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Aggregation-induced emission. : materials and applications
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ISBN: 0841231575 Year: 2016 Publisher: Washington, District of Columbia : American Chemical Society : Oxford University Press,

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Biofilms : characterization, applications and recent advances
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ISBN: 1536101524 9781536101522 9781536101386 1536101389 Year: 2016 Publisher: New York : Nova Publishers,

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Protein Solubility and Aggregation in Bacteria
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Year: 2016 Publisher: Frontiers Media SA

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Proteins suffer many conformational changes and interactions through their life, from their synthesis at ribosomes to their controlled degradation. Only folded and soluble proteins are functional. Thus, protein folding and solubility are controlled genetically, transcriptionally, and at the protein sequence level. In addition, a well-conserved cellular machinery assists the folding of polypeptides to avoid misfolding and ensure the attainment of soluble and functional structures. When these redundant protective strategies are overcome, misfolded proteins are recruited into aggregates. Recombinant protein production is an essential tool for the biotechnology industry and also supports expanding areas of basic and biomedical research, including structural genomics and proteomics. Although bacteria still represent a convenient production system, many recombinant polypeptides produced in prokaryotic hosts undergo irregular or incomplete folding processes that usually result in their accumulation as insoluble aggregates, narrowing thus the spectrum of protein-based drugs that are available in the biotechnology market. In fact, the solubility of bacterially produced proteins is of major concern in production processes, and many orthogonal strategies have been exploited to try to increase soluble protein yields. Importantly, contrary to the usual assumption that the bacterial aggregates formed during protein production are totally inactive, the presence of a fraction of molecules in a native-like structure in these assemblies endorse them with a certain degree of biological activity, a property that is allowing the use of bacteria as factories to produce new functional materials and catalysts. The protein embedded in intracellular bacterial deposits might display different conformations, but they are usually enriched in beta-sheet-rich assemblies resembling the amyloid fibrils characteristic of several human neurodegenerative diseases. This makes bacterial cells simple, but biologically relevant model systems to address the mechanisms behind amyloid formation and the cellular impact of protein aggregates. Interestingly, bacteria also exploit the structural principles behind amyloid formation for functional purposes such as adhesion or cytotoxicity. In the present research topic we collect papers addressing all the issues mentioned above from both the experimental and computational point of view.


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Protein Solubility and Aggregation in Bacteria
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Year: 2016 Publisher: Frontiers Media SA

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Proteins suffer many conformational changes and interactions through their life, from their synthesis at ribosomes to their controlled degradation. Only folded and soluble proteins are functional. Thus, protein folding and solubility are controlled genetically, transcriptionally, and at the protein sequence level. In addition, a well-conserved cellular machinery assists the folding of polypeptides to avoid misfolding and ensure the attainment of soluble and functional structures. When these redundant protective strategies are overcome, misfolded proteins are recruited into aggregates. Recombinant protein production is an essential tool for the biotechnology industry and also supports expanding areas of basic and biomedical research, including structural genomics and proteomics. Although bacteria still represent a convenient production system, many recombinant polypeptides produced in prokaryotic hosts undergo irregular or incomplete folding processes that usually result in their accumulation as insoluble aggregates, narrowing thus the spectrum of protein-based drugs that are available in the biotechnology market. In fact, the solubility of bacterially produced proteins is of major concern in production processes, and many orthogonal strategies have been exploited to try to increase soluble protein yields. Importantly, contrary to the usual assumption that the bacterial aggregates formed during protein production are totally inactive, the presence of a fraction of molecules in a native-like structure in these assemblies endorse them with a certain degree of biological activity, a property that is allowing the use of bacteria as factories to produce new functional materials and catalysts. The protein embedded in intracellular bacterial deposits might display different conformations, but they are usually enriched in beta-sheet-rich assemblies resembling the amyloid fibrils characteristic of several human neurodegenerative diseases. This makes bacterial cells simple, but biologically relevant model systems to address the mechanisms behind amyloid formation and the cellular impact of protein aggregates. Interestingly, bacteria also exploit the structural principles behind amyloid formation for functional purposes such as adhesion or cytotoxicity. In the present research topic we collect papers addressing all the issues mentioned above from both the experimental and computational point of view.


Book
Protein Solubility and Aggregation in Bacteria
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Year: 2016 Publisher: Frontiers Media SA

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Abstract

Proteins suffer many conformational changes and interactions through their life, from their synthesis at ribosomes to their controlled degradation. Only folded and soluble proteins are functional. Thus, protein folding and solubility are controlled genetically, transcriptionally, and at the protein sequence level. In addition, a well-conserved cellular machinery assists the folding of polypeptides to avoid misfolding and ensure the attainment of soluble and functional structures. When these redundant protective strategies are overcome, misfolded proteins are recruited into aggregates. Recombinant protein production is an essential tool for the biotechnology industry and also supports expanding areas of basic and biomedical research, including structural genomics and proteomics. Although bacteria still represent a convenient production system, many recombinant polypeptides produced in prokaryotic hosts undergo irregular or incomplete folding processes that usually result in their accumulation as insoluble aggregates, narrowing thus the spectrum of protein-based drugs that are available in the biotechnology market. In fact, the solubility of bacterially produced proteins is of major concern in production processes, and many orthogonal strategies have been exploited to try to increase soluble protein yields. Importantly, contrary to the usual assumption that the bacterial aggregates formed during protein production are totally inactive, the presence of a fraction of molecules in a native-like structure in these assemblies endorse them with a certain degree of biological activity, a property that is allowing the use of bacteria as factories to produce new functional materials and catalysts. The protein embedded in intracellular bacterial deposits might display different conformations, but they are usually enriched in beta-sheet-rich assemblies resembling the amyloid fibrils characteristic of several human neurodegenerative diseases. This makes bacterial cells simple, but biologically relevant model systems to address the mechanisms behind amyloid formation and the cellular impact of protein aggregates. Interestingly, bacteria also exploit the structural principles behind amyloid formation for functional purposes such as adhesion or cytotoxicity. In the present research topic we collect papers addressing all the issues mentioned above from both the experimental and computational point of view.


Book
Topology and Geometric Group Theory : Ohio State University, Columbus, USA, 2010–2011
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ISBN: 3319436732 3319436740 Year: 2016 Publisher: Cham : Springer International Publishing : Imprint: Springer,

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This book presents articles at the interface of two active areas of research: classical topology and the relatively new field of geometric group theory. It includes two long survey articles, one on proofs of the Farrell–Jones conjectures, and the other on ends of spaces and groups. In 2010–2011, Ohio State University (OSU) hosted a special year in topology and geometric group theory. Over the course of the year, there were seminars, workshops, short weekend conferences, and a major conference out of which this book resulted. Four other research articles complement these surveys, making this book ideal for graduate students and established mathematicians interested in entering this area of research.


Book
Geometry and Topology of Manifolds : 10th China-Japan Conference 2014
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ISBN: 443156019X 4431560211 Year: 2016 Publisher: Tokyo : Springer Japan : Imprint: Springer,

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Since the year 2000, we have witnessed several outstanding results in geometry that have solved long-standing problems such as the Poincaré conjecture, the Yau–Tian–Donaldson conjecture, and the Willmore conjecture. There are still many important and challenging unsolved problems including, among others, the Strominger–Yau–Zaslow conjecture on mirror symmetry, the relative Yau–Tian–Donaldson conjecture in Kähler geometry, the Hopf conjecture, and the Yau conjecture on the first eigenvalue of an embedded minimal hypersurface of the sphere. For the younger generation to approach such problems and obtain the required techniques, it is of the utmost importance to provide them with up-to-date information from leading specialists. The geometry conference for the friendship of China and Japan has achieved this purpose during the past 10 years. Their talks deal with problems at the highest level, often accompanied with solutions and ideas, which extend across various fields in Riemannian geometry, symplectic and contact geometry, and complex geometry.


Book
Basic Algebraic Topology and its Applications
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ISBN: 8132228413 813222843X Year: 2016 Publisher: New Delhi : Springer India : Imprint: Springer,

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This book provides an accessible introduction to algebraic topology, a field at the intersection of topology, geometry and algebra, together with its applications. Moreover, it covers several related topics that are in fact important in the overall scheme of algebraic topology. Comprising eighteen chapters and two appendices, the book integrates various concepts of algebraic topology, supported by examples, exercises, applications and historical notes. Primarily intended as a textbook, the book offers a valuable resource for undergraduate, postgraduate and advanced mathematics students alike. Focusing more on the geometric than on algebraic aspects of the subject, as well as its natural development, the book conveys the basic language of modern algebraic topology by exploring homotopy, homology and cohomology theories, and examines a variety of spaces: spheres, projective spaces, classical groups and their quotient spaces, function spaces, polyhedra, topological groups, Lie groups and cell complexes, etc. The book studies a variety of maps, which are continuous functions between spaces. It also reveals the importance of algebraic topology in contemporary mathematics, theoretical physics, computer science, chemistry, economics, and the biological and medical sciences, and encourages students to engage in further study.


Book
Geometry and Quantization of Moduli Spaces
Authors: --- --- --- --- --- et al.
ISBN: 3319335782 3319335774 Year: 2016 Publisher: Cham : Springer International Publishing : Imprint: Birkhäuser,

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This volume is based on four advanced courses held at the Centre de Recerca Matemàtica (CRM), Barcelona. It presents both background information and recent developments on selected topics that are experiencing extraordinary growth within the broad research area of geometry and quantization of moduli spaces. The lectures focus on the geometry of moduli spaces which are mostly associated to compact Riemann surfaces, and are presented from both classical and quantum perspectives.


Book
Topologie algébrique : Chapitres 1 à 4
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ISBN: 3662493608 3662493616 Year: 2016 Publisher: Berlin, Heidelberg : Springer Berlin Heidelberg : Imprint: Springer,

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Ce livre des Éléments de mathématique est consacré à la Topologie algébrique. Les quatre premiers chapitres présentent la théorie des revêtements d'un espace topologique et du groupe de Poincaré. On construit le revêtement universel d'un espace connexe pointé délaçable et on établit l'équivalence de catégories entre revêtements de cet espace et actions du groupe de Poincaré. On démontre une version générale du théorème de van Kampen exprimant le groupoïde de Poincaré d'un espace topologique comme un coégalisateur de diagrammes de groupoïdes. Dans de nombreuses situations géométriques, on en déduit une présentation explicite du groupe de Poincaré. .

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