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The Mycobacterial Cell Wall--Peptidoglycan and Arabinogalactan

Cold Spring Harbor perspectives in medicine, 2015-08, Vol.5 (8), p.a021113-a021113

2015

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Potentiation of curing by a broad-host-range self-transmissible vector for displacing resistance plasmids to tackle AMR

PloS one, 2020-01, Vol.15 (1), p.e0225202

2020

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New Multidrug Efflux Inhibitors for Gram-Negative Bacteria

mBio, 2020-07, Vol.11 (4)

2020

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The C-terminal domain of the Arabinosyltransferase Mycobacterium tuberculosis EmbC is a lectin-like carbohydrate binding module

PLoS pathogens, 2011-02, Vol.7 (2), p.e1001299

2011

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Targets for the MalI repressor at the divergent Escherichia coli K-12 malX-malI promoters

FEMS microbiology letters, 2010-04, Vol.305 (1), p.28-34

2010

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Iteron control of oriV function in IncP-1 plasmid RK2

Plasmid, 2023-05, Vol.126, p.102681-102681, Article 102681

2023

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Determinants of the C-Terminal Domain of the Escherichia coli RNA Polymerase α Subunit Important for Transcription at Class I Cyclic AMP Receptor Protein-Dependent Promoters

Journal of Bacteriology, 2002-04, Vol.184 (8), p.2273-2280

2002

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Biochemical characterization of the Mycobacterium tuberculosis phosphoribosyl-1-pyrophosphate synthetase

Glycobiology (Oxford), 2011-04, Vol.21 (4), p.410-425

2011

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New targets for the cyclic AMP receptor protein in the Escherichia coli K-12 genome

FEMS microbiology letters, 2007-09, Vol.274 (1), p.89-94

2007

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Activation of sigma 28-dependent transcription in Escherichia coli by the cyclic AMP receptor protein requires an unusual promoter organization

Molecular microbiology, 2010-03, Vol.75 (5), p.1098-1111

2010

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Activation of σ²⁸-dependent transcription in Escherichia coli by the cyclic AMP receptor protein requires an unusual promoter organization

Molecular microbiology, 2010-03, Vol.75 (5), p.1098-1111

2010

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Transcription initiation in the Escherichia coli K-12 malI-malX intergenic region and the role of the cyclic AMP receptor protein

FEMS microbiology letters, 2008-11, Vol.288 (2), p.250-257

2008

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Exploitation of a Chemical Nuclease to Investigate the Location and Orientation of the Escherichia coli RNA Polymerase α Subunit C-terminal Domains at Simple Promoters That Are Activated by Cyclic AMP Receptor Protein

The Journal of biological chemistry, 2003-12, Vol.278 (52), p.52944-52952

2003

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Requirement for two copies of RNA polymerase alpha subunit C-terminal domain for synergistic transcription activation at complex bacterial promoters

Genes & development, 2002-10, Vol.16 (19), p.2557-2565

2002

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Location of the Escherichia coli RNA polymerase α subunit C-terminal domain at an FNR-dependent promoter: analysis using an artificial nuclease

FEBS letters, 2004-01, Vol.558 (1), p.13-18

2004

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Spacing requirements for interactions between the C-terminal domain of the alpha subunit of Escherichia coli RNA polymerase and the cAMP receptor protein

Biochemical journal, 1998-02, Vol.330 ( Pt 1) (1), p.413-420

1998

Volltextzugriff (PDF)

Targets for the MalI repressor at the divergent Escherichia coli K-12 malX-malI promoters: The E. coli malX-malI regulatory region

FEMS microbiology letters, 2010-04, Vol.305 (1), p.28-34

2010

Volltextzugriff (PDF)

Targets for the Mall repressoratthe divergent Escherichia coliK-12 malX-malI promoters

FEMS microbiology letters, 2010, Vol.305 (1), p.28-34

2010

Volltextzugriff (PDF)

Activation of s28-dependent transcription in Escherichia coli by the cyclic AMP receptor protein requires an unusual promoter organization

Molecular microbiology, 2010-03, Vol.75 (5), p.1098-1111

2010

Volltextzugriff (PDF)

Activation of [sigma]^sup 28^-dependent transcription in Escherichia coli by the cyclic AMP receptor protein requires an unusual promoter organization

Molecular microbiology, 2010-03, Vol.75 (5), p.1098

2010

Volltextzugriff (PDF)

Transcription initiation in the Escherichia coli K-12 malIâmalX intergenic region and the role of the cyclic AMP receptor protein

FEMS microbiology letters, 2008-11, Vol.288 (2), p.250-257

2008

Volltextzugriff (PDF)

Transcription initiation in the Escherichia coli K-12 mall-malX intergenic region and the role of the cyclic AMP receptor protein

FEMS microbiology letters, 2008, Vol.288 (2), p.250-257

2008

Volltextzugriff (PDF)

Transcription activation at Class II CRP-dependent promoters: identification of determinants in the C-terminal domain of the RNA polymerase α subunit

The EMBO journal, 1998-06, Vol.17 (12), p.3439-3447

1998

Volltextzugriff (PDF)

Exploitation of a Chemical Nuclease to Investigate the Location and Orientation of the Escherichia coli RNA Polymerase Î± Subunit C-terminal Domains at Simple Promoters That Are Activated by Cyclic AMP Receptor Protein

The Journal of biological chemistry, 2003-12, Vol.278 (52), p.52944

2003

Volltextzugriff (PDF)

Inhibition and metal ion activation of pig kidney aminopeptidase P: Dependence on nature of substrate

Biochemical pharmacology, 1996-07, Vol.52 (2), p.229-236

1996

Volltextzugriff (PDF)

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The Mycobacterial Cell Wall--Peptidoglycan and Arabinogalactan

Potentiation of curing by a broad-host-range self-transmissible vector for displacing resistance plasmids to tackle AMR

New Multidrug Efflux Inhibitors for Gram-Negative Bacteria

The C-terminal domain of the Arabinosyltransferase Mycobacterium tuberculosis EmbC is a lectin-like carbohydrate binding module

Targets for the MalI repressor at the divergent Escherichia coli K-12 malX-malI promoters

Iteron control of oriV function in IncP-1 plasmid RK2

Determinants of the C-Terminal Domain of the Escherichia coli RNA Polymerase α Subunit Important for Transcription at Class I Cyclic AMP Receptor Protein-Dependent Promoters

Biochemical characterization of the Mycobacterium tuberculosis phosphoribosyl-1-pyrophosphate synthetase

New targets for the cyclic AMP receptor protein in the Escherichia coli K-12 genome

Activation of sigma 28-dependent transcription in Escherichia coli by the cyclic AMP receptor protein requires an unusual promoter organization

Activation of σ²⁸-dependent transcription in Escherichia coli by the cyclic AMP receptor protein requires an unusual promoter organization

Transcription initiation in the Escherichia coli K-12 malI-malX intergenic region and the role of the cyclic AMP receptor protein

Exploitation of a Chemical Nuclease to Investigate the Location and Orientation of the Escherichia coli RNA Polymerase α Subunit C-terminal Domains at Simple Promoters That Are Activated by Cyclic AMP Receptor Protein

Requirement for two copies of RNA polymerase alpha subunit C-terminal domain for synergistic transcription activation at complex bacterial promoters

Location of the Escherichia coli RNA polymerase α subunit C-terminal domain at an FNR-dependent promoter: analysis using an artificial nuclease

Spacing requirements for interactions between the C-terminal domain of the alpha subunit of Escherichia coli RNA polymerase and the cAMP receptor protein

Targets for the MalI repressor at the divergent Escherichia coli K-12 malX-malI promoters: The E. coli malX-malI regulatory region

Targets for the Mall repressoratthe divergent Escherichia coliK-12 malX-malI promoters

Activation of s28-dependent transcription in Escherichia coli by the cyclic AMP receptor protein requires an unusual promoter organization

Activation of [sigma]^sup 28^-dependent transcription in Escherichia coli by the cyclic AMP receptor protein requires an unusual promoter organization

Transcription initiation in the Escherichia coli K-12 malIâmalX intergenic region and the role of the cyclic AMP receptor protein

Transcription initiation in the Escherichia coli K-12 mall-malX intergenic region and the role of the cyclic AMP receptor protein

Transcription activation at Class II CRP-dependent promoters: identification of determinants in the C-terminal domain of the RNA polymerase α subunit

Exploitation of a Chemical Nuclease to Investigate the Location and Orientation of the Escherichia coli RNA Polymerase Î± Subunit C-terminal Domains at Simple Promoters That Are Activated by Cyclic AMP Receptor Protein

Inhibition and metal ion activation of pig kidney aminopeptidase P: Dependence on nature of substrate

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