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  • Book
    Avinash Kale, editor.
    Contents:
    Intro; Preface; Contents; About the Editor; Abbreviations;
    1: Actin Polymerization: A Cellular Perspective for Motility; 1.1 Introduction; 1.1.1 Cancer and Polycystic Ovarian Syndrome (PCOS); 1.1.2 Age-Related Neurodegenerative Disorders; 1.2 Actin: A Vital Player in Cell Motility; 1.2.1 Swimming: A Cellular Motility Phenomenon; 1.2.2 Actin-Driven Cellular Motility; 1.2.2.1 Directional Motility; 1.2.2.2 Cytokinesis; 1.2.2.3 Organelle Transport and Protein Trafficking; 1.3 Gliding Motility; 1.3.1 Gliding Motility in Apicomplexan; Bibliography
    2: Actin: The Central Ubiquitous Player in the Phenomenon2.1 Introduction; 2.2 Sequence Analysis of the G-Actin; 2.3 Structure of G-Actin; 2.3.1 3D Structure of G-Actin; 2.3.1.1 Architecture of G-Actin; 2.3.1.2 Loops; 2.3.1.2.1 S-Loop (Residues 11-16) and G-Loop (Residues 154-161); 2.3.1.2.2 H-Loop (Residues70-78); 2.3.1.3 Dnase-Binding Loop (D-Loop, Residues 38-52); 2.3.1.4 Loop 60-69; 2.3.1.5 W-Loop (Residues 165-172); 2.3.1.6 Hydrophobic Plug (H-Plug) (Residues 264-273); 2.3.1.7 C-Terminal (Residues 349-375) and N-Terminal (Residues 1-10) Loops; 2.4 Role of Metal Ions 2.5 Conformational States of Actin2.6 Upsi-Phosphate Sensing; 2.7 Filamentous Actin (F-Actin); 2.7.1 Actin Polymerization; 2.8 Mechanism of Actin Polymerization; 2.9 Kinetics of Actin Polymerization; 2.10 Thermodynamics of Actin Polymerization; 2.11 Stability of Actin Filament; 2.12 Drugs Binding to Actin; Bibliography;
    3: Formin: The Multidomain Elongator of Actin Polymer; 3.1 Introduction; 3.2 Localization; 3.3 Function; 3.4 Domain Organization; 3.4.1 Formin Homology-1 (FH1) Domain; 3.4.2 Formin Homology-2 (FH2) Domain; 3.4.3 Diaphanous Autoregulatory Domain (DAD) 3.4.4 Other Accessory Domains3.4.5 Domain-Isotype Relationship; Bibliography;
    4: Profilin: The Associates of Formin; 4.1 Introduction; 4.2 Functions; 4.3 Structure; 4.4 Binding Partners of Profilin; 4.5 Poly-Proline-Binding Site; 4.6 Actin-Binding Sites; 4.7 Affinity of Profilin for Actin; 4.8 Hydrophobic Core; 4.9 Regulators of Profilin; Bibliography;
    5: ADF (Actin Depolymerizing Factor): The Breaker of the Polymer in Homeostasis; 5.1 Introduction; 5.2 Isoforms of ADF; 5.3 Functions; 5.4 Structure; 5.5 Stability of ADF; 5.6 Regulators of ADF; 5.6.1 PIP2; 5.6.2 Phosphorylation; 5.6.3 pH
    Digital Access Springer 2019
  • Article
    Hara T, Matsuda M, Yoneda M.
    Biken J. 1977 Dec;20(3-4):105-15.
    Nontoxigenic derivatives of a toxigenic strain of Clostridium tetani were isolated gy treatment with acridine orange, N-methyl-N'-nitro-soguanidine, rifampicin or ultraviolet light. The frequency of appearance fo non-toxigenic derivatives on these treatments was 0.8 to 3.2 per cent. The nontoxigenic derivatives peoduced all the same extracellular antigenic and protein components as the toxigenic parent strain, except the toxin and materials cross-reacting with the toxin. The nontoxigenic strains, like the toxigenic parent strain, were lyzed by trratment with mitomycin C. Bacteriophage was detected in the lysates of all the nontoxigenic derivatives produced with mitomycin C, and this bacteriophage was morphologically indistinguishable from that obtained from the toxigenic parent strain. The genetic factor controlling tetanus toxin production is discussed.
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