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CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8

PloS one, 2014-02, Vol.9 (2), p.e87750-e87750

2014

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The Methylococcus capsulatus (Bath) secreted protein, MopE, binds both reduced and oxidized copper

PloS one, 2012-08, Vol.7 (8), p.e43146-e43146

2012

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An Oxidized Tryptophan Facilitates Copper Binding in Methylococcus capsulatus-secreted Protein MopE

The Journal of biological chemistry, 2008-05, Vol.283 (20), p.13897-13904

2008

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BOMP: a program to predict integral beta-barrel outer membrane proteins encoded within genomes of Gram-negative bacteria

Nucleic acids research, 2004-07, Vol.32 (Web Server issue), p.W394

2004

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Multiple polypeptide forms observed in two-dimensional gels of Methylococcus capsulatus (Bath) polypeptides are generated during the separation procedure

Electrophoresis, 2003-02, Vol.24 (4), p.757-761

2003

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The copper responding surfaceome of Methylococccus capsulatus Bath

FEMS microbiology letters, 2011-10, Vol.323 (2), p.97-104

2011

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The Surface-Associated and Secreted MopE Protein of Methylococcus capsulatus (Bath) Responds to Changes in the Concentration of Copper in the Growth Medium

Applied and Environmental Microbiology, 2003-04, Vol.69 (4), p.2386-2388

2003

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The Major Outer Membrane Protein of Fusobacterium nucleatum (FomA) Folds and Inserts into Lipid Bilayers via Parallel Folding Pathways

Journal of molecular biology, 2006-01, Vol.355 (3), p.548-561

2006

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Methylococcus capsulatus (Bath): From Genome to Protein Function, and Vice Versa

Methods in Methane Metabolism, Part B, 2011, Vol.495, p.63-79

2011

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Analysing the outer membrane subproteome of Methylococcus capsulatus (Bath) using proteomics and novel biocomputing tools

Archives of microbiology, 2006-02, Vol.184 (6), p.362-377

2006

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Characterization of a prokaryotic haemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath)

The FEBS journal, 2005-05, Vol.272 (10), p.2428-2440

2005

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Methanotroph Outer Membrane Preparation

Methods in Enzymology, 2011, Vol.495, p.167-176

2011

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Identification of a copper-repressible C-type heme protein of Methylococcus capsulatus (Bath). A member of a novel group of the bacterial di-heme cytochrome c peroxidase family of proteins

The FEBS journal, 2005-12, Vol.272 (24), p.6324-6335

2005

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The bioconversion of ethanol to biosurfactants and dye by a novel coproduction technique

Journal of the American Oil Chemists' Society, 1996-07, Vol.73 (7), p.851-856

1996

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Structural characterization of the fusobacterial non-specific porin FomA suggests a 14-stranded topology, unlike the classical porins

Microbiology (Society for General Microbiology), 2002-11, Vol.148 (Pt 11), p.3395-3403

2002

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Identification of a copper‐repressible C‐type heme protein of Methylococcus capsulatus (Bath)

The FEBS journal, 2005-12, Vol.272 (24), p.6324-6335

2005

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The C-terminal part of the surface-associated protein MopE of the methanotroph Methylococcus capsulatus (Bath) is secreted into the growth medium

Archives of microbiology, 2001-09, Vol.176 (3), p.197-203

2001

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CorA Is a Copper Repressible Surface-Associated Copper

PloS one, 2014-02, Vol.9 (2), p.e87750

2014

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The Fusobacterium nucleatum porin FomA possesses the general topology of the non-specific porins

Microbiology (Society for General Microbiology), 2000-06, Vol.146 ( Pt 6) (6), p.1437-1445

2000

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Molecular analysis of an outer membrane protein, MopB, of Methylococcus capsulatus (Bath) and structural comparisons with proteins of the OmpA family

Archives of microbiology, 2000-05, Vol.173 (5-6), p.346-351

2000

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The Methylococcus capsulatus

PloS one, 2012-08, Vol.7 (8), p.e43146

2012

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Topological investigations of the FomA porin from Fusobacterium nucleatum and identification of the constriction loop L6 The GenBank accession number for the sequence reported in this paper is X72583

Microbiology (Society for General Microbiology), 2001-04, Vol.147 (4), p.1059-1067

2001

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Topological investigations of the FomA porin from Fusobacterium nucleatum and identification of the constriction loop L6

Microbiology (Society for General Microbiology), 2001-04, Vol.147 (Pt 4), p.1059

2001

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Outer membrane proteins of Methylococcus capsulatus (Bath)

Archives of microbiology, 1997-08, Vol.168 (2), p.128-135

1997

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Complete sequence of omp1, the structural gene encoding the 40-kDa outer membrane protein of Fusobacterium nucleatum strain Fev1

Gene, 1993-09, Vol.132 (1), p.107-112

1993

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CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8

The Methylococcus capsulatus (Bath) secreted protein, MopE, binds both reduced and oxidized copper

An Oxidized Tryptophan Facilitates Copper Binding in Methylococcus capsulatus-secreted Protein MopE

BOMP: a program to predict integral beta-barrel outer membrane proteins encoded within genomes of Gram-negative bacteria

Multiple polypeptide forms observed in two-dimensional gels of Methylococcus capsulatus (Bath) polypeptides are generated during the separation procedure

The copper responding surfaceome of Methylococccus capsulatus Bath

The Surface-Associated and Secreted MopE Protein of Methylococcus capsulatus (Bath) Responds to Changes in the Concentration of Copper in the Growth Medium

The Major Outer Membrane Protein of Fusobacterium nucleatum (FomA) Folds and Inserts into Lipid Bilayers via Parallel Folding Pathways

Methylococcus capsulatus (Bath): From Genome to Protein Function, and Vice Versa

Analysing the outer membrane subproteome of Methylococcus capsulatus (Bath) using proteomics and novel biocomputing tools

Characterization of a prokaryotic haemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath)

Methanotroph Outer Membrane Preparation

Identification of a copper-repressible C-type heme protein of Methylococcus capsulatus (Bath). A member of a novel group of the bacterial di-heme cytochrome c peroxidase family of proteins

The bioconversion of ethanol to biosurfactants and dye by a novel coproduction technique

Structural characterization of the fusobacterial non-specific porin FomA suggests a 14-stranded topology, unlike the classical porins

Identification of a copper‐repressible C‐type heme protein of Methylococcus capsulatus (Bath)

The C-terminal part of the surface-associated protein MopE of the methanotroph Methylococcus capsulatus (Bath) is secreted into the growth medium

CorA Is a Copper Repressible Surface-Associated Copper

The Fusobacterium nucleatum porin FomA possesses the general topology of the non-specific porins

Molecular analysis of an outer membrane protein, MopB, of Methylococcus capsulatus (Bath) and structural comparisons with proteins of the OmpA family

The Methylococcus capsulatus

Topological investigations of the FomA porin from Fusobacterium nucleatum and identification of the constriction loop L6 The GenBank accession number for the sequence reported in this paper is X72583

Topological investigations of the FomA porin from Fusobacterium nucleatum and identification of the constriction loop L6

Outer membrane proteins of Methylococcus capsulatus (Bath)

Complete sequence of omp1, the structural gene encoding the 40-kDa outer membrane protein of Fusobacterium nucleatum strain Fev1

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