICSIF3.92009-01-2923PRE
MscL of Bacillus subtilis prevents selective release of cytoplasmic proteins in a hypotonic environmentPROTEOMICSIF3.92009-01-219PRE
The Twin-Arginine Signal Peptide of Bacillus subtilis YwbN Can Direct either Tat- or Sec-Dependent Secretion of Different Cargo Proteins: Secretion of Active Subtilisin via the B. subtilis Tat PathwayAPPLIED AND ENVIRONMENTAL MICROBIOLOGYIF3.72008-12-1540OAAI
The twin-arginine translocation (Tat) systems from Bacillus subtilis display a conserved mode of complex organization and similar substrate recognition requirementsFEBS JOURNALIF4.22008-12-1236OAAI
Bifunctional TatA subunits in minimal Tat protein translocasesTRENDS IN MICROBIOLOGYIF14.92006-01-0169PREAI