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Welcome to the Pubget Medical Subject Headings (MESH) browser. Click on a topic or subtopic below to explore related papers. In the gold box is the most recent paper about the current MESH term, and below are 20 related papers.
Periplasmic Proteins (0):
Recent article
Periplasmic Proteins
Journal of Physical Chemistry B (114)34 2010
Abstract
The periplasmic sensor domains encoded by genes gsu0582 and gsu0935 are part of methyl accepting chemotaxis proteins in the bacterium Geobacter sulfurreducens (Gs). The sensor domains of these proteins contain a heme-c prosthetic group and a PAS-like fold as revealed by their crystal structures. Bio...
|
PMID: 20690670
PDF is available here.
PDF is available here.
| < More recent | Older article > |
Abstract
We measured the effects of various mutations introduced to the L2 loop's region (residues 228-238) on the stability of HtrA molecule and its proteolytic activity. We demonstrated that most mutations affected the activity of HtrA. In the case of the following substitutions: L229N, N235I, I238N, the p...
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PMID: 20515644
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in...
|
PMID: 20497502
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that proper regulation of this signalling pathway is essential for cell viability. Without the small 83 amino acid protein FeuN, S. meliloti cells are unable to grow, and this phenotype is dependent on the FeuPQ pathway. Using Escherichia coli as a heterologous system, we show that expressio...
|
PMID: 20487268
PDF is available here.
PDF is available here.