Literature DB >> 8100379

SecB: a molecular chaperone of Escherichia coli protein secretion pathway.

D N Collier1.   

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Year:  1993        PMID： 8100379     DOI： 10.1016/s0065-3233(08)60567-7

Source DB:  PubMed          Journal:  Adv Protein Chem        ISSN： 0065-3233


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  13 in total

1.  The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding.

Authors:  L L Randall; S J Hardy; T B Topping; V F Smith; J E Bruce; R D Smith
Journal:  Protein Sci       Date:  1998-11       Impact factor: 6.725

2.  Calorimetric analyses of the interaction between SecB and its ligands.

Authors:  L L Randall; T B Topping; D Suciu; S J Hardy
Journal:  Protein Sci       Date:  1998-05       Impact factor: 6.725

3.  Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding protein.

Authors:  V F Smith; S J Hardy; L L Randall
Journal:  Protein Sci       Date:  1997-08       Impact factor: 6.725

4.  The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter.

Authors:  P Delepelaire; C Wandersman
Journal:  EMBO J       Date:  1998-02-16       Impact factor: 11.598

5.  Influence of impaired chaperone or secretion function on SecB production in Escherichia coli.

Authors:  J P Müller
Journal:  J Bacteriol       Date:  1996-11       Impact factor: 3.490

6.  Demonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioning.

Authors:  V J Khisty; L L Randall
Journal:  J Bacteriol       Date:  1995-06       Impact factor: 3.490

7.  Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coli.

Authors:  S M Strobel; J G Cannon; P J Bassford
Journal:  J Bacteriol       Date:  1993-11       Impact factor: 3.490

8.  Export of periplasmic galactose-binding protein in Escherichia coli depends on the chaperone SecB.

Authors:  E L Powers; L L Randall
Journal:  J Bacteriol       Date:  1995-04       Impact factor: 3.490

9.  Escherichia coli signal peptides direct inefficient secretion of an outer membrane protein (OmpA) and periplasmic proteins (maltose-binding protein, ribose-binding protein, and alkaline phosphatase) in Bacillus subtilis.

Authors:  D N Collier
Journal:  J Bacteriol       Date:  1994-05       Impact factor: 3.490

10.  The roles of signal peptide and mature protein in RNase (barnase) export from Bacillus subtilis.

Authors:  M Chen; V Nagarajan
Journal:  Mol Gen Genet       Date:  1993-06
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