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Biochemistry|August 8, 1995
Diffusion-limited interaction between unfolded polypeptides and the Escherichia coli chaperone SecBP Fekkes, T den Blaauwen, A J DriessenBiochemistry|September 17, 1996
Domain interactions of the peripheral preprotein Translocase subunit SecAT den Blaauwen, P Fekkes, J G de Wit, et al.Archives of Microbiology|January 1, 1996
Sec-dependent preprotein translocation in bacteriaT den Blaauwen, A J DriessenMolecular Microbiology|March 11, 2000
Non-hydrolysable GTP-gamma-S stabilizes the FtsZ polymer in a GDP-bound stateD J Scheffers, T den Blaauwen, A J DriessenMolecular Microbiology|November 1, 1996
SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasmC van der Does, T den Blaauwen, J G de Wit, et al.Microbiology and Molecular Biology Reviews : MMBR|March 6, 1999
Protein targeting to the bacterial cytoplasmic membraneP Fekkes, A J DriessenFEBS Letters|November 22, 1997
Interaction of SecB with soluble SecAT den Blaauwen, E Terpetschnig, J R Lakowicz, et al.Biochemistry|April 23, 1999
Outer membrane protein A of Escherichia coli inserts and folds into lipid bilayers by a concerted mechanismJ H Kleinschmidt, T den Blaauwen, A J Driessen, et al.FEBS Letters|April 12, 2001
Substitution of a conserved aspartate allows cation-induced polymerization of FtsZD J Scheffers, J G de Wit, T den Blaauwen, et al.The EMBO Journal|October 8, 1997
The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocationP Fekkes, C van der Does, A J DriessenPageof 17