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| Author | : Martin Johan Olof Widenbrant |
| Publisher | : |
| Total Pages | : 380 |
| Release | : 2007 |
| Genre | : |
| ISBN | : |
| Author | : Sidney A. Simon |
| Publisher | : Academic Press |
| Total Pages | : 606 |
| Release | : 2002-11-13 |
| Genre | : Science |
| ISBN | : 0080925855 |
This volume contains a comprehensive overview of peptide-lipid interactions by leading researchers. The first part covers theoretical concepts, experimental considerations, and thermodynamics. The second part presents new results obtained through site-directed EPR, electron microscopy, NMR, isothermal calorimetry, and fluorescence quenching. The final part covers problems of biological interest, including signal transduction, membrane transport, fusion, and adhesion. Key Features * world-renowned experts * state-of-the-art experimental methods * monolayers, bilayers, biological membranes * theoretical aspects and computer simulations * rafts * synaptic transmission * membrane fusion * signal transduction
| Author | : Raz Jelinek |
| Publisher | : John Wiley & Sons |
| Total Pages | : 431 |
| Release | : 2011-04-27 |
| Genre | : Science |
| ISBN | : 3527634339 |
Addressing one of the biggest riddles in current molecular cell biology, this ground-breaking monograph builds the case for the crucial involvement of lipids and membranes in the formation of amyloid deposits. Tying together recent knowledge from in vitro and in vivo studes, and built on a sound biophysical and biochemical foundation, this overview brings the reader up to date with current models of the interplay between membranes and amyloid formation. Required reading for any researcher interested in amyloid formation and amyloid toxicity, and possible avenues for the prevention or treatment of neurodegenerative disorders. From the contents: * Interactions of Alpha-Synuclein with Lipids * Interaction of hIAPP and its Precursors with Membranes * Amyloid Polymorphisms: Structural Basis and Significance in Biology and Molecular Medicine * The Role of Lipid Rafts in Alzheimer's Disease * Alzheimer's Disease as a Membrane-Associated Enzymopathy of Beta-Amyloid Precursor Protein (APP) Secretases * Impaired Regulation of Glutamate Receptor Channels and Signaling Molecules by Beta-Amyloid in Alzheimer's Disease * Membrane Changes in BSE and Scrapie * Experimental Approaches and Technical Challenges for Studying Amyloid-Membrane Interactions and more
| Author | : Olga Gursky |
| Publisher | : Springer |
| Total Pages | : 270 |
| Release | : 2015-07-06 |
| Genre | : Science |
| ISBN | : 3319173448 |
Protein conversion from a water-soluble native conformation to the insoluble aggregates and fibrils, which can deposit in amyloid plaques, underlies more than 20 human diseases, representing a major public health problem and a scientific challenge. Such a conversion is called protein misfolding. Protein misfolding can also involve errors in the topology of the folded proteins and their assembly in lipid membranes. Lipids are found in nearly all amyloid deposits in vivo, and can critically influence protein misfolding in vitro and in vivo in many different ways. This book focuses on recent advances in our understanding of the role of lipids in modulating the misfolding of various proteins. The main emphasis is on the basic biophysical studies that address molecular basis of protein misfolding and amyloid formation, and the role of lipids in this complex process.
| Author | : Natasha S. Barteneva |
| Publisher | : Humana |
| Total Pages | : 0 |
| Release | : 2015-11-23 |
| Genre | : Medical |
| ISBN | : 9781493933006 |
This detailed volume for the first time explores techniques and protocols involving quantitative imaging flow cytometry (IFC), which has revolutionized our ability to analyze cells, cellular clusters, and populations in a remarkable fashion. Beginning with an introduction to technology, the book continues with sections addressing protocols for studies on the cell nucleus, nucleic acids, and FISH techniques using an IFC instrument, immune response analysis and drug screening, IFC protocols for apoptosis and cell death analysis, as well as morphological analysis and the identification of rare cells. Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Imaging Flow Cytometry: Methods and Protocols will be a critical source for all laboratories seeking to implement IFC in their research studies.
| Author | : |
| Publisher | : |
| Total Pages | : |
| Release | : 2010 |
| Genre | : |
| ISBN | : |
| Author | : A.D. Roses |
| Publisher | : Springer Science & Business Media |
| Total Pages | : 208 |
| Release | : 2012-12-06 |
| Genre | : Medical |
| ISBN | : 3642801099 |
There is now considerable genetic evidence that the type 4 allele of the apolipoprotein E gene is a major susceptibility factor associated with late-onset Alzheimer's disease, the common form of the disease defined as starting after sixty years of age. The role of apolipoprotein E in normal brain metabolism and in the pathogenesis of Alzheimer's disease are new and exciting avenues of research. This book, written by the most outstanding scientists in this new filed, is the first presentation of results concerning the implications of apolipoprotein E on the genetics, cell biology, neuropathology, biochemistry, and therapeutic management of Alzheimer's disease.
| Author | : Wei Qi |
| Publisher | : |
| Total Pages | : 320 |
| Release | : 2009 |
| Genre | : |
| ISBN | : |
| Author | : E. Edward Bittar |
| Publisher | : JAI Press(NY) |
| Total Pages | : 0 |
| Release | : 1997 |
| Genre | : Cell-mediated cytotoxicity |
| ISBN | : 9780762301416 |
Cellular toxicology has entered a new era. No longer are we concerned only with necrotic cell death produced by severe, acute insult (often to multiple intracellular targets) leading to disruption of the cell membrane. New advances in molecular and cellular biology are allowing the dissection of mechanisms of cell death involving more subtle targets within the cell. Toxicology has been very important, not only in understanding the mechanisms, nature, and severity of toxicity and thereby helping in risk assessment, but toxicology has also played a very important role in helping to understand basic biological processes. Historically this has perhaps been most evident in the use of toxic agents to interfere with specific reactions in the body and hence help to dissect out the mechanisms of metabolic processes. For example, the use of chemical inhibitors was very important in understanding the process of oxidative phosphorylation, or the tricarboxylic acid cycle. More recent examples are seen herein where toxicology interfaces with, for example structural biology in the study of the cytoskeletal components and their interactions. Indirectly, an understanding of the mechanisms of endogenous protective systems also improves knowledge of basic cell biology. Toxic insult and manipulation of cell signalling and control mechanisms in cell growth and differentation also highlight how important the discipline of cell toxicity has been and will continue to be a major contributor to our understanding of basic issues in the biological and biomedical sciences. This book offers selected reviews of some of the principal molecular mechanisms of cell toxicity.
| Author | : Jian Xiong |
| Publisher | : |
| Total Pages | : 94 |
| Release | : 2014 |
| Genre | : |
| ISBN | : |
The amyloid-[beta] (A[beta]) peptide, a major component of the insoluble plaques associated with Alzheimer’s disease (AD), is the cleavage product of the transmembrane (TM) amyloid precursor protein (APP) and is known to possess amiphiphilic nature. To better understand the aggregation propensity and the role of peptide-membrane interactions in AD, knowledge about how small molecule and membrane characteristics affect binding, solvation, and secondary structure of A[beta]. Two site mutants, Ab(25-40) G37A and I32A, have been designed to interrupt the peptide backbone hydrogen bonding as well as reduce hydrophobic interactions. Further Thioflavin T (ThT) assays and circular dichroism (CD) results indicate that the hydrophobic interactions may be crucial in A[beta](25-40)’s intrinsic aggregation propensity and also play an important role in the interaction of between myricetin and A[beta]. Deep-ultraviolet resonance Raman (dUVRR) and size exclusion chromatography (SEC) experiments suggest that the various initial oligomeric state may contributes to the altered A[beta](25-40) property. Ab(25-40) is also found to spontaneously associate with anionic lipid bilayers and the structure of the membrane associated Ab(25-40) was depend on both the hydrophobic thickness of the bilayer and duration of incubation. Further studies regarding the full lengths peptide indicates similarity between Ab(25-40) and Ab(1-40). After spontaneously associating with negatively charged lipid bilayer, the full length Ab(1-40) initially adopts a mixed confirmation of [alpha]-helical and disordered structures. The mixed structures, then convert to a more b-sheet structures over longer timeframes, compared to the initial stage. b-sheet structure appears prior to the unwinding of [alpha]-helix, implying a progress in which b-sheet structure, formed initially from disordered regions, destabilized membrane solvated helical structure and then lead to the escape of peptide from the membrane surfaces. In order to better define dUVRR characteristics of membrane associated/solvated protein secondary structure and establish potential quantitative relationships between the spectral response and the size of protein TM domain, a series of model peptides, poly-(LA)x, were designed based on known TM helical peptide. It is found that both the length of the TM region of the peptide and the hydrophobic thicknesses determined by the lipid bilayer play important roles in the confirmation of the final adopted structure, while the overall peptide secondary structures are predictable based on the TM region/ hydrophobic thicknesses ratio and lipid bilayer composition.
