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Multidisciplinary Approaches to Cholinesterase Functions

Editat de Avigdor Shafferman, B. Velan
en Limba Engleză Paperback – 24 oct 2012

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Specificații

ISBN-13: 9781461363286
ISBN-10: 1461363284
Pagini: 316
Ilustrații: XVI, 293 p.
Dimensiuni: 178 x 254 x 17 mm
Greutate: 0.55 kg
Ediția:1992
Editura: Springer Us
Colecția Springer
Locul publicării:New York, NY, United States

Public țintă

Research

Cuprins

Impact of Recombinant DNA Technology and Protein Structure Determination on Past and Future Studies on Acetylcholinesterase.- Molecular Polymorphism.- Biosynthesis of the Molecular Forms of Acetylcholinesterase.- Binding of Asymmetric (A12) Acetylcholinesterase to C2 Muscle Cells and to CHO Mutants Defective in Glycosaminoglycan Synthesis.- Subunit Assembly and Glycosylation of Mammalian Brain Acetylcholinesterase.- Molecular Organization of Recombinant Human Acetylcholinesterase.- Expression and Refolding of Functional Human Butyrylcholinesterase from E. coli.- 1: Genetic Variant of Human Acetylcholinesterase - Part 2: SV-40 Transformed Cell Lines, for Example COS-1, but Not Parental Untransformed Cell Lines, Express Butyrylcholinesterase (BCHE).- Heterogeneity of the Silent Phenotype of Human Butyrylcholinesterase — Identification of Eight New Mutations.- Nematode Acetylcholinesterases: Several Genes and Molecular Forms of their Products.- Drosophila Acetylcholinesterase: Analysis of Structure and Sensitivity to Insecticides by In Vitro Mutagenesis and Expression.- Altered Form of Acetylcholinesterase in Insecticide-Resistant Houseflies (Musca domestica).- PCR Generated Homologous DNA Probes and Sequence for Acetylcholinesterase Genes in Insect Pests.- Testicular Gene Amplification and Impaired BChE Transcription Induced in Transgenic Mice by the Human BChE Coding Sequence.- Structure Function Relationship.- Three-Dimensional Structure of Acetylcholinesterase.- Sequence Alignment of Esterases and Lipases Based on 3-D Structures of Two Members of This Family.- Structural Analysis of Acetylcholinesterase Ammonium Binding Sites.- Structural Investigations of the Acetylcholinesterase.- Substrate-Selective Inhibition and Peripheral Site Labeling of Acetylcholinesteraseby Platinum (Terpyridine) Chloride.- Cryptic Catalysis and Cholinesterase Function.- Influence of Ionic Composition of the Medium on Acetylcholinesterase Conformation.- Molecular Dissection of Functional Domains in Human Cholinesterases Expressed in Microinjected Xenopus Oocytes.- Acetylcholinesterase Catalysis - Protein Engineering Studies.- Site-Directed Mutagenesis of Functional Residues in Torpedo Acetylcholinesterase.- Structurally Important Residues in the Region SER91 to ASN98 of Torpedo Acetylcholinesterase.- A Model of Butyryicholinesterase Based on the X-ray Structure of Acetylcholinesterase Indicates Differences in Specificity.- Molecular Models for Human AChE and its Phosphonylation Products.- Relationships Between Activity of Organophosphorus Inhibitors of Acetylcholinesterase and Accessibility of Phosphorus Atom as Estimated by Molecular Mechanics Calculations.- Physiological Role and Clinical Applications.- Factors Influencing Acetylcholinesterase Regulation in Slow and Fast Skeletal Muscles.- Compartmentalization of Acetylcholinesterase mRNA and Protein Expression in Skeletal Muscle In Vitro and In Vivo: Implications for Regulation at the Neuromuscular Junction.- Towards a Functional Analysis Cholinesterases in Neurogenesis: Histological, Molecular, and Regulatory Features of BChE from Chicken Brain.- Acetylcholinesterase as a Modulatory Neuroprotein and its Influence on Motor Control.- Different Influence of Inhibitors on Acetylcholinesterase Molecular Forms G1 and G4 Isolated from Alzheimer’s Disease and Control Brains.- Acetylcholinesterase Inhibition by Novel Carbamates: A Kinetic and Nuclear Magnetic Resonance Study.- Experimental Acetylcholinesterase Autoimmunity.- Clinical Implications of Cholinesterase Aberrations in Syndromes of HemopoieticCell Division.- Acetylcholinesterase: A Pretreatment Drug for Organophosphate Toxicity.- Recommendations for Nomenclature in Cholinesterases.