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Prioria balsamifera

Known as: Gossweilerodendron balsamiferum, agba, tola 
 
National Institutes of Health

Papers overview

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Highly Cited
2010
Highly Cited
2010
The caulobacter Tol-Pal complex is essential for outer membrane integrity and the positioning of a polar localization factor.
Cell division in Caulobacter crescentus involves constriction and fission of the inner membrane (IM) followed about 20 min later… Expand
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Highly Cited
2009
Highly Cited
2009
An adaptive energy efficient MAC protocol for the medical body area network
Medical body area networks will employ both implantable and bodyworn devices to support a diverse range of applications with… Expand
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Highly Cited
2005
Highly Cited
2005
The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides.
The TonB protein transduces energy from the proton gradient across the cytoplasmic membrane of Gram-negative bacteria to TonB… Expand
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Highly Cited
2002
Highly Cited
2002
Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity.
The Tol-Pal system of gram-negative bacteria is composed of five proteins. TolA, TolQ, and TolR are inner membrane proteins, TolB… Expand
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Highly Cited
2001
Highly Cited
2001
The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB.
The Tol-Pal system of Escherichia coli is required for the maintenance of outer membrane stability. Recently, proton motive force… Expand
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Highly Cited
2000
Highly Cited
2000
Modifications of pyrethroid effects associated with kdr mutation in Anopheles gambiae.
Effects of knockdown resistance (kdr) were investigated in three pyrethroid-resistant (RR) strains of the Afrotropical mosquito… Expand
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Highly Cited
2000
Highly Cited
2000
Proton motive force drives the interaction of the inner membrane TolA and outer membrane pal proteins in Escherichia coli.
The Tol-Pal system of the Escherichia coli envelope is formed from the inner membrane TolQ, TolR and TolA proteins, the… Expand
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Highly Cited
1999
Highly Cited
1999
Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA.
BACKGROUND Infection of male Escherichia coli cells by filamentous Ff bacteriophages (M13, fd, and f1) involves interaction of… Expand
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Highly Cited
1997
Highly Cited
1997
The C-Terminal Domain of TolA Is the Coreceptor for Filamentous Phage Infection of E. coli
Filamentous bacteriophages infecting gram-negative bacteria display tropism for a variety of pilus structures. However, the… Expand
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Highly Cited
1993
Highly Cited
1993
Evolutionary relationship of uptake systems for biopolymers in Escherichia coli: cross-complementation between the TonB-ExbB-ExbD and the TolA-TolQ-TolR proteins.
Escherichia coli possesses two energy-coupled import systems through which substances of low concentration and of a size too… Expand
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