Relevant bibliographies by topics / ATP – Structure

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'ATP – Structure'

Author: Grafiati
Published: 4 June 2021
Last updated: 10 February 2022

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Journal articles on the topic "ATP – Structure"

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Yan, Yan, X. Zhou, H. Xu, and Karsten Melcher. "Structure and Physiological Regulation of AMPK." International Journal of Molecular Sciences 19, no. 11 (2018): 3534. http://dx.doi.org/10.3390/ijms19113534.

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Adenosine monophosphate (AMP)-activated protein kinase (AMPK) is a heterotrimeric αβγ complex that functions as a central regulator of energy homeostasis. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK’s kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs. AMPK senses the cellular energy state by competitive binding of the three adenine nucleotides AMP, ADP, and ATP to three sites in its γ subunit, each, which in turn modulates the activity of AMPK’s kinase domain in its α subunit. Our current understanding of adenine nucleotide binding and the mechanisms by which differential adenine nucleotide occupancies activate or inhibit AMPK activity has been largely informed by crystal structures of AMPK in different activity states. Here we provide an overview of AMPK structures, and how these structures, in combination with biochemical, biophysical, and mutational analyses provide insights into the mechanisms of adenine nucleotide binding and AMPK activity modulation.
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Klingenberg, Martin. "Structure-function of the ADP/ATP carrier." Biochemical Society Transactions 20, no. 3 (1992): 547–50. http://dx.doi.org/10.1042/bst0200547.

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Haines, Thomas H. "Cardiolipin's Structure, ATP Synthesis & Barth'S Syndrome." Biophysical Journal 96, no. 3 (2009): 242a. http://dx.doi.org/10.1016/j.bpj.2008.12.1193.

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Klingenberg, Martin, and David R. Nelson. "Structure-function relationships of the ADP/ATP carrier." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1187, no. 2 (1994): 241–44. http://dx.doi.org/10.1016/0005-2728(94)90119-8.

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Neupane, Prashant, Sudina Bhuju, Nita Thapa, and Hitesh Kumar Bhattarai. "ATP Synthase: Structure, Function and Inhibition." Biomolecular Concepts 10, no. 1 (2019): 1–10. http://dx.doi.org/10.1515/bmc-2019-0001.

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AbstractOxidative phosphorylation is carried out by five complexes, which are the sites for electron transport and ATP synthesis. Among those, Complex V (also known as the F1F0 ATP Synthase or ATPase) is responsible for the generation of ATP through phosphorylation of ADP by using electrochemical energy generated by proton gradient across the inner membrane of mitochondria. A multi subunit structure that works like a pump functions along the proton gradient across the membranes which not only results in ATP synthesis and breakdown, but also facilitates electron transport. Since ATP is the major energy currency in all living cells, its synthesis and function have widely been studied over the last few decades uncovering several aspects of ATP synthase. This review intends to summarize the structure, function and inhibition of the ATP synthase.
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THOMAS, P., M. BIANCHET, D. GARBOCZI, J. HULLIHEN, L. AMZEL, and P. PEDERSEN. "ATP synthase: structure-function relationships." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1101, no. 2 (1992): 228–31. http://dx.doi.org/10.1016/s0005-2728(05)80027-1.

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WU, Xueji, Mihiro YANO, Hiroyo WASHIDA, and Hiroshi KIDO. "The second metal-binding site of 70 kDa heat-shock protein is essential for ADP binding, ATP hydrolysis and ATP synthesis." Biochemical Journal 378, no. 3 (2004): 793–99. http://dx.doi.org/10.1042/bj20031680.

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The chaperone activity of Hsp70 (70 kDa heat-shock protein) in protein folding and its conformational switch, including oligomeric and monomeric interconversion, are regulated by the hydrolysis of ATP and the ATP–ADP exchange cycle. The crystal structure of human ATPase domain shows two metal-binding sites, the first for ATP binding and a second, in close proximity to the first, whose function remains unknown [Sriram, Osipiuk, Freeman, Morimoto and Joachimiak (1997) Structure 5, 403–414]. In this study, we have characterized the second metal-binding motif by site-directed mutagenesis and the kinetics of ATP and ADP binding, and found that the second metal-binding site, comprising a loop co-ordinated by His-227, Glu-231 and Asp-232, participates both in ATP hydrolysis and ATP-synthetic activities, in co-operation with the first metal-binding site. The first metal-binding site, a catalytic centre, is essential for ATP binding and the second site for ADP binding in the reactions of ATP hydrolysis and ATP synthesis.
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Petri, Jessica, Yoshio Nakatani, Martin G. Montgomery, et al. "Structure of F1-ATPase from the obligate anaerobeFusobacterium nucleatum." Open Biology 9, no. 6 (2019): 190066. http://dx.doi.org/10.1098/rsob.190066.

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The crystal structure of the F1-catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacteriumFusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially inhibited. The structure is similar to those of the F1-ATPases fromCaldalkalibacillus thermarum, which is more strongly inhibited in ATP hydrolysis, and inMycobacterium smegmatis, which has a very low ATP hydrolytic activity. The βE-subunits in all three enzymes are in the conventional ‘open’ state, and in the case ofC. thermarumandM. smegmatis, they are occupied by an ADP and phosphate (or sulfate), but inF. nucleatum, the occupancy by ADP appears to be partial. It is likely that the hydrolytic activity of theF. nucleatumenzyme is regulated by the concentration of ADP, as in mitochondria.
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Ko, Tzu-Ping, Yu-Chuan Wang, Chia-Ling Tsai, Chia-Shin Yang, Mei-Hui Hou, and Yeh Chen. "Crystal structure and functional implication of a bacterial cyclic AMP–AMP–GMP synthetase." Nucleic Acids Research 49, no. 8 (2021): 4725–37. http://dx.doi.org/10.1093/nar/gkab165.

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Abstract Mammalian cyclic GMP-AMP synthase (cGAS) and its homologue dinucleotide cyclase in Vibrio cholerae (VcDncV) produce cyclic dinucleotides (CDNs) that participate in the defense against viral infection. Recently, scores of new cGAS/DncV-like nucleotidyltransferases (CD-NTases) were discovered, which produce various CDNs and cyclic trinucleotides (CTNs) as second messengers. Here, we present the crystal structures of EcCdnD, a CD-NTase from Enterobacter cloacae that produces cyclic AMP-AMP-GMP, in its apo-form and in complex with ATP, ADP and AMPcPP, an ATP analogue. Despite the similar overall architecture, the protein shows significant structural variations from other CD-NTases. Adjacent to the donor substrate, another nucleotide is bound to the acceptor binding site by a non-productive mode. Isothermal titration calorimetry results also suggest the presence of two ATP binding sites. GTP alone does not bind to EcCdnD, which however binds to pppApG, a possible intermediate. The enzyme is active on ATP or a mixture of ATP and GTP, and the best metal cofactor is Mg2+. The conserved residues Asp69 and Asp71 are essential for catalysis, as indicated by the loss of activity in the mutants. Based on structural analysis and comparison with VcDncV and RNA polymerase, a tentative catalytic pathway for the CTN-producing EcCdnD is proposed.
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Clémençon, Benjamin, Martial Rey, Véronique Trézéguet, Eric Forest, and Ludovic Pelosi. "Yeast ADP/ATP Carrier Isoform 2." Journal of Biological Chemistry 286, no. 41 (2011): 36119–31. http://dx.doi.org/10.1074/jbc.m111.277376.

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The mitochondrial ADP/ATP carrier, or Ancp, is a member of the mitochondrial carrier family responsible for exchanging ADP and ATP across the mitochondrial inner membrane. ADP/ATP transport involves Ancp switching between two conformational states. These can be analyzed using specific inhibitors, carboxyatractyloside (CATR) and bongkrekic acid (BA). The high resolution three-dimensional structure of bovine Anc1p (bAnc1p), as a CATR-carrier complex, has been solved. However, because the structure of the BA-carrier complex has not yet been determined, the detailed mechanism of transport remains unknown. Recently, sample processing for hydrogen/deuterium exchange experiments coupled to mass spectrometry was improved, providing novel insights into bAnc1p conformational transitions due to inhibitor binding. In this work we performed both hydrogen/deuterium exchange-mass spectrometry experiments and genetic manipulations. Because these are very difficult to apply with bovine Anc1p, we used Saccharomyces cerevisiae Anc isoform 2 (ScAnc2p). Significant differences in solvent accessibility were observed throughout the amino acid sequence for ScAnc2p complexed to either CATR or BA. Interestingly, in detergent solution, the conformational dynamics of ScAnc2p were dissimilar to those of bAnc1p, in particular for the upper half of the cavity, toward the intermembrane space, and the m2 loop, which is thought to be easily accessible to the solvent from the matrix in bAnc1p. Our study then focused on the methionyl residues of the Ancp signature sequence, RRRMMM. All our results indicate that the methionine cluster is involved in the ADP/ATP transport mechanism and confirm that the Ancp cavity is a highly dynamic structure.
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Dissertations / Theses on the topic "ATP – Structure"

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Woźnicka-Misăilă, Aleksandra. "An investigation and characterization of different ADP/ATP Carrier homologs." Thesis, Université Grenoble Alpes (ComUE), 2016. http://www.theses.fr/2016GREAV011/document.

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L'objectif principal de ce projet de thèse était d'obtenir de nouvelles données structurales sur les transporteurs ADP/ATP mitochondriaux et de développer des outils pour les approches de micro- et nano-cristallographie appliquées à la biologie structurale des protéines membranaires.Le rôle principal du transporteur ADP/ATP (AAC) est d'importer et d'exporter respectivement de l’ADP3- et l’ATP4- à travers la membrane mitochondriale interne, entre l'espace intermembranaire et la matrice. AAC est le transporteur mitochondrial le mieux caractérisé de toute cette famille de protéines. De nombreuses études ont été menées pour caractériser sa fonction et sa structure. Toutefois, les données structurales n’étant disponibles que pour une conformation de la protéine, de nombreuses questions fondamentales notamment sur les différents états conformationnels adoptés par la protéine au cours du processus de transport restent encore posées. Dans cette thèse, nous avons étudié les 4 isoformes humaines d’AAC. Elles sont impliquées dans diverses maladies génétiques, mais jouent également un rôle dans la cancérogenèse. Cette thèse décrit ainsi en détail la caractérisation structurale et fonctionnelle de ces protéines et leur comparaison. C’est est une étape essentielle pour définir leurs propriétés, et constitue un point de départ précieux dans le développement de nouvelles thérapies.Le domaine de la biologie structurale ne cesse de connaître de nouveaux développements, comme c’est le cas par exemple avec l’avènement de la cristallographie sérielle. Il y a donc un besoin constant de nouvelles approches notamment pour la préparation des échantillons, leur montage sur les lignes de lumière et les collectes de données afin de continuer à améliorer la qualité des données collectées au synchrotron. Ainsi, notre objectif était d'utiliser différents échantillons de protéines membranaires pour développer de nouvelles techniques de cristallisation et de montage d’échantillons sur les lignes de lumière afin de préserver au mieux la qualité des échantillons tout en permettant des collectes de données plus rapides, plus efficaces et plus simples<br>The main objective of this PhD project was to gain new structural data on the mitochondrial ADP/ATP carriers and develop tools for micro- and nano-crystallography approaches applied to membrane protein structural biology.The main role of the ADP/ATP carrier (AAC) is to import and export ADP3- and ATP4- respectively between the intermembrane space and the matrix through the inner mitochondrial membrane. AAC is the best characterized among all mitochondrial carriers. Much has been done to investigate its function and structure. However, since structural data are only available for one conformation of the protein some fundamental questions about the different conformational states adopted during the transport process still need to be answered.In this thesis we considered 4 human AAC homologs as a main target. They are involved in different genetic diseases but play also a role in cancerogenesis. This thesis describes and compares in detail the functional and structural characterization of the human AAC isoforms. It was an essential step to give insight into their native properties and is a precious starting point for the drug development field.Since the structural biology field is rapidly developing especially in serial crystallography techniques, there are more and more new applications for samples preparation, mounting and measurements in order to improve the quality of the data collected at the synchrotrons. Hence, our second objective was to use different membrane protein samples to develop new crystal-friendly crystallization set up combined with different sample environment on the beamline toward faster, more efficient and simpler data collection
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Dahout-Gonzalez, Cécile. "Transporteur mitochondrial ADP/ATP : structure tridimensionnelle à 2,2 Å de résolution et dynamique fonctionnelle." Université Joseph Fourier (Grenoble), 2003. http://www.theses.fr/2003GRE10192.

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Ward, Douglas. "Subunit structure and dual ATP effects of Na, K-ATPase." Thesis, University of Leicester, 1997. http://hdl.handle.net/2381/29915.

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The Na,K-ATPase activity of membrane-bound sodium pump exhibits non-Michaelis kinetics with respect to ATP. The enzyme consists of promoters (one plus one -subunit) that may be organised into higher oligomers. Each -subunit is believed (although it has not been proven) to posses only one ATP binding site. It is not understood how the low-affinity ATP effect arises. Experiments thus far have not been able to convincingly distinguish between the following possibilities: 1) negative co-operatively between the ATP binding sites of the two halves of a dimeric enzyme, 2) the single ATP binding site of a protomeric enzyme exhibiting variable affinity and function around the reaction cycle, and 3) a second, uncharacterised, ATP binding site on the -subunit. The experiments presented in this thesis investigate how the dual ATP effects are related to the subunit structure of the sodium pump. I solubilise Na,K-ATPase with dodecyl octaethyleneglycol monoether (C12E8). The aggregation state of the C12E8- solubilised enzyme is quantified by analytical ultracentrifugation and found to be predominantly protomeric. These soluble protomers retain dual responses towards ATP as determined from the substrate dependence curve of their Na,K-ATPase activity and their response to non-hydrolysable ATP analogs. Hence, the dual ATP responses are intrinsic to the protomer and do not arise from - interactions within an oligomeric enzyme. Furthermore, protomers that have their high-affinity ATP binding sites irreversibly blocked with fluorescein 5'-isothiocyanate can still bind 2'(3')-O-(2,4,6-trinitrophenyl)ADP indicating that each protomer possesses two nucleotide binding sites.
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Panwar, Pankaj. "Relations structure-fonction des transporteurs nucléotides." Phd thesis, Université de Grenoble, 2012. http://tel.archives-ouvertes.fr/tel-00684264.

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Le transporteur NTT1 est responsable pour l'import d'ATP dans les chloroplastes afin de maintenir le métabolisme en période d'activité réduite ou nulle de la photosynthèse. Cependant, le mécanisme moléculaire de ce transporteur est encore méconnu, essentiellement du à la difficulté de manipulation des protéines membranaires. Nous avons réussi à développer un protocole pour la production de ce transporteur, permettant une bon rendement de solubilisation et obtention de protéines purifiées pour des études structurales. Combinant des caractérisations biochimiques et biophysiques, nous avons pu identifier des conditions de préparation d'échantillons qui ont mené aux premiers cristaux. Afin d'étendre notre connaissance sur les transporteurs de nucléotides, nous avons également entrepris des études structurales et fonctionnelles sur AAC, le transporteur ADP/ATP des mitochondries. AAC et NTT1 appartiennent à des familles de protéines différentes mais ont des fonctions voisines. À partir de la première structure d'AAC déjà connue, nous avons recherché par des criblages in silico de nouvelles molécules se liant au transporteur de façon compétitive avec le nucléotide et pouvant ainsi inhiber le transport. Les outils de docking ont été mis en place et ont permis à partir d'une librairie de 75000 composés d'identifier 17 molécules. Ensuite, nous avons testés ces molécules expérimentalement et montré qu'une d'entre elles inhibent le transport. De plus, trois nouveaux analogues d'ADP ont également été identifiés comme inhibiteurs.
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Mittelstädt, Gerd Horst. "Allosteric regulation of the adenosine triphosphate phosphoribosyltransferase from campylobacter jejuni." Thesis, University of Canterbury. Chemistry, 2015. http://hdl.handle.net/10092/10799.

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The enzyme adenosine triphosphate phosphoribosyltransferase (ATP-PRT) catalyses the first reaction of the histidine biosynthetic pathway. ATP-PRT also represents a metabolic control point, directing the flux of metabolites through this energetically expensive pathway. Two distinctly different forms of ATP-PRT exist, the long form and the short form, which differ in the presence of a C-terminal regulatory domain. In the short form, where this domain is absent, it is functionally replaced by a regulatory protein, called HisZ. ATP-PRT activity is modulated by two layers of regulation: active site inhibition by adenosine monophosphate, which reflects cellular energy levels, and pathway end product feedback inhibition by histidine. In the long form ATP-PRT histidine binds to the allosteric site at the regulatory domain, but the exact nature of the inhibitory mechanism is still debated. This thesis characterises a new member of the ATP-PRT long form from Campylobacter jejuni (CjeATP-PRT) and investigates the molecular mechanisms involved in the feed back inhibition by histidine. Chapter 2 describes the characterisation of the CjeATP-PRT including a detailed description of its crystal structure. The C. jejuni enzyme is similar to the previously described enzymes of the ATP-PRT long form, but exists only as hexameric species under experimental conditions, which contradicts previous assumptions that the hexamer is exclusively inactive. Chapter 3 investigates the catalytic apparatus of CjeATP-PRT by separating the catalytic and regulatory domains of the enzyme for individual study. The isolated catalytic portion of the enzyme, the CjeATP-PRT Core mutant, forms a dimeric species with very limited catalytic capabilities but high substrate and product affnities. The CjeATP-PRT Core characteristics suggest that it exists in a permanently inhibited conformation, highlighting the requirement of the regulatory domain not only for feedback regulation but also for enzyme function. Additionally this supports the evolutionary need for the recruitment of a regulatory apparatus. In chapter 4 a potential intramolecular communication pathway from the allosteric to the active site is probed by the generation of several single site mutations. One of these, CjeATP-PRT R216A, is completely insensitive to histidine inhibition, although this ligand is still able to bind at the allosteric site, which is consistent with the involvement of R216 in the allosteric signal communication. The catalytic abilities of CjeATP-PRT R216A are largely impaired, leading to the assumption that this mutation causes a permanent inhibitory response. In summary this thesis supports the existence of a simple physical regulatorymechanism for the feedback inhibition of the ATP-PRT long form, the change between two different hexamer conformations depending on the presence of the allosteric effector.
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Fronzes, Rémi. "Etude structurale et fonctionnelle de la sous-unité h de la F1F0ATP synthase de la levure Saccharomyces cerevisiae." Bordeaux 2, 2004. http://www.theses.fr/2004BOR21126.

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La F1 F0 ATP synthase est un complexe enzymatique situé au niveau de la membrane interne mitochondriale. La sous-unité h est une sous-unité de l'ATP synthase découverte en 1996 et localisée au niveau de la tige périphérique de l'enzyme. Le principal objectif des travaux présentés dans ce mémoire a été de déterminer la place de la sous-unité h dans la F1 F0 ATP synthase et de comprendre pourquoi cette sous-unité est essentielle à l'assemblage et/ou au fonctionnement de cet enzyme. Ainsi au cours de cette étude, il a été démontré que la sous-unité h est un composant majeur de la tige périphérique. De plus, une nouvelle fonction de la sous-unité h a été mise au jour. En effet, nous avons découvert que cette sous-unité est capable de se dimériser et semble fortement impliquée dans le processus de dimérisation de l'ATP synthase. Enfin, nous avons étudié les conséquences structurales et fonctionnelles de l'absence de la sous-unité h dans les cellules<br>The F1 F0 ATP synthase is an enzymatic protein complex localised in the inner membrane of mitochondria. Subunit h has been discovered in 1996 and has been localised in the peripheral stalk of the enzyme. The aim of this project was to determine the functional and structural role of the subunit h in the F1 F0 ATP synthase and to understand why this subunit is necessary to the ATP sunthase assembly and activity. First we studied the topological environment of subunit h in the complex to define its position. We showed subunit h was an essential component of the peripheral stalk. We also discovered a new function for subunit h. It was able to dimerise and seemed to be highly implicated in the ATP synthase oligomerisation/dimerisation process. We studied the structural and functional consequences of subunit h depletion in the cell
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Dayl, Sudad Amer. "Molecular modelling of ATP-gated P2X receptor ion channels." Thesis, University of Leicester, 2018. http://hdl.handle.net/2381/42761.

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P2X receptors (P2XRs) are trimeric cation channels activated by extracellular ATP. Human P2XRs (P2X1-7) are expressed in nearly all mammalian tissues, and they are an important drug target because of their involvement in inflammation and neuropathic pain. The aim of this thesis is to address the following questions. P2XR crystal structures have revealed an unusual U-shape conformation for bound ATP; how does the U-shape conformation of ATP and its derivatives affect channel activation? Where and how do the selective, non-competitive inhibitors AZ10606120 and A438079 bind to P2X7R? What is the structure of the hP2X1R intracellular domain in the closed state? Molecular modelling and bioinformatics were used to answer these questions, hypotheses resulting from this work were tested in collaboration with Prof. Evans. Investigating the binding modes of ATP and its deoxy forms in hP2X1R showed that the ribose 2′-hydroxyl group is stabilising the U-shape conformation by a hydrogen bond to the γ-phosphate. The reduced ability of 2′-deoxy ATP to adopt the U-shape conformation could explain its weak agonist action in contrast to full agonists ATP and 3′-deoxy ATP. Ligand docking of AZ10606120 and A438079 into the hP2X7R predicted an allosteric binding site, this site has meanwhile been confirmed by P2X7R/antagonist X-ray structures. MD simulations suggested that unique P2X7R regions (residues 73-79 and T90/T94) contribute to an increase of the allosteric pocket volume compared to the hP2X1R. This difference in size might be the key for selectivity. The hP2X1R intracellular domain in the closed state was modelled ab initio, and interpreted in context of chemical cross-links (collaboration with Prof. Evans). This suggests a symmetrical arrangement of two short b-antiparallel strands within the Nterminal region and short a-helix in the C-terminal region and additional asymmetrical states.
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Turton, Janet Susan. "An investigation of chloroplast ATPase structure and function using anti-peptide antibodies." Thesis, Keele University, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.260303.

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Noël, Florence. "Etude des relations structure-fonction du transporteur ADP/ATP mitochondrial de Saccharomyces cerevisiae : approche par photomarquage et protéolyse limitée." Université Joseph Fourier (Grenoble), 2000. http://www.theses.fr/2000GRE10175.

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Le transporteur adp/atp est une proteine de la membrane interne mitochondriale qui assure l'export, vers le cytoplasme, de l'atp neosynthetise dans la matrice, en echange d'adp. Ce systeme de transport peut etre inhibe de maniere tres specifique par l'atractyloside (atr) et le carboxyatractyloside (catr) d'une part, et l'acide bongkrekique (ba) d'autre part. Les travaux presentes dans ce memoire se rapportent a l'etude topographique du transporteur adp/atp de saccharomyces cerevisi. Nous avons travaille avec une souche de levure n'exprimant que l'isoforme anc2, modifiee par une extension polyhistidine en son extremite c-terminale, et appelee anc2-ht. La premiere partie de ce travail a consiste a determiner les sites de fixation de derives de substrat ou d'inhibiteur sur le transporteur adp/atp par photomarquage. Differentes sondes, photoactivables et radioactives, ont ete synthetisees. Elles ont permis d'explorer le transporteur insere dans la membrane mitochondriale. La fixation covalente d'un derive de substrat, l'an-adp (2-azido-3-o-naphtoyl 3 2padp), a ete localisee dans deux regions du transporteur, situees entre les residus s182-r190 et i310-k317. Un derive d'atr, i 1 2 5iasa (3- 1 2 5i-4-p-azidosalicylamidobutylamino-succinyl atractyloside), a permis de mettre en evidence au moins un site de fixation, sur le segment s212-e223 du transporteur anc2-ht. La deuxieme approche utilisee, la proteolyse limitee, a permis d'etudier les differences de conformation adoptees par le transporteur adp/atp au sein des complexes anc2-ht-catr et anc2-ht-ba, dans la membrane mitochondriale. L'accessibilite aux proteases de differentes regions du transporteur, sur les deux faces de la membrane, a revele certains elements de l'arrangement membranaire du transporteur anc2-ht dans chacune des conformations. A partir de l'ensemble de ces donnees, il est propose un modele d'arrangement du transporteur adp/atp dans la membrane mitochondriale, faisant apparaitre les regions flexibles, probablement impliquees dans le mecanisme du transport des adenine nucleotides lui-meme.
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Nicolaou, Michael. "Structure and function analysis of the mammalian ATP-binding cassette transporters, ABCB1 and ABCB4." Thesis, Queen Mary, University of London, 2012. http://qmro.qmul.ac.uk/xmlui/handle/123456789/8560.

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Mammalian ABC (ATP-binding cassette) transporters are integral membrane proteins that translocate allocrites across biological membranes using ATP as a substrate. ABCB1 is a polyspecific efflux pump which can confer multidrug resistance in cancer. ABCB1 is also expressed in a variety of normal tissues where it functions to prevent the accumulation of toxic allocrites. Direct inhibition of ABCB1 can therefore have detrimental effects on patients. Identification of ABCB1-interacting partners that influence trafficking or function would therefore provide alternative targets for therapy which may be cell- or tissue-type specific. The “split-ubiquitin” yeast two-hybrid system, that can detect protein:protein interactions at the plasma membrane, was used to screen for ABCB1-interactors in a human liver library. All candidates isolated from the screen interacted with ABCB1 in a non-specific manner when subjected to strict testing. ABCB4, a close relative of ABCB1, is expressed primarily at the hepatocyte canalicular membrane where it flops phosphatidylcholine (PC) into the outer leaflet for extraction by bile salts. Many ABCB4 non-synonymous mutations have been linked to cholestatic liver diseases in humans, but data confirming an impact on ABCB4 function is lacking. Transient expression of wild-type (WT) ABCB4 in tissue culture has proved difficult because the protein is toxic to HEK293T cells. However, co-expression of the phosphatidylserine flippase ATP8B1 (FIC1) and its accessory protein CDC50A allowed the cells to tolerate ABCB4. To investigate the impact of SNPs on ABCB4 function, equivalent changes were introduced into the ABCB4 cDNA for transient expression in the presence or absence of ATP8B1/CDC50A. ABCB4 expression and targeting to the plasma membrane were monitored by western analysis and confocal microscopy, respectively, and, by “feeding” the transfected cells [methyl-3H]choline, PC efflux to added bile salt acceptor was measured. By thus mimicking the situation at the canalicular membrane I report the preliminary characterisation of nine variants of ABCB4 that have been linked to cholestatic liver disease.
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Books on the topic "ATP – Structure"

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International, Seminar/Workshop on the Molecular Structure Function and Assembly of ATP Synthases (1987 Honolulu Hawaii). Molecular structure, function, and assembly of the ATP synthases. Plenum Press, 1989.

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Marzuki, Sangkot, ed. Molecular Structure, Function, and Assembly of the ATP Synthases. Springer US, 1990. http://dx.doi.org/10.1007/978-1-4613-0593-4.

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Alessi, Dario R. Synthesis of a conformationally restricted spin-labelled analogue of ATP for the study of the motion and structure of the myosin crossbridges. University of Birmingham, 1991.

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Maurer, Boris. R & D, Innovation and Industrial Structure. Physica-Verlag HD, 1996. http://dx.doi.org/10.1007/978-3-642-95925-7.

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Kerschen, Gaetan, Matthew R. W. Brake, and Ludovic Renson, eds. Nonlinear Structures & Systems, Volume 1. Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-47626-7.

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Commission of the European Communities. Directorate-General for Development. La cooperation UE-ACP en 1995 =: EU-ACP cooperation in 1995 : quel adjustement structurel? : what form of structural adjustment?. European Commission, 1995.

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Forsyth, Michael, ed. Structures & Construction in Historic Building Conservation. Blackwell Publishing Ltd, 2007. http://dx.doi.org/10.1002/9780470691816.

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Pandey, M., Wei-Chau Xie, and Lei Xu, eds. Advances in Engineering Structures, Mechanics & Construction. Springer Netherlands, 2006. http://dx.doi.org/10.1007/1-4020-4891-2.

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Descalzi, Orazio, Javier Martínez, and Enrique Tirapegui, eds. Instabilities and Nonequilibrium Structures VII & VIII. Springer Netherlands, 2004. http://dx.doi.org/10.1007/978-1-4020-2149-7.

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Saouma, Victor E., ed. Diagnosis & Prognosis of AAR Affected Structures. Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-44014-5.

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Book chapters on the topic "ATP – Structure"

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Meier, Thomas, and Denys Pogoryelov. "ATP Synthase Structure." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_206.

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Jencks, W. P. "How Does ATP Make Work?" In Protein Structure and Protein Engineering. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-74173-9_1.

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Jacobs, Howard T. "Mitochondrial ATP Synthase: Structure, Biogenesis and Pathology." In Organellar Proton-ATPases. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-662-22265-2_5.

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Mayer, Florian, and Volker Müller. "ATP Synthases from Archaea: Structure and Function." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_204.

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Rottenberg, Hagai, Todd P. Silverstein, Ken Hashimoto, and Sonia Steiner-Mordoch. "ATP Synthesis Driven by Intramembranal Protons." In Molecular Structure, Function, and Assembly of the ATP Synthases. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4613-0593-4_20.

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Kagawa, Yasuo, and Shigeo Ohta. "Gene Structure of Human ATP Synthase Beta Subunit." In Bioenergetics. Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5835-0_31.

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Malyan, Alexander N. "The Structure and Regulation of Chloroplast ATP Synthase." In Photosynthesis. John Wiley & Sons, Inc., 2015. http://dx.doi.org/10.1002/9781119084150.ch4.

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Kagawa, Yasuo, Shigeo Ohta, Masafumi Yohda, Hajime Hirata, Toshiro Hamamoto, and Kakuko Matsuda. "Gene Structure and Function of Thermophilic ATP Synthase." In Molecular Structure, Function, and Assembly of the ATP Synthases. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4613-0593-4_1.

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Gräber, Peter, Bettina Böttcher, and Egbert J. Boekema. "The Structure of the ATP-Synthase from Chloroplasts." In Bioelectrochemistry III. Springer US, 1990. http://dx.doi.org/10.1007/978-1-4757-9459-5_11.

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Gonoi, T., and S. Seino. "Structure and Function of ATP-Sensitive K+ Channels." In Pharmacology of Ionic Channel Function: Activators and Inhibitors. Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-642-57083-4_11.

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Conference papers on the topic "ATP – Structure"

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Kohno, Kenjiro, Yuichi Hiratsuka, and Hiroaki Onoe. "Analysis on Internal Biomolcular Network Structure of ATP-Drive Actomyosin-Collagen Hybrid Actuator." In 2021 21st International Conference on Solid-State Sensors, Actuators and Microsystems (Transducers). IEEE, 2021. http://dx.doi.org/10.1109/transducers50396.2021.9495488.

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Rahimian, M. Sadegh, and Ali M. Hussein. "ATP modelling of the lightning current within a tall structure and the attached channel." In 2012 International Conference on Lightning Protection (ICLP). IEEE, 2012. http://dx.doi.org/10.1109/iclp.2012.6344390.

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Gonzales, Silvia D., Chong Wang, Amaris A. Genemaras, and C. Y. Charles Huang. "Novel Measuring System of ATP-Induced Transmembrane Potential Change of Nucleus Pulposus Cells." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80539.

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Low back pain is a serious concern in industrialized societies that affects millions of people around the world [1]. It can be attributed to several spine disorders; intervertebral disc (IVD) degeneration being one of the most common causes [2]. IVDs are the largest avascular tissue in the body and are composed of two differentiated anatomical structures: the nucleus pulposus (NP) and the annulus fibrosus (AF). The ability to withstand compressive loads due to weight and bending is provided by the swelling of the NP structure, while the ability to resist tensile forces during bending and twisting is provided by the AF fibers [3]. The biomechanical functions of NP and AF rely on their extracellular matrix (ECM) structure and composition. Previous studies have demonstrated that static and dynamic compressive loading alters ATP production, which may have an effect on ECM synthesis [2]. In addition, dynamic loading has shown an increase in ATP release from NP cells, which may contribute to endplate calcification and therefore to IVD degeneration [2, 4]. When tissue is damaged, ATP, which is found in millimolar concentrations in all cells, leaks or is released into the extracellular milieu [5, 6]. Extracellular ATP is a powerful signaling molecule that can regulate cell metabolism, survival, and growth [7]. However, IVD cell response to ATP has not been investigated. The receptors involved in transducing responses to ATP are found in many tissues throughout the body and are responsible for different kinds of intercellular communication. ATP receptor subtypes are ligand-gated ion channels (P2X) and G-protein coupled receptors (P2Y). P2X receptors show calcium permeability while P2Y receptors mediate calcium release from intracellular stores in response to ATP [6]. Direct ATP application to the cell has been reported to cause a change in membrane conductance in a variety of tissues [8]. The voltage sensitive dye di-8-ANEPPS allows for a noninvasive method of measuring fluorescence changes of the cell membrane, which are proportional to variations of the transmembrane potential [8]. Therefore, the objectives of this study were (1) to develop a novel transmembrane potential measuring system using di-8-ANEPPS dye and (2) to investigate the response of NP cells to ATP by measuring the change in transmembrane potential.
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Kawakubo, Tatsuyuki, Okimasa Okada, and Tomoyuki Minami. "Dynamic Structure Change due to ATP Hydrolysis in the Motor Domain of Myosin: Molecular Dynamics Simulations." In NOISE AND FLUCTUATIONS: 19th International Conference on Noise and Fluctuations; ICNF 2007. AIP, 2007. http://dx.doi.org/10.1063/1.2759761.

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Baxer, Merissa, Sandra Craig, Campbell McInnes, and Michael Wyatt. "Abstract 4574: Polo box-targeted PLK1 inhibitors: structure activity relationships and activity in cells resistant to ATP-based inhibitors." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4574.

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Poulhaon, Fabien, Chady Ghnatios, Brice Bognet, Anais Barasinski, Adrien Leygue, and Francisco Chinesta. "A Numerical Approach for the Evaluation of Residual Stresses in the Automated Tape Placement Process." In ASME 2012 11th Biennial Conference on Engineering Systems Design and Analysis. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/esda2012-82544.

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Automated tape placement (ATP) is a process recently developed for the production of large parts (plates, shells) made of thermoplastic composites. In ATP a tape is placed on the previous ply and welded by a local heating and pressure to build up a laminated structure. The numerical modeling of such a process is a challenging issue since the thermal history of each ply is different, depending on its position within the structure. The evaluation of residual stresses is particularly important for determining the deformed shape of the piece at the end of the process. A numerical model based on the Proper Generalized Decomposition is proposed. The solution of the 3D thermal problem is performed first. Thermal contact resistances are in particular introduced in order to model the imperfect heat conduction at the interface of two neighboring plies. The computed temperature field is then introduced in the mechanical model considering a thermo-elastic behavior for the material. An incremental approach is therefore used on a control volume in order to compute the evolution of the stresses within the laminated structure during the process.
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Ueno, H., T. Yasunaga, C. Shingyoji, T. Yamaguchi, and K. Hirose. "Dynein Pulls Microtubules Without Rotating Its Stalk." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206430.

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Dynein is a motor protein that hydrolyses ATP and moves toward the minus end of a microtubule (MT). A dynein molecule has one to three heavy chains, each consisting of three domains: a head, a stalk and a tail. ATP is bound and hydrolysed in the head, which has a ring-like structure composed of 6 AAA+ domains. The stalk is an antiparallel coiled-coil, 10–15 nm long, and has a nucleotide-dependent MT-binding domain at the tip (1) (Fig. 1). It has been proposed that the nucleotide-dependent binding affinity of the tubulin-binding site at the tip of the stalk is modulated by the two alpha helices in the coiled-coil sliding over each other (2). However, it is not known how a dynein molecule moves along a microtubule (MT).
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Yuan, Tai-Yi, Hanan N. Fernando, Jessica Czamanski, Chong Wang, Wei Yong Gu, and Chun-Yuh Huang. "Effects of Static Compression on Energy Metabolism of Porcine Intervertebral Disc." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19600.

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Degeneration of the intervertebral disc (IVD) has been associated with low back pain, which is one of the major socio-economic problems in the United States. Since IVD is the largest avascular cartilaginous structure in the human body, poor nutrient supply has been suggested as a potential mechanism for IVD degeneration. Biosynthesis of extracellular matrix is an energy demanding process which is required to maintain tissue integrity [1]. Cells consume glucose and oxygen to produce adenosine triphosphate (ATP), the main energy form in cells. Glycolysis, the primary metabolic pathway for production of ATP in IVD cells, is strongly regulated by local oxygen concentration and pH (which is governed by lactate concentration) [2]. Therefore, energy metabolism may play an important role in the malnutrition pathway leading to IVD degeneration. The objective of this study was to investigate the effect of mechanical loading on cellular energy metabolism in whole disc and in agarose gels.
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Wurtele, Eve S., Diane C. Bassham, Julie Dickerson, et al. "Meta!Blast: A Serious Game to Explore the Complexities of Structural and Metabolic Cell Biology." In ASME 2010 World Conference on Innovative Virtual Reality. ASMEDC, 2010. http://dx.doi.org/10.1115/winvr2010-3708.

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Knowledge of cellular structure and function has increased dramatically with the advent of modern molecular and computational technologies. Helping students to understand cellular dynamics is a major challenge to educators. To address this challenge, we have developed the Kabala Engine, an open source engine based on OpenSG (http://www.opensg.org) and VRJuggler (http://www.vrjuggler.org). This engine is designed to enable biologists, and indeed any domain expert — chemists, artists, psychologists — to create virtual interactive worlds for teaching or research. As a proof-of-concept, we have used this engine to create Meta!Blast, a virtual plant cell containing a prototype chloroplast in which students can enter, activate the light reactions, including electron excitation, and create molecular oxygen and ATP.
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Hendricks, Adam G., Bogdan I. Epureanu, and Edgar Meyho¨fer. "Synchronization of Motor Proteins Coupled Through a Shared Load." In ASME 2006 International Mechanical Engineering Congress and Exposition. ASMEDC, 2006. http://dx.doi.org/10.1115/imece2006-15752.

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Kinesin-1 is a processive molecular motor that converts the energy from adenosine triphosphate (ATP) hydrolysis and thermal fluctuations into motion along microtubules. This motion can be interpreted as a result of ATP-fueled nonlinear nonsmooth oscillations of coupled motor domains which interact with a microtubule to transport a cargo. This class of nano-scale motors transport cargoes for distances of several micrometers in cells. This transport can also be achieved in vitro, opening the possibility of developing robust and extremely versatile nano-scale actuators or sensors based on the machinery used by biological systems. These devices could be used in a range of nano-scale applications such as drug delivery and lab-on-a-chip. However, to design such systems, a quantitative, in-depth understanding of molecular motors is essential. Single-molecule techniques have allowed the experimental characterization of kinesin-1 in vitro at a range of loads and ATP concentrations. Existing models of kinesin movement are stochastic in nature and are not well suited to describing transient dynamics. However, kinesin-1 is expected to undergo transient dynamics when external perturbations (e.g. interaction with other kinesin molecules) cause the load to vary in time. It is thought that in the cell, several kinesin motors work cooperatively to transport a common load. Thus, a transient description is integral to capturing kinesin behavior. This paper presents a mechanistic model that describes, deterministically, the average motion of kinesin-1. The structure of the kinesin-1 molecule is approximated with a simplified geometry, explicitly describing the coupling between its two heads. The diffusion is modeled using a novel approach based on the mean first-passage time, where the potential in which the free head diffuses is time varying and updated at each instant during the motion. The mechanistic model is able to predict existing force-velocity data over a wide range of ATP concentrations (including the interval 1μM to 10 mM). More importantly, the model provides a transient description, allowing predictions of kinesin-1 pulling time-varying loads and coordinated transport involving several kinesin-1 molecules. The deterministic approach is validated by comparing results to experiments and Monte Carlo simulations of the stochastic dynamics. Furthermore, using this model, the synchronization of several kinesin-1 molecules transporting a common load is investigated. Novel methods to characterize synchronization, tailored to the particularities of these nonsmooth systems, are presented.
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Reports on the topic "ATP – Structure"

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Ebeling, Robert, та Barry White. Load and resistance factors for earth retaining, reinforced concrete hydraulic structures based on a reliability index (β) derived from the Probability of Unsatisfactory Performance (PUP) : phase 2 study. Engineer Research and Development Center (U.S.), 2021. http://dx.doi.org/10.21079/11681/39881.

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This technical report documents the second of a two-phase research and development (R&amp;D) study in support of the development of a combined Load and Resistance Factor Design (LRFD) methodology that accommodates geotechnical as well as structural design limit states for design of the U.S. Army Corps of Engineers (USACE) reinforced concrete, hydraulic navigation structures. To this end, this R&amp;D effort extends reliability procedures that have been developed for other non-USACE structural systems to encompass USACE hydraulic structures. Many of these reinforced concrete, hydraulic structures are founded on and/or retain earth or are buttressed by an earthen feature. Consequently, the design of many of these hydraulic structures involves significant soil structure interaction. Development of the required reliability and corresponding LRFD procedures has been lagging in the geotechnical topic area as compared to those for structural limit state considerations and have therefore been the focus of this second-phase R&amp;D effort. Design of an example T-Wall hydraulic structure involves consideration of five geotechnical and structural limit states. New numerical procedures have been developed for precise multiple limit state reliability calculations and for complete LRFD analysis of this example T-Wall reinforced concrete, hydraulic structure.
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Heymsfield, Ernie, and Jeb Tingle. State of the practice in pavement structural design/analysis codes relevant to airfield pavement design. Engineer Research and Development Center (U.S.), 2021. http://dx.doi.org/10.21079/11681/40542.

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An airfield pavement structure is designed to support aircraft live loads for a specified pavement design life. Computer codes are available to assist the engineer in designing an airfield pavement structure. Pavement structural design is generally a function of five criteria: the pavement structural configuration, materials, the applied loading, ambient conditions, and how pavement failure is defined. The two typical types of pavement structures, rigid and flexible, provide load support in fundamentally different ways and develop different stress distributions at the pavement – base interface. Airfield pavement structural design is unique due to the large concentrated dynamic loads that a pavement structure endures to support aircraft movements. Aircraft live loads that accompany aircraft movements are characterized in terms of the load magnitude, load area (tire-pavement contact surface), aircraft speed, movement frequency, landing gear configuration, and wheel coverage. The typical methods used for pavement structural design can be categorized into three approaches: empirical methods, analytical (closed-form) solutions, and numerical (finite element analysis) approaches. This article examines computational approaches used for airfield pavement structural design to summarize the state-of-the-practice and to identify opportunities for future advancements. United States and non-U.S. airfield pavement structural codes are reviewed in this article considering their computational methodology and intrinsic qualities.
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Bell, Gary, and Duncan Bryant. Red River Structure physical model study : bulkhead testing. Engineer Research and Development Center (U.S.), 2021. http://dx.doi.org/10.21079/11681/40970.

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The US Army Corps of Engineers, St. Paul District, and its non-federal sponsors are designing and constructing a flood risk management project that will reduce the risk of flooding in the Fargo-Moorhead metropolitan area. There is a 30-mile long diversion channel around the west side of the city of Fargo, as well as a staging area that will be formed upstream of a 20-mile long dam (referred to as the Southern Embankment) that collectively includes an earthen embankment with three gated structures: the Diversion Inlet Structure, the Wild Rice River Structure, and the Red River Structure (RRS). A physical model has been constructed and analyzed to assess the hydraulic conditions near and at the RRS for verification of the structure’s flow capacity as well as optimization of design features for the structure. This report describes the modeling techniques and instrumentation used in the investigation and details the evaluation of the forces exerted on the proposed bulkheads during emergency operations for the RRS.
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Rees, David, and Timothy J. Fuller-Rowell. Atmospheric Structure & Variability. Defense Technical Information Center, 1990. http://dx.doi.org/10.21236/ada223439.

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Colson, Steven D., and Roy E. Gephart. Annual Report 2002. Chemical Structure & Dynamics. Office of Scientific and Technical Information (OSTI), 2003. http://dx.doi.org/10.2172/971118.

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Montgomery, Michael T. Fundamental Studies In Tropical Cyclone Structure & Intensity Change. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada627326.

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Moore, Branden J., Gwendolyn Renae Voskuilen, Arun F. Rodrigues, Simon David Hammond, and Karl Scott Hemmert. Structural Simulation Toolkit. Lunch & Learn. Office of Scientific and Technical Information (OSTI), 2015. http://dx.doi.org/10.2172/1227913.

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Sakla, S. CC Pre-Amp Platform: Structural Analysis. Office of Scientific and Technical Information (OSTI), 1994. http://dx.doi.org/10.2172/1032132.

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Weiss, Paul S. Control of Structures & Properties in Ultrathin Films. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada436657.

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S. Bricker, C. Compton, W. Hartung, et al. 805 MHz Beta = 0.47 Elliptical Accelerating Structure R & D. Office of Scientific and Technical Information (OSTI), 2008. http://dx.doi.org/10.2172/937509.

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