Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin - Test2 - elhamkhani - TriplyDB

Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin

Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin

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Pertussis toxin and adenylate cyclase toxin: key virulence factors of Bordetella pertussis and cell biology tools Molecular details of cAMP generation in mammalian cells: a tale of two systems RTX proteins: a highly diverse family secreted by a common mechanism Bacillus anthracis edema factor substrate specificity: evidence for new modes of action A 1.3-Å Structure of Zinc-bound N-terminal Domain of Calmodulin Elucidates Potential Early Ion-binding Step The vacuolar transporter chaperone (VTC) complex is required for microautophagy Bordetella adenylate cyclase toxin interacts with filamentous haemagglutinin to inhibit biofilm formation in vitro.The Bordetella adenylate cyclase repeat-in-toxin (RTX) domain is immunodominant and elicits neutralizing antibodies.Delivery of large heterologous polypeptides across the cytoplasmic membrane of antigen-presenting cells by the Bordetella RTX hemolysin moiety lacking the adenylyl cyclase domain.Vibrio vulnificus biotype 3 multifunctional autoprocessing RTX toxin is an adenylate cyclase toxin essential for virulence in mice Elucidating the mechanisms of cooperative calcium-calmodulin interactions: a structural systems biology approach.Use of allostery to identify inhibitors of calmodulin-induced activation of Bacillus anthracis edema factor.Bis-halogen-anthraniloyl-substituted nucleoside 5'-triphosphates as potent and selective inhibitors of Bordetella pertussis adenylyl cyclase toxin.Pseudomonas aeruginosa exotoxin Y-mediated tau hyperphosphorylation impairs microtubule assembly in pulmonary microvascular endothelial cells.Effects of 39 Compounds on Calmodulin-Regulated Adenylyl Cyclases AC1 and Bacillus anthracis Edema Factor Kinetic regulation of multi-ligand binding proteins.Sensor-response regulator interactions in a cross-regulated signal transduction network.Analysis of Membrane Protein Interactions with a Bacterial Adenylate Cyclase-Based Two-Hybrid (BACTH) Technique.Crystallization of the class IV adenylyl cyclase from Yersinia pestis.CaMELS: In silico prediction of calmodulin binding proteins and their binding sites.Order-disorder-order transitions mediate the activation of cholera toxin.Bacillus anthracis edema toxin activates nuclear glycogen synthase kinase 3beta.Virulence factor secretion and translocation by Bordetella species.The adenylyl cyclase activity of anthrax edema factor.Interactions of Bordetella pertussis adenylyl cyclase toxin CyaA with calmodulin mutants and calmodulin antagonists: comparison with membranous adenylyl cyclase I.Targeting bacterial toxins.Biological roles of cAMP: variations on a theme in the different kingdoms of life.Design and Synthesis of Fluorescent Acyclic Nucleoside Phosphonates as Potent Inhibitors of Bacterial Adenylate Cyclases.Bisamidate Prodrugs of 2-Substituted 9-[2-(Phosphonomethoxy)ethyl]adenine (PMEA, adefovir) as Selective Inhibitors of Adenylate Cyclase Toxin from Bordetella pertussis.Interaction with adenylate cyclase toxin from Bordetella pertussis affects the metal binding properties of calmodulin.Amidate prodrugs of 9-[2-(phosphonomethoxy)ethyl]adenine as inhibitors of adenylate cyclase toxin from Bordetella pertussis.Molecular Modeling of the Catalytic Domain of CyaA Deepened the Knowledge of Its Functional Dynamics.Inhibition of the adenylyl cyclase toxin, edema factor, from Bacillus anthracis by a series of 18 mono- and bis-(M)ANT-substituted nucleoside 5'-triphosphates.Negatively charged residues of the segment linking the enzyme and cytolysin moieties restrict the membrane-permeabilizing capacity of adenylate cyclase toxin.Block V RTX Domain of Adenylate Cyclase from Bordetella pertussis: A Conformationally Dynamic Scaffold for Protein Engineering Applications.Allosteric activation of Bordetella pertussis adenylyl cyclase by calmodulin: molecular dynamics and mutagenesis studies Cytidylyl and uridylyl cyclase activity of bacillus anthracis edema factor and Bordetella pertussis CyaA.Different Roles of N-Terminal and C-Terminal Domains in Calmodulin for Activation of Bacillus anthracis Edema Factor.Protein-protein docking and analysis reveal that two homologous bacterial adenylyl cyclase toxins interact with calmodulin differently.Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin.

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Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin

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2005 nî lūn-bûn

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2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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Structural basis for the inter ...... cyclase toxin with calmodulin

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Structural basis for the inter ...... cyclase toxin with calmodulin

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Structural basis for the inter ...... cyclase toxin with calmodulin

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Structural basis for the inter ...... cyclase toxin with calmodulin

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Structural basis for the inter ...... cyclase toxin with calmodulin

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Structural basis for the inter ...... cyclase toxin with calmodulin

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Structural basis for the inter ...... cyclase toxin with calmodulin

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Structural basis for the inter ...... cyclase toxin with calmodulin

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Structural basis for the inter ...... cyclase toxin with calmodulin

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The EMBO Journal

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Structural basis for the inter ...... cyclase toxin with calmodulin

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Craig S Gibbs

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Qing Guo

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Young-Sam Lee

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Yuequan Shen

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P2860

Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin

Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin

Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor.

Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection

Pertussis toxin and adenylate cyclase toxin provide a one-two punch for establishment of Bordetella pertussis infection of the respiratory tract

The adenylate cyclase toxin of Bordetella pertussis binds to target cells via the alpha(M)beta(2) integrin (CD11b/CD18)

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin

Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins

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10.1038/SJ.EMBOJ.7600800

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18

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24

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2005-09-21T00:00:00Z

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7623349

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16138079

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Bordetella pertussis

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1224690

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