Cargando…

The MoxR ATPase RavA and Its Cofactor ViaA Interact with the NADH:Ubiquinone Oxidoreductase I in Escherichia coli

MoxR ATPases are widespread throughout bacteria and archaea. The experimental evidence to date suggests that these proteins have chaperone-like roles in facilitating the maturation of dedicated protein complexes that are functionally diverse. In Escherichia coli, the MoxR ATPase RavA and its putativ...

Descripción completa

Detalles Bibliográficos
Autores principales:	Wong, Keith S., Snider, Jamie D., Graham, Chris, Greenblatt, Jack F., Emili, Andrew, Babu, Mohan, Houry, Walid A.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2014
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3893208/ https://www.ncbi.nlm.nih.gov/pubmed/24454883 http://dx.doi.org/10.1371/journal.pone.0085529

Ejemplares similares

Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex
por: Jessop, Matthew, et al.
Publicado: (2020)

Quantification of NADH:ubiquinone oxidoreductase (complex I) content in biological samples
por: Ansari, Fariha, et al.
Publicado: (2021)

The Subunit Composition of Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I) From Pichia pastoris
por: Bridges, Hannah R., et al.
Publicado: (2010)

Reduction of Hydrophilic Ubiquinones by the Flavin in Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I) and Production of Reactive Oxygen Species
por: King, Martin S., et al.
Publicado: (2009)

The RavA-ViaA chaperone complex modulates bacterial persistence through its association with the fumarate reductase enzyme
por: Bhandari, Vaibhav, et al.
Publicado: (2023)

Effects of the deletion of the Escherichia coli frataxin homologue CyaY on the respiratory NADH:ubiquinone oxidoreductase
por: Pohl, Thomas, et al.
Publicado: (2007)

The AAA+ ATPase RavA and its binding partner ViaA modulate E. coli aminoglycoside sensitivity through interaction with the inner membrane
por: Felix, Jan, et al.
Publicado: (2022)

Clinical Relevance and Tumor Growth Suppression of Mitochondrial ROS Regulators along NADH:Ubiquinone Oxidoreductase Subunit B3 in Thyroid Cancer
por: Zhu, Jiao, et al.
Publicado: (2022)

Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA
por: Kandiah, Eaazhisai, et al.
Publicado: (2016)

Origin and Evolution of the Sodium -Pumping NADH: Ubiquinone Oxidoreductase
por: Reyes-Prieto, Adrian, et al.
Publicado: (2014)

A novel drug for uncomplicated malaria: targeted high throughput screening (HTS) against the type II NADH:ubiquinone oxidoreductase (PfNdh2) of Plasmodium falciparum
por: Ward, Steve A, et al.
Publicado: (2010)

Cryo-EM structures of Na(+)-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae
por: Kishikawa, Jun-ichi, et al.
Publicado: (2022)

The RavA/VemR two‐component system plays vital regulatory roles in the motility and virulence of Xanthomonas campestris
por: Lin, Maojuan, et al.
Publicado: (2021)

Mycobacterium tuberculosis protein MoxR1 enhances virulence by inhibiting host cell death pathways and disrupting cellular bioenergetics
por: Quadir, Neha, et al.
Publicado: (2023)

Interaction of Mycobacterium tuberculosis Virulence Factor RipA with Chaperone MoxR1 Is Required for Transport through the TAT Secretion System
por: Bhuwan, Manish, et al.
Publicado: (2016)

In vitro characterization of mitochondrial function and structure in rat and human cells with a deficiency of the NADH: ubiquinone oxidoreductase Ndufc2 subunit
por: Raffa, Salvatore, et al.
Publicado: (2017)

Insights into the structure-function relationship of the NorQ/NorD chaperones from Paracoccus denitrificans reveal shared principles of interacting MoxR AAA+/VWA domain proteins
por: Kahle, Maximilian, et al.
Publicado: (2023)

Oxidoreductases and metal cofactors in the functioning of the earth
por: Hay Mele, Bruno, et al.
Publicado: (2023)

The mechanism of catalysis by type-II NADH:quinone oxidoreductases
por: Blaza, James N., et al.
Publicado: (2017)

RAVA: Region-Based Average Video Quality Assessment
por: Wu, Xuanyi, et al.
Publicado: (2021)

A novel cytosolic NADH:quinone oxidoreductase from Methanothermobacter marburgensis
por: Ullmann, Eva, et al.
Publicado: (2014)

Regulation of the mechanism of Type-II NADH: Quinone oxidoreductase from S. aureus
por: Sena, Filipa V., et al.
Publicado: (2018)

Occurrence and Function of the Na(+)-Translocating NADH:Quinone Oxidoreductase in Prevotella spp.
por: Deusch, Simon, et al.
Publicado: (2019)

Therapeutic potential of chrysin nanoparticle-mediation inhibition of succinate dehydrogenase and ubiquinone oxidoreductase in pancreatic and lung adenocarcinoma
por: Ragab, Eman M., et al.
Publicado: (2022)

Ubiquinone binding site of yeast NADH dehydrogenase revealed by structures binding novel competitive- and mixed-type inhibitors
por: Yamashita, Tetsuo, et al.
Publicado: (2018)

CMY-1/MOX-family AmpC β-lactamases MOX-1, MOX-2 and MOX-9 were mobilized independently from three Aeromonas species
por: Ebmeyer, Stefan, et al.
Publicado: (2019)

Mutation of a distal gating residue modulates NADH binding in NADH:Quinone oxidoreductase from Pseudomonas aeruginosa PAO1
por: Moni, Bilkis Mehrin, et al.
Publicado: (2023)

Role of NADH: quinone oxidoreductase-1 in the tight junctions of colonic epithelial cells
por: Nam, Seung Taek, et al.
Publicado: (2014)

The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductase
por: Folgosa, Filipe, et al.
Publicado: (2018)

Cyclic-di-GMP binds to histidine kinase RavS to control RavS-RavR phosphotransfer and regulates the bacterial lifestyle transition between virulence and swimming
por: Cheng, Shou-Ting, et al.
Publicado: (2019)

Chemical Nature and Reaction Mechanisms of the Molybdenum Cofactor of Xanthine Oxidoreductase
por: Okamoto, Ken, et al.
Publicado: (2013)

Nanobiocatalysts with inbuilt cofactor recycling for oxidoreductase catalysis in organic solvents
por: Sahlin, Jenny, et al.
Publicado: (2023)

Development of a novel drug for uncomplicated malaria targeting the mitochondrial NADH:quinone oxidoreductase
por: Biagini, Giancarlo A, et al.
Publicado: (2010)

Structural and Functional insights into the catalytic mechanism of the Type II NADH:quinone oxidoreductase family
por: Marreiros, Bruno C., et al.
Publicado: (2017)

The Profound Influence of Lipid Composition on the Catalysis of the Drug Target NADH Type II Oxidoreductase
por: Godoy-Hernandez, Albert, et al.
Publicado: (2021)

Unlocking the Antibiofilm Potential of Natural Compounds by Targeting the NADH:quinone Oxidoreductase WrbA
por: Ratti, Alessandro, et al.
Publicado: (2023)

Conformational coupling of redox-driven Na(+)-translocation in Vibrio cholerae NADH:quinone oxidoreductase
por: Hau, Jann-Louis, et al.
Publicado: (2023)

A Self‐Assembled Respiratory Chain that Catalyzes NADH Oxidation by Ubiquinone‐10 Cycling between Complex I and the Alternative Oxidase
por: Jones, Andrew J. Y., et al.
Publicado: (2015)

Cofactor engineering to regulate NAD(+)/NADH ratio with its application to phytosterols biotransformation
por: Su, Liqiu, et al.
Publicado: (2017)

Distribution of valence electrons of the flavin cofactor in NADH-cytochrome b(5) reductase
por: Takaba, Kiyofumi, et al.
Publicado: (2017)

Cannot write session to /tmp/vufind_sessions/sess_jots0av1ns86k0vukgmdu2jeet