Cargando…

Flavin-Induced Oligomerization in Escherichia coli Adaptive Response Protein AidB

[Image: see text] The process known as “adaptive response” allows Escherichia coli to respond to small doses of DNA-methylating agents by upregulating the expression of four proteins. While the role of three of these proteins in mitigating DNA damage is well understood, the function of AidB is less...

Descripción completa

Detalles Bibliográficos
Autores principales:	Hamill, Michael J., Jost, Marco, Wong, Cintyu, Elliott, Sean J., Drennan, Catherine L.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	American Chemical Society 2011
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3217306/ https://www.ncbi.nlm.nih.gov/pubmed/22004173 http://dx.doi.org/10.1021/bi201340t

Ejemplares similares

Electrochemical Characterization of Escherichia coli Adaptive Response Protein AidB
por: Hamill, Michael J., et al.
Publicado: (2012)

Repair of DNA Alkylation Damage by the Escherichia coli Adaptive Response Protein AlkB as Studied by ESI-TOF Mass Spectrometry
por: Li, Deyu, et al.
Publicado: (2010)

The alkylation response protein AidB is localized at the new poles and constriction sites in Brucella abortus
por: Dotreppe, Delphine, et al.
Publicado: (2011)

Exocyclic Carbons Adjacent to the N(6) of Adenine are Targets for Oxidation by the Escherichia coli Adaptive Response Protein AlkB
por: Li, Deyu, et al.
Publicado: (2012)

Escherichia coli Fails to Efficiently Maintain the Activity of an Important Flavin Monooxygenase in Recombinant Overexpression
por: Milker, Sofia, et al.
Publicado: (2017)

Structural Insights into Catalytic Versatility of the Flavin-dependent Hydroxylase (HpaB) from Escherichia coli
por: Shen, Xiaolin, et al.
Publicado: (2019)

Structural Analysis of an Open Active Site Conformation of Nonheme Iron Halogenase CytC3
por: Wong, Cintyu, et al.
Publicado: (2009)

Removal of N-Alkyl Modifications from N(2)-Alkylguanine and N(4)-Alkylcytosine in DNA by the Adaptive Response Protein AlkB
por: Li, Deyu, et al.
Publicado: (2013)

Broadening the Scope of the Flavin‐Tag Method by Improving Flavin Incorporation and Incorporating Flavin Analogs
por: Tong, Yapei, et al.
Publicado: (2022)

The FAD Cofactor of RebC Shifts to an IN Conformation upon Flavin Reduction(,)
por: Ryan, Katherine S., et al.
Publicado: (2008)

Crystallographic Evidence of Drastic Conformational Changes in the Active Site of a Flavin-Dependent N-Hydroxylase
por: Setser, Jeremy W., et al.
Publicado: (2014)

Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases
por: Sydor, Andrew M., et al.
Publicado: (2013)

Correction to Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases
por: Sydor, Andrew M., et al.
Publicado: (2013)

Factors Defining the Functional Oligomeric State of Escherichia coli DegP Protease
por: Iwanczyk, Jack, et al.
Publicado: (2011)

The Oligomeric Form of the Escherichia coli Dps Protein Depends on the Availability of Iron Ions
por: Antipov, Sergey, et al.
Publicado: (2017)

Direct Electrochemical Analyses of a Thermophilic Thioredoxin Reductase: Interplay between Conformational Change and Redox Chemistry
por: Hamill, Michael J., et al.
Publicado: (2008)

Oligomerization and DNA binding of Ler, a master regulator of pathogenicity of enterohemorrhagic and enteropathogenic Escherichia coli
por: García, Jesús, et al.
Publicado: (2012)

Functional Irreplaceability of Escherichia coli and Shewanella oneidensis OxyRs Is Critically Determined by Intrinsic Differences in Oligomerization
por: Sun, Weining, et al.
Publicado: (2022)

A Set of Engineered Escherichia coli Expression Strains for Selective Isotope and Reactivity Labeling of Amino Acid Side Chains and Flavin Cofactors
por: Mehlhorn, Jennifer, et al.
Publicado: (2013)

A nucleotide-dependent oligomerization of the Escherichia coli replication initiator DnaA requires residue His136 for remodeling of the chromosomal origin
por: Saxena, Rahul, et al.
Publicado: (2020)

Escherichia coli transcription termination factor NusA: heat-induced oligomerization and chaperone activity
por: Li, Kun, et al.
Publicado: (2013)

Biocatalytic Enantioselective Oxidation of Sec‐Allylic Alcohols with Flavin‐Dependent Oxidases
por: Gandomkar, Somayyeh, et al.
Publicado: (2019)

Flavine in Ophthalmic Practice
por: Ganguli, P.
Publicado: (1920)

Flavine in Ophthalmic Practice
por: Ganguli, P.
Publicado: (1921)

Flavine: the Ideal Antiseptic
Publicado: (1917)

The Antiseptic “Flavine” (Acriflavine)
Publicado: (1918)

Imprecision of Adaptation in Escherichia coli Chemotaxis
por: Neumann, Silke, et al.
Publicado: (2014)

CRISPR-Cas adaptation in Escherichia coli
por: Mitić, Damjan, et al.
Publicado: (2023)

Structural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric Structure
por: Zhang, Yi, et al.
Publicado: (2014)

Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli
por: Zimanyi, Christina M, et al.
Publicado: (2016)

Structural Basis of Low-Affinity Nickel Binding to the Nickel-Responsive Transcription Factor NikR from Escherichia coli
por: Phillips, Christine M., et al.
Publicado: (2010)

Inhibiting translation elongation can aid genome duplication in Escherichia coli
por: Myka, Kamila K., et al.
Publicado: (2017)

New Light in Flavin Autofluorescence
por: Croce, A.C., et al.
Publicado: (2015)

Flavine as a Therapeutic Agent
por: Ganguli, P.
Publicado: (1922)

Note on the Germicidal Power of Flavine
Publicado: (1917)

EXPERIMENTS ON THE ADAPTATION OF ESCHERICHIA COLI TO SODIUM CHLORIDE
por: Doudoroff, Michael
Publicado: (1940)

Chemotactic Response and Adaptation Dynamics in Escherichia coli
por: Clausznitzer, Diana, et al.
Publicado: (2010)

Evolution of enzyme functionality in the flavin-containing monooxygenases
por: Bailleul, Gautier, et al.
Publicado: (2023)

Crystallographic and thermodynamic evidence of negative cooperativity of flavin and tryptophan binding in the flavin-dependent halogenases AbeH and BorH
por: Ashaduzzaman, Md, et al.
Publicado: (2023)

Trade-Offs of Escherichia coli Adaptation to an Intracellular Lifestyle in Macrophages
por: Azevedo, M., et al.
Publicado: (2016)

Cannot write session to /tmp/vufind_sessions/sess_bh7rj0tgh6jbljf4ns578hmv3s