Escherichia coli DegP: a structure-driven functional model.
about
The Legionella HtrA homologue DegQ is a self-compartmentizing protease that forms large 12-meric assembliesProteolytic regulation of alginate overproduction in Pseudomonas aeruginosa.Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex.NlpI-mediated modulation of outer membrane vesicle production through peptidoglycan dynamics in Escherichia coli.Synthetic effect between envelope stress and lack of outer membrane vesicle production in Escherichia coli.Recent advances in understanding the assembly and repair of photosystem II.Thermal-triggerd proteinquake leads to disassembly of DegP hexamer as an imperative activation step.Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.Temperature dependent dynamics of DegP-trimer: A molecular dynamics study.
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Escherichia coli DegP: a structure-driven functional model.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 22 May 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Escherichia coli DegP: a structure-driven functional model.
@en
Escherichia coli DegP: a structure-driven functional model.
@nl
type
label
Escherichia coli DegP: a structure-driven functional model.
@en
Escherichia coli DegP: a structure-driven functional model.
@nl
prefLabel
Escherichia coli DegP: a structure-driven functional model.
@en
Escherichia coli DegP: a structure-driven functional model.
@nl
P2093
P2860
P356
P1476
Escherichia coli DegP: a structure-driven functional model.
@en
P2093
Ahmad Jomaa
Jack Iwanczyk
Joaquin Ortega
P2860
P304
P356
10.1128/JB.00472-09
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P577
2009-05-22T00:00:00Z