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Refinado por: Nome da Publicação: The Journal Of Biological Chemistry remover
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11
A Peptidomimetic Antibiotic Targets Outer Membrane Proteins and Disrupts Selectively the Outer Membrane in Escherichia coli
A Peptidomimetic Antibiotic Targets Outer Membrane Proteins and Disrupts Selectively the Outer Membrane in Escherichia coli
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A Peptidomimetic Antibiotic Targets Outer Membrane Proteins and Disrupts Selectively the Outer Membrane in Escherichia coli

Urfer, Matthias ; Bogdanovic, Jasmina ; Lo Monte, Fabio ; Moehle, Kerstin ; Zerbe, Katja ; Omasits, Ulrich ; Ahrens, Christian H. ; Pessi, Gabriella ; Eberl, Leo ; Robinson, John A.

The Journal of biological chemistry, 2016-01, Vol.291 (4), p.1921-1932 [Periódico revisado por pares]

United States: Elsevier Inc

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12
The architecture of the OmpC–MlaA complex sheds light on the maintenance of outer membrane lipid asymmetry in Escherichia coli
The architecture of the OmpC–MlaA complex sheds light on the maintenance of outer membrane lipid asymmetry in Escherichia coli
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The architecture of the OmpC–MlaA complex sheds light on the maintenance of outer membrane lipid asymmetry in Escherichia coli

Yeow, Jiang ; Tan, Kang Wei ; Holdbrook, Daniel A. ; Chong, Zhi-Soon ; Marzinek, Jan K. ; Bond, Peter J. ; Chng, Shu-Sin

The Journal of biological chemistry, 2018-07, Vol.293 (29), p.11325-11340 [Periódico revisado por pares]

United States: Elsevier Inc

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13
The sensor of the bacterial histidine kinase CpxA is a novel dimer of extracytoplasmic Per-ARNT-Sim domains
The sensor of the bacterial histidine kinase CpxA is a novel dimer of extracytoplasmic Per-ARNT-Sim domains
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The sensor of the bacterial histidine kinase CpxA is a novel dimer of extracytoplasmic Per-ARNT-Sim domains

Cho, Timothy H.S. ; Murray, Cameron ; Malpica, Roxana ; Margain-Quevedo, Rodrigo ; Thede, Gina L. ; Lu, Jun ; Edwards, Ross A. ; Glover, J.N.Mark ; Raivio, Tracy L.

The Journal of biological chemistry, 2024-05, Vol.300 (5), p.107265-107265, Article 107265 [Periódico revisado por pares]

United States: Elsevier Inc

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14
Escherichia coli has robust regulatory mechanisms against elevated peptidoglycan cleavage by lytic transglycosylases
Escherichia coli has robust regulatory mechanisms against elevated peptidoglycan cleavage by lytic transglycosylases
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Escherichia coli has robust regulatory mechanisms against elevated peptidoglycan cleavage by lytic transglycosylases

Liang, Yaquan ; Zhao, Yilin ; Kwan, Jeric Mun Chung ; Wang, Yue ; Qiao, Yuan

The Journal of biological chemistry, 2023-04, Vol.299 (4), p.104615-104615, Article 104615 [Periódico revisado por pares]

United States: Elsevier Inc

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15
ClbP Is a Prototype of a Peptidase Subgroup Involved in Biosynthesis of Nonribosomal Peptides
ClbP Is a Prototype of a Peptidase Subgroup Involved in Biosynthesis of Nonribosomal Peptides
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ClbP Is a Prototype of a Peptidase Subgroup Involved in Biosynthesis of Nonribosomal Peptides

Dubois, Damien ; Baron, Olivier ; Cougnoux, Antony ; Delmas, Julien ; Pradel, Nathalie ; Boury, Michèle ; Bouchon, Bernadette ; Bringer, Marie-Agnès ; Nougayrède, Jean-Philippe ; Oswald, Eric ; Bonnet, Richard

The Journal of biological chemistry, 2011-10, Vol.286 (41), p.35562-35570 [Periódico revisado por pares]

United States: Elsevier Inc

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16
The FtsLB subcomplex of the bacterial divisome is a tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions
The FtsLB subcomplex of the bacterial divisome is a tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions
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The FtsLB subcomplex of the bacterial divisome is a tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions

Condon, Samson G.F. ; Mahbuba, Deena-Al ; Armstrong, Claire R. ; Diaz-Vazquez, Gladys ; Craven, Samuel J. ; LaPointe, Loren M. ; Khadria, Ambalika S. ; Chadda, Rahul ; Crooks, John A. ; Rangarajan, Nambirajan ; Weibel, Douglas B. ; Hoskins, Aaron A. ; Robertson, Janice L. ; Cui, Qiang ; Senes, Alessandro

The Journal of biological chemistry, 2018-02, Vol.293 (5), p.1623-1641 [Periódico revisado por pares]

United States: Elsevier Inc

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17
Mfd translocase is necessary and sufficient for transcription-coupled repair in Escherichia coli
Mfd translocase is necessary and sufficient for transcription-coupled repair in Escherichia coli
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Mfd translocase is necessary and sufficient for transcription-coupled repair in Escherichia coli

Adebali, Ogun ; Sancar, Aziz ; Selby, Christopher P.

The Journal of biological chemistry, 2017-11, Vol.292 (45), p.18386-18391 [Periódico revisado por pares]

United States: Elsevier Inc

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18
New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE
New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE
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New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE

Rossi, Maria-Agustina ; Pozhidaeva, Alexandra K ; Clerico, Eugenia M ; Petridis, Constantine ; Gierasch, Lila M

The Journal of biological chemistry, 2024-01, Vol.300 (1), p.105574-105574, Article 105574 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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19
Topological analyses of the L-lysine exporter LysO reveal a critical role for a conserved pair of intramembrane solvent-exposed acidic residues
Topological analyses of the L-lysine exporter LysO reveal a critical role for a conserved pair of intramembrane solvent-exposed acidic residues
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Topological analyses of the L-lysine exporter LysO reveal a critical role for a conserved pair of intramembrane solvent-exposed acidic residues

Dubey, Swati ; Majumder, Puja ; Penmatsa, Aravind ; Sardesai, Abhijit A.

The Journal of biological chemistry, 2021-10, Vol.297 (4), p.101168, Article 101168 [Periódico revisado por pares]

United States: Elsevier Inc

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20
Dimerization site 2 of the bacterial DNA-binding protein H-NS is required for gene silencing and stiffened nucleoprotein filament formation
Dimerization site 2 of the bacterial DNA-binding protein H-NS is required for gene silencing and stiffened nucleoprotein filament formation
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Dimerization site 2 of the bacterial DNA-binding protein H-NS is required for gene silencing and stiffened nucleoprotein filament formation

Yamanaka, Yuki ; Winardhi, Ricksen S. ; Yamauchi, Erika ; Nishiyama, So-ichiro ; Sowa, Yoshiyuki ; Yan, Jie ; Kawagishi, Ikuro ; Ishihama, Akira ; Yamamoto, Kaneyoshi

The Journal of biological chemistry, 2018-06, Vol.293 (24), p.9496-9505 [Periódico revisado por pares]

United States: Elsevier Inc

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