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The TolQ–TolR proteins energize TolA and share homologies with the flagellar motor proteins  MotA–MotB

Molecular microbiology, 2001-11, Vol.42 (3), p.795-807

2001

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Escherichia coli tol-pal Mutants Form Outer Membrane Vesicles

Journal of Bacteriology, 1998-09, Vol.180 (18), p.4872-4878

1998

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The Tol-Pal proteins of the Escherichia coli cell envelope: an energized system required for outer membrane integrity?

Research in Microbiology, 2001-07, Vol.152 (6), p.523-529

2001

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Colicin import into Escherichia coli cells

Journal of bacteriology, 1998-10, Vol.180 (19), p.4993-5002

1998

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Proton motive force drives the interaction of the inner membrane TolA and outer membrane Pal proteins in Escherichia coli

Molecular microbiology, 2000-11, Vol.38 (4), p.904-915

2000

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TolA central domain interacts with Escherichia coli porins

The EMBO journal, 1996-12, Vol.15 (23), p.6408-6415

1996

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Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli

The Journal of biological chemistry, 1995-05, Vol.270 (19), p.11071-11077

1995

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Protein complex within Escherichia coli inner membrane. TolA N-terminal domain interacts with TolQ and TolR proteins

The Journal of biological chemistry, 1995-05, Vol.270 (19), p.11078-11084

1995

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Colicin A unfolds during its translocation in Escherichia coli cells and spans the whole cell envelope when its pore has formed

The EMBO journal, 1992-02, Vol.11 (2), p.441-447

1992

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Protein import into Escherichia coli: colicins A and E1 interact with a component of their translocation system

The EMBO journal, 1991-08, Vol.10 (8), p.1989-1995

1991

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Deletion analyses of the peptidoglycan‐associated lipoprotein Pal reveals three independent binding sequences including a TolA box

Molecular microbiology, 2004-02, Vol.51 (3), p.873-885

2004

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The colicin A pore‐forming domain fused to mitochondrial intermembrane space sorting signals can be functionally inserted into the Escherichia coli plasma membrane by a mechanism that bypasses the Tol proteins

Molecular microbiology, 1994-09, Vol.13 (6), p.1121-1131

1994

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Comparison of the uptake systems for the entry of various BtuB group colicins into Escherichia coli

Journal of general microbiology, 1989-12, Vol.135 (12), p.3413

1989

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Mutational Analyses Define Helix Organization and Key Residues of a Bacterial Membrane Energy-transducing Complex

Journal of molecular biology, 2007-03, Vol.366 (5), p.1424-1436

2007

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Colicin import into Escherichia coli cells requires the proximity of the inner and outer membranes and other factors

International journal of medical microbiology, 2000-10, Vol.290 (4), p.337-344

2000

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Circular dichroism and molecular modeling of the E. coli TolA periplasmic domains

Biospectroscopy (New York, N.Y.), 1999, Vol.5 (3), p.189-198

1999

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Extracellular release of colicin A is non‐specific

The EMBO journal, 1987-08, Vol.6 (8), p.2463-2468

1987

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Complete nucleotide sequence of the structural gene for colicin A, a gene translated at non-uniform rate

Journal of molecular biology, 1983-10, Vol.170 (2), p.271-285

1983

Volltextzugriff (PDF)

Pal Lipoprotein of Escherichia coli Plays a Major Role in Outer Membrane Integrity

Journal of Bacteriology, 2002-02, Vol.184 (3), p.754-759

2002

Volltextzugriff (PDF)

Functional domains of colicin A

Molecular microbiology, 1988-11, Vol.2 (6), p.807-811

1988

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Tol-Dependent Macromolecule Import through the Escherichia coli Cell Envelope Requires the Presence of an Exposed TolA Binding Motif

Journal of Bacteriology, 2005-11, Vol.187 (21), p.7526-7534

2005

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Solution Structure of the E. coli TolA C-terminal Domain Reveals Conformational Changes upon Binding to the Phage g3p N-terminal Domain

Journal of molecular biology, 2005-03, Vol.346 (4), p.1047-1057

2005

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Colicin A and the Tol proteins involved in its translocation are preferentially located in the contact sites between the inner and outer membranes of Escherichia coli cells

The Journal of biological chemistry, 1994-02, Vol.269 (8), p.5874-5880

1994

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The TolB protein interacts with the porins of Escherichia coli

Journal of Bacteriology, 1997-12, Vol.179 (23), p.7274-7279

1997

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LexA repressor induces operator-dependent DNA bending

Journal of molecular biology, 1988-12, Vol.204 (4), p.1049-1054

1988

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The TolQ–TolR proteins energize TolA and share homologies with the flagellar motor proteins  MotA–MotB

Escherichia coli tol-pal Mutants Form Outer Membrane Vesicles

The Tol-Pal proteins of the Escherichia coli cell envelope: an energized system required for outer membrane integrity?

Colicin import into Escherichia coli cells

Proton motive force drives the interaction of the inner membrane TolA and outer membrane Pal proteins in Escherichia coli

TolA central domain interacts with Escherichia coli porins

Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli

Protein complex within Escherichia coli inner membrane. TolA N-terminal domain interacts with TolQ and TolR proteins

Colicin A unfolds during its translocation in Escherichia coli cells and spans the whole cell envelope when its pore has formed

Protein import into Escherichia coli: colicins A and E1 interact with a component of their translocation system

Deletion analyses of the peptidoglycan‐associated lipoprotein Pal reveals three independent binding sequences including a TolA box

The colicin A pore‐forming domain fused to mitochondrial intermembrane space sorting signals can be functionally inserted into the Escherichia coli plasma membrane by a mechanism that bypasses the Tol proteins

Comparison of the uptake systems for the entry of various BtuB group colicins into Escherichia coli

Mutational Analyses Define Helix Organization and Key Residues of a Bacterial Membrane Energy-transducing Complex

Colicin import into Escherichia coli cells requires the proximity of the inner and outer membranes and other factors

Circular dichroism and molecular modeling of the E. coli TolA periplasmic domains

Extracellular release of colicin A is non‐specific

Complete nucleotide sequence of the structural gene for colicin A, a gene translated at non-uniform rate

Pal Lipoprotein of Escherichia coli Plays a Major Role in Outer Membrane Integrity

Functional domains of colicin A

Tol-Dependent Macromolecule Import through the Escherichia coli Cell Envelope Requires the Presence of an Exposed TolA Binding Motif

Solution Structure of the E. coli TolA C-terminal Domain Reveals Conformational Changes upon Binding to the Phage g3p N-terminal Domain

Colicin A and the Tol proteins involved in its translocation are preferentially located in the contact sites between the inner and outer membranes of Escherichia coli cells

The TolB protein interacts with the porins of Escherichia coli

LexA repressor induces operator-dependent DNA bending

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