Relevant bibliographies by topics / ATP hydrolysis

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

Academic literature on the topic 'ATP hydrolysis'

Author: Grafiati
Published: 4 June 2021
Last updated: 12 February 2022

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Journal articles on the topic "ATP hydrolysis"

1

Willadsen, P., J. M. Nielsen, and G. A. Riding. "Purification and properties of a novel nucleotide-hydrolysing enzyme (5′-nucleotidase) from Boophilus microplus." Biochemical Journal 258, no. 1 (February 15, 1989): 79–85. http://dx.doi.org/10.1042/bj2580079.

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The tick Boophilus microplus contains a nucleoside phosphate-hydrolysing enzyme which, in many respects, resembles the well characterized 5'-nucleotidase from mammalian tissue. The tick enzyme has been purified to homogeneity. It is a membrane-bound glycoprotein with an apparent Mr of 67,000 and, although it fails to hydrolyse a range of nucleoside 2'- or 3'-monophosphates, it has broad specificity for the 5' derivatives. Further investigation of the enzyme's substrate specificity, however, shows some important differences from the mammalian nucleotidases. It hydrolyses both bis-p-nitrophenyl phosphate and p-nitrophenyl phenylphosphonate, typical substrates for phosphodiesterases. However, the tick enzyme is most strikingly different from the mammalian enzymes in that it hydrolyses not only AMP but ADP and ATP as well. Further, the products of the hydrolysis of ATP are adenosine and tripolyphosphate, a reaction which has not been reported previously. The products of ADP hydrolysis are adenosine and pyrophosphate.
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Dahlmann, B., L. Kuehn, and H. Reinauer. "Studies on the activation by ATP of the 26 S proteasome complex from rat skeletal muscle." Biochemical Journal 309, no. 1 (July 1, 1995): 195–202. http://dx.doi.org/10.1042/bj3090195.

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The 26 S proteasome complex is thought to catalyse the breakdown of ubiquitinated proteins within eukaryotic cells. In addition it has been found that the complex also degrades short-lived proteins such as ornithine decarboxylase in a ubiquitin-independent manner. Both proteolytic processes are paralleled by the hydrolysis of ATP. Here we show that ATP also affects the hydrolytic activity towards fluorigenic peptide substrates by the 26 S proteasome complex from rat skeletal muscle tissue. Low concentrations of ATP (about 25 microM) optimally activate the so-called chymotryptic and tryptic activity by increasing the rate of peptide hydrolysis but not peptidylglutamylpeptide hydrolysis. Activation of the enzyme by ATP is transient but this effect can be enhanced and prolonged by including in the assay an ATP-regenerating system, indicating that ATP is hydrolysed by the 26 S proteasome complex. Although ATP cannot be substituted for by adenosine 5′-[beta,gamma-methylene]triphosphate or AMP, hydrolysis of the phosphoanhydride bond of ATP seems not to be necessary for the activation process of the proteasome complex, a conclusion drawn from the findings that ATP analogues such as adenosine 5′-[beta,gamma-imido]triphosphate, adenosine 5′-O-[gamma-thio]triphosphate, adenosine 5′-O-[beta-thio]-diphosphate and adenosine 5′-[alpha,beta-methylene]triphosphate give the same effect as ATP, and vanadate does not prevent ATP activation. These effects are independent of the presence of Mg2+. Thus, ATP and other nucleotides may act as allosteric activators of peptide-hydrolysing activities of the 26 S proteasome complex as has also been found with the lon protease from Escherichia coli.
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ROCHA, J. B. T., C. F. Mello, J. J. F. Sarkis, and R. D. Dias. "Undernutrition during the preweaning period changes calcium ATPase and ADPase activities of synaptosomal fractions of weanling rats." British Journal of Nutrition 63, no. 2 (March 1990): 273–83. http://dx.doi.org/10.1079/bjn19900114.

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The presence of activities that hydrolyse externally added ATP to adenosine in synaptosomal preparations from various sources is well demonstrated. The hydrolysis of ATP to AMP can be mediated either by the concerted action of enzymes or by an ATP-diphosphohydrolase (EC 3.6.1.5; apyrase). Undernutrition during the preweaning period can delay the development of several enzymes involved in the metabolism of neurotransmitters or neuronal function. In young rats, the presence of an apyrase in synaptosomal preparations from cerebral cortex was investigated. The results suggested that the hydrolysis of externally added ATP and ADP can be mediated by a single enzyme. The effects of preweaning undernutrition on the hydrolysis of ATP and ADP were also investigated. In weanling rats, previous undernutrition caused a decrease of about 20% in the hydrolysis of both substrates in synaptosomal fractions.
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Petri, Jessica, Yoshio Nakatani, Martin G. Montgomery, Scott A. Ferguson, David Aragão, Andrew G. W. Leslie, Adam Heikal, John E. Walker, and Gregory M. Cook. "Structure of F1-ATPase from the obligate anaerobeFusobacterium nucleatum." Open Biology 9, no. 6 (June 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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Buchet, Rene, Camille Tribes, Valentine Rouaix, Bastien Doumèche, Michele Fiore, Yuqing Wu, David Magne, and Saida Mebarek. "Hydrolysis of Extracellular ATP by Vascular Smooth Muscle Cells Transdifferentiated into Chondrocytes Generates Pi but Not PPi." International Journal of Molecular Sciences 22, no. 6 (March 14, 2021): 2948. http://dx.doi.org/10.3390/ijms22062948.

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(1) Background: Tissue non-specific alkaline phosphatase (TNAP) is suspected to induce atherosclerosis plaque calcification. TNAP, during physiological mineralization, hydrolyzes the mineralization inhibitor inorganic pyrophosphate (PPi). Since atherosclerosis plaques are characterized by the presence of necrotic cells that probably release supraphysiological concentrations of ATP, we explored whether this extracellular adenosine triphosphate (ATP) is hydrolyzed into the mineralization inhibitor PPi or the mineralization stimulator inorganic phosphate (Pi), and whether TNAP is involved. (2) Methods: Murine aortic smooth muscle cell line (MOVAS cells) were transdifferentiated into chondrocyte-like cells in calcifying medium, containing ascorbic acid and β-glycerophosphate. ATP hydrolysis rates were determined in extracellular medium extracted from MOVAS cultures during their transdifferentiation, using 31P-NMR and IR spectroscopy. (3) Results: ATP and PPi hydrolysis by MOVAS cells increased during transdifferentiation. ATP hydrolysis was sequential, yielding adenosine diphosphate (ADP), adenosine monophosphate (AMP), and adenosine without any detectable PPi. The addition of levamisole partially inhibited ATP hydrolysis, indicating that TNAP and other types of ectonucleoside triphoshatediphosphohydrolases contributed to ATP hydrolysis. (4) Conclusions: Our findings suggest that high ATP levels released by cells in proximity to vascular smooth muscle cells (VSMCs) in atherosclerosis plaques generate Pi and not PPi, which may exacerbate plaque calcification.
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Marquenet, Emélie, and Evelyne Richet. "Conserved Motifs Involved in ATP Hydrolysis by MalT, a Signal Transduction ATPase with Numerous Domains from Escherichia coli." Journal of Bacteriology 192, no. 19 (August 6, 2010): 5181–91. http://dx.doi.org/10.1128/jb.00522-10.

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ABSTRACT The signal transduction ATPases with numerous domains (STAND) are sophisticated signaling proteins that are related to AAA+ proteins and control various biological processes, including apoptosis, gene expression, and innate immunity. They function as tightly regulated switches, with the off and on positions corresponding to an ADP-bound, monomeric form and an ATP-bound, multimeric form, respectively. Protein activation is triggered by inducer binding to the sensor domain. ATP hydrolysis by the nucleotide-binding oligomerization domain (NOD) ensures the generation of the ADP-bound form. Here, we use MalT, an Escherichia coli transcription activator, as a model system to identify STAND conserved motifs involved in ATP hydrolysis besides the catalytic acidic residue. Alanine substitution of the conserved polar residue (H131) that is located two residues downstream from the catalytic residue (D129) blocks ATP hydrolysis and traps MalT in an active, ATP-bound, multimeric form. This polar residue is also conserved in AAA+. Based on AAA+ X-ray structures, we proposed that it is responsible for the proper positioning of the catalytic and the sensor I residues for the hydrolytic attack. Alanine substitution of the putative STAND sensor I (R160) abolished MalT activity. Substitutions of R171 impaired both ATP hydrolysis and multimerization, which is consistent with an arginine finger function and provides further evidence that ATP hydrolysis is primarily catalyzed by MalT multimers.
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Sarkis, J. J. F., J. A. Guimarães, and J. M. C. Ribeiro. "Salivary apyrase of Rhodnius prolixus. Kinetics and purification." Biochemical Journal 233, no. 3 (February 1, 1986): 885–91. http://dx.doi.org/10.1042/bj2330885.

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The salivary apyrase activity of the blood-sucking bug Rhodnius prolixus was found to reside in a true apyrase (ATP diphosphohydrolase, EC 3.6.1.5) enzyme. The crude saliva was devoid of 5′-nucleotidase, inorganic pyrophosphatase, phosphatase and adenylate kinase activities. ATP hydrolysis proceeded directly to AMP and Pi without significant accumulation of ADP. Km values for ATP and ADP hydrolysis were 229 and 291 microM respectively. Ki values for ATP and ADP inhibition of ADP and ATP hydrolysis were not different from the Km values, and these experiments indicated competitive inhibition. Activities were purified 126-fold by combined gel filtration and ion-exchange chromatography procedures with a yield of 63%. The purified enzyme displayed specific activities of 580 and 335 mumol of Pi released/min per mg of protein for ATP and ADP hydrolysis respectively. The action of the purified enzyme on several phosphate esters indicates that Rhodnius apyrase is a non-specific nucleosidetriphosphate diphosphohydrolase.
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Ferguson, Scott A., Gregory M. Cook, Martin G. Montgomery, Andrew G. W. Leslie, and John E. Walker. "Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum." Proceedings of the National Academy of Sciences 113, no. 39 (September 12, 2016): 10860–65. http://dx.doi.org/10.1073/pnas.1612035113.

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The crystal structure has been determined of the F1-catalytic domain of the F-ATPase from Caldalkalibacillus thermarum, which hydrolyzes adenosine triphosphate (ATP) poorly. It is very similar to those of active mitochondrial and bacterial F1-ATPases. In the F-ATPase from Geobacillus stearothermophilus, conformational changes in the ε-subunit are influenced by intracellular ATP concentration and membrane potential. When ATP is plentiful, the ε-subunit assumes a “down” state, with an ATP molecule bound to its two C-terminal α-helices; when ATP is scarce, the α-helices are proposed to inhibit ATP hydrolysis by assuming an “up” state, where the α-helices, devoid of ATP, enter the α3β3-catalytic region. However, in the Escherichia coli enzyme, there is no evidence that such ATP binding to the ε-subunit is mechanistically important for modulating the enzyme’s hydrolytic activity. In the structure of the F1-ATPase from C. thermarum, ATP and a magnesium ion are bound to the α-helices in the down state. In a form with a mutated ε-subunit unable to bind ATP, the enzyme remains inactive and the ε-subunit is down. Therefore, neither the γ-subunit nor the regulatory ATP bound to the ε-subunit is involved in the inhibitory mechanism of this particular enzyme. The structure of the α3β3-catalytic domain is likewise closely similar to those of active F1-ATPases. However, although the βE-catalytic site is in the usual “open” conformation, it is occupied by the unique combination of an ADP molecule with no magnesium ion and a phosphate ion. These bound hydrolytic products are likely to be the basis of inhibition of ATP hydrolysis.
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Krah, Alexander, Mariel Zarco-Zavala, and Duncan G. G. McMillan. "Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data." Open Biology 8, no. 5 (May 2018): 170275. http://dx.doi.org/10.1098/rsob.170275.

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ATP synthases catalyse the formation of ATP, the most common chemical energy storage unit found in living cells. These enzymes are driven by an electrochemical ion gradient, which allows the catalytic evolution of ATP by a binding change mechanism. Most ATP synthases are capable of catalysing ATP hydrolysis to varying degrees, and to prevent wasteful ATP hydrolysis, bacteria and mitochondria have regulatory mechanisms such as ADP inhibition. Additionally, ɛ subunit inhibition has also been described in three bacterial systems, Escherichia coli , Bacillus PS3 and Caldalkalibacillus thermarum TA2.A1. Previous studies suggest that the ɛ subunit is capable of undergoing an ATP-dependent conformational change from the ATP hydrolytic inhibitory ‘extended’ conformation to the ATP-induced non-inhibitory ‘hairpin’ conformation. A recently published crystal structure of the F 1 domain of the C. thermarum TA2.A1 F 1 F o ATP synthase revealed a mutant ɛ subunit lacking the ability to bind ATP in a hairpin conformation. This is a surprising observation considering it is an organism that performs no ATP hydrolysis in vivo , and appears to challenge the current dogma on the regulatory role of the ɛ subunit. This has prompted a re-examination of present knowledge of the ɛ subunits role in different organisms. Here, we compare published biochemical, biophysical and structural data involving ɛ subunit-mediated ATP hydrolysis regulation in a variety of organisms, concluding that the ɛ subunit from the bacterial F-type ATP synthases is indeed capable of regulating ATP hydrolysis activity in a wide variety of bacteria, making it a potentially valuable drug target, but its exact role is still under debate.
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COIMBRA, E. S., S. C. GONÇALVES-DA-COSTA, S. CORTE-REAL, F. G. R. DE FREITAS, A. C. DURÃO, C. S. F. SOUZA, M. I. SILVA-SANTOS, and E. G. VASCONCELOS. "Characterization and cytochemical localization of an ATP diphosphohydrolase from Leishmania amazonensis promastigotes." Parasitology 124, no. 2 (February 2002): 137–43. http://dx.doi.org/10.1017/s0031182001001056.

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An ATP diphosphohydrolase was identified in the plasma membranes isolated from promastigote forms of Leishmania amazonensis. Both ATP and ADP were hydrolysed at similar rates by the enzyme. Other nucleotides such as UTP, GTP and CTP were also degraded, revealing a broad substrate specificity. Adding ATP and ADP simultaneously, the amount of hydrolysis achieved was compatible with the presence of a single enzyme. ATPase activity was not affected by addition of vanadate, ouabain, thapsigargin, dicyclohexylcarbodiimide, oligomycin and bafilomycin A, thus excluding involvement of P-, F- and V-type ATPases. The effects of pH in the range 6·5–8·5 were examined using ATP or p-NPP as substrate. At pH 7·4, the phosphatase activity decreased, and did not show a significant contribution to ATP hydrolysis. In addition, the enzyme was not inhibited by levamisole and ammonium molybdate, excluding alkaline phosphatase and nucleotidase activities, respectively. Sodium azide (5–10 mM) caused inhibition of the ATP and ADP hydrolysis in a dose-dependent manner. Calcium was the best activating metal ion for both ATPase and ADPase activities. Ultrastructural cytochemical microscopy showed ATP diphosphohydrolase on the surface and flagellar pocket of the parasite. We have proposed that L. amazonensis ATP diphosphohydrolase may participate in the salvage pathway of nucleosides.
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Dissertations / Theses on the topic "ATP hydrolysis"

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Chen, Min. "Mechanistic insights into ATP hydrolysis by the ABC transporter TAP." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972577971.

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Schwarzl, Sonja M. "Understanding the ATP hydrolysis mechanism in myosin using computer simulation techniques." [S.l. : s.n.], 2005. http://nbn-resolving.de/urn:nbn:de:bsz:16-opus-63890.

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Heidelberg, Univ., Diss., 2005.
Aus: S.M. Schwarzl, Understanding the ATP hydrolysis mechanism in myosin using computer simulation techniques, Mensch und Buch Verlag Berlin 2006, ISBN 3-86664-044-7.
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Shaw, Sudipta. "Role of ATP Hydrolysis and Mechanism of Substrate Reduction in Nitrogenase." DigitalCommons@USU, 2017. https://digitalcommons.usu.edu/etd/5729.

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Nitrogenase consists of two metalloproteins, the MoFe protein and the Fe protein. The MoFe protein is an α2β2 heterotetramer and the Fe protein is an α2 homodimer. The catalytic cycle of nitrogenase involves binding of the Fe protein to each αβ catalytic half of the MoFe protein, electron transfer followed by ATP hydrolysis, Pi release and eventually dissociation of the two proteins. This cycle has to be repeated eight consecutive times to reduce one molecule of N2. The two catalytic halves of the MoFe protein had been considered to be independent of each other. The research presented here showed that there is negative cooperativity associated between the two catalytic halves of the MoFe protein. The results suggested that only one half of the MoFe protein is operative during the first turnover of the enzyme. In order to understand the substrate reduction mechanism of nitrogenase, the study focused on two important enzymes of the biogeochemical nitrogen cycle: nitrite (NO2 -) and nitrate (NO3 -). Two intermediates of NO2 - reduction were trapped by a remodeled nitrogenase (α-70Ala/α-195Gln MoFe protein) and characterized by advanced spectroscopic studies. These intermediates were found to be identical to the intermediates trapped during reduction of diazene (N2H2) and hydrazine (N2H4). The pathway for reduction NO2 - to ammonia (NH3) was also proposed. NO3 - was established as a new substrate of nitrogenase. The advanced spectroscopic studies confirmed that the same two intermediates were trapped by the remodeled nitrogenase. Kinetic studies showed that two competing pathways lead to NO3 - reduction by nitrogenase, a primary 2 e- reduction pathway to form nitrite and a secondary 8 e- reduction pathway to form NH3. The pathways for reduction of NO3 - to NO2 - and NH3 were proposed.
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Balasubramanian, Krithika. "ATP hydrolysis in Rho: Identifying active site residues and their roles." Diss., Temple University Libraries, 2010. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/80319.

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Biochemistry
Ph.D.
Escherichia coli transcription termination factor Rho is a hexameric RNA/DNA helicase that terminates transcription using energy derived from the hydrolysis of ATP. The ATP binding sites of Rho are located at the interfaces of adjoining subunit Cterminal domains and have the Walker A and B motifs, characteristic of many ATPases (Skordalakes & Berger, 2003; Richardson 2002). Available Rho crystal structures capture the protein with its active site in an open configuration that must close to permit ATP hydrolysis. Because of this, the identities of active site residues predicted to mediate ATP hydrolysis are uncertain. To determine which amino acids activate water, stabilize transition state, sense the γ- phosphoryl group, and coordinate the magnesium ion of MgATP, we have carried out site-specific mutagenesis on candidate residues which are conserved across bacterial species, and characterized the relevant properties of the mutant proteins. The residues chosen were E211 as the water activator, R212 as the γ sensor, R366 as the arginine finger, and D265 as the residue that coordinates Mg2+. Each mutant protein was investigated for its ability to oligomerize as hexamers, assayed for ATPase activity, ATP and RNA binding, and pre-steady-state kinetics. The results show that the mutant proteins form hexamers similarly as to wild type Rho. The RhoE211 mutants display at least a 200-fold lower activity as ATPases, bind both ATP and RNA with similar affinities as the wild type protein, and display no burst in pre-steady-state kinetics. RhoR212A protein has 20-fold lower activity as an ATPase compared to wild type Rho, binds ATP with at least a 50-fold weaker affinity, and RNA with a 2-fold higher KD compared to wild type Rho. RhoR366A functions as an ATPase with 50-fold lower activity, binds RNA with similar affinity as wild type Rho and binds ATP with a 5- fold weaker affinity. RhoD265N displays 150-fold lower ATPase activity compared to the wild type enzyme, binds ATP with a 10-fold weaker affinity, and binds RNA with similar affinity as wild type Rho. Pre-steady-state kinetics studies indicate that the mutant proteins investigated show no burst kinetics, indicating a failure or a significantly slower rate of the hydrolysis (chemistry) step. It is possible that the rate-limiting step is the chemistry step in these mutant proteins, contrary to the wild type protein where the chemistry step is much faster (300/s). Together, the results obtained are consistent with the proposed roles for these residues: E211 is involved in activating a water molecule, R212 functions as the γ sensor, R366 functions as the arginine finger and D265 is involved in coordination of the Mg2+ ion. This study has elucidated the mechanism of ATP hydrolysis, by determining some of the key residues involved in the hydrolysis reaction. This study is only a part of the characterization of the active site residues. There might be other residues involved in one or all of the functions proposed. Utilizing the findings from this study, other experiments and models can be implemented to understand how Rho hydrolyzes ATP and utilizes the energy to move along the RNA molecule and functions as a helicase.
Temple University--Theses
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Oliveira, Ana Sofia Fernandes. "Molecular modelling of ABC transporters: from ATP hydrolysis to substrate transport." Doctoral thesis, Universidade Nova de Lisboa. Instituto de Tecnologia Química e Biológica, 2010. http://hdl.handle.net/10362/5793.

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Dissertação para a obtenção de grau de doutor em Bioquímica pelo Instituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa
Despite the great advances that have been made in the past decades in the ABC transporters field, the molecular mechanisms involved in transport across membranes remains largely an enigma. To date, questions regarding the molecular mechanism of transport, nucleotide hydrolysis and inorganic phosphate exit from the binding sites are still unanswered. In this thesis the dynamic behavior of several ABC transporters during the ATP-hydrolytic cycle is investigated using molecular modeling methods. The content of this thesis is compiled in three main scientific publications [1-3], corresponding to sections 3, 4 and 5, respectively. Although these three works are performed in prokaryotic family ABC transporters, it is likely that eukaryotic ones use similar mechanisms for nucleotide hydrolysis, inter-domain communication and allocrite translocation.(...)
Esta tese teve o apoio financeiro da FCT e do FSE no âmbito do Quadro Comunitário de Apoio, BD nº SFRH/BD/21433/2005
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Kimura, Yasuhisa. "Analysis of ATP hydrolysis activities of ABC transporters involved in multidrug resistance and K[ATP] channel regulation." Kyoto University, 2005. http://hdl.handle.net/2433/59289.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第11833号
農博第1523号
新制||農||918(附属図書館)
学位論文||H17||N4082(農学部図書室)
UT51-2005-K499
京都大学大学院農学研究科応用生命科学専攻
(主査)教授 植田 和光, 教授 植田 充美, 教授 矢﨑 一史
学位規則第4条第1項該当
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Hunter, Andrew W. "Coupling of ATP hydrolysis to microtubule depolymerization by mitotic centromere-associated kinesin /." Thesis, Connect to this title online; UW restricted, 2002. http://hdl.handle.net/1773/10549.

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Liu, Fei. "ATP Utilization by the DEAD-Box Protein DED1P." Case Western Reserve University School of Graduate Studies / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=case1259924176.

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Fung, Emma. "Dissecting the roles of ParA ATP binding and hydrolysis in P1 plasmid partition." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0023/MQ50429.pdf.

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Angove, Hayley Clare. "Energy transduction by nitrogenase involving ATP hydrolysis coupled to proton and electron transfers." Thesis, University of Sussex, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.282081.

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Books on the topic "ATP hydrolysis"

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Suzuki, Makoto, ed. The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-8459-1.

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Fung, Emma. Dissecting the roles of ParA ATP binding and hydrolysis in P1 plasmid partition. Ottawa: National Library of Canada, 2000.

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Davey, Megan Jeannette. The P1 plasmid partition protein ParA: Roles for ATP binding and hydrolysis in plasmid partition. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1997.

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Kazeykin, Valeriy, and Vladimir Tolstolugov. Theory and practice of implementation of high energy efficient technologies in construction based on Thermaron heat generators. ru: INFRA-M Academic Publishing LLC., 2020. http://dx.doi.org/10.12737/1146805.

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The monograph summarizes the legislative and regulatory framework, as well as shows the theory and practice of energy saving and energy efficiency development in Russia and in the world with the actualization of the use of a breakthrough domestic high-energy-efficient technology based on molecular heat generators Termaron. These devices use the principles of hydrolysis, cavitation, magnetism, resonance and synergy of these processes. The results of research conducted with the participation of specialists from Dubna state University, as well as the practice of using the Termaron ATP, showed that its operation provides a high efficiency in the use of electric energy, equal to 0.98, and the coefficient of conversion of electric energy to heat is from 2.3 to 4.6 (on average, 3.45). At the same time, the cost of heat energy and hot water supply is two to three times lower compared to traditional types of heat generating devices. It is intended for representatives of government authorities, University teachers, scientific and practical specialists in the field of design, construction and operation of energy-efficient residential and commercial real estate, state and municipal employees, managers and employees of development companies, students, masters, postgraduates and other specialists interested in improving their competencies in the field of energy efficiency based on domestic innovative breakthrough technologies in Russia and abroad.
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Suzuki, Makoto. The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery. Springer, 2018.

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Suzuki, Makoto. The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery. Springer, 2018.

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7

SKULACHEV, V. Chloroplast H+ ATPase: Regulation & Mechanism of Coupling of Proton Translocation with ATP Synthesis/Hydrolysis (Soviet Scientific Reviews Series, Section D). Routledge, 1994.

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Abhishek, Abhishek, and Michael Doherty. Pathophysiology of calcium pyrophosphate deposition. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199668847.003.0049.

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Calcium pyrophosphate (CPP) dihydrate crystals form extracellularly. Their formation requires sufficient extracellular inorganic pyrophosphate (ePPi), calcium, and pro-nucleating factors. As inorganic pyrophosphate (PPi) cannot cross cell membranes passively due to its large size, ePPi results either from hydrolysis of extracellular ATP by the enzyme ectonucleotide pyrophosphatase/phosphodiesterase 1 (also known as plasma cell membrane glycoprotein 1) or from the transcellular transport of PPi by ANKH. ePPi is hydrolyzed to phosphate (Pi) by tissue non-specific alkaline phosphatase. The level of extracellular PPi and Pi is tightly regulated by several interlinked feedback mechanisms and growth factors. The relative concentration of Pi and PPi determines whether CPP or hydroxyapatite crystal is formed, with low Pi/PPi ratio resulting in CPP crystal formation, while a high Pi/PPi ratio promotes basic calcium phosphate crystal formation. CPP crystals are deposited in the cartilage matrix (preferentially in the middle layer) or in areas of chondroid metaplasia. Hypertrophic chondrocytes and specific cartilage matrix changes (e.g. high levels of dermatan sulfate and S-100 protein) are related to CPP crystal deposition and growth. CPP crystals cause inflammation by engaging with the NALP3 inflammasome, and with other components of the innate immune system, and is marked with a prolonged neutrophilic inflitrate. The pathogenesis of resolution of CPP crystal-induced inflammation is not well understood.
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Allison, Willaim S. F1-ATPase: A molecular motor that hydrolyzes ATP with sequentail opening and closing of catalytic sites coupled to rotation of its y subunit. American Chemical Society, 1998.

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Book chapters on the topic "ATP hydrolysis"

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Bagshaw, Clive R. "Mechanism of ATP hydrolysis." In Muscle Contraction, 58–70. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-015-6839-5_5.

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Nederkoorn, Paul H. J., Henk Timmerman, and Gabriëlle M. Donné-Op den Kelder. "ATP Hydrolysis and Synthesis Mechanisms." In Signal Transduction by G Protein-Coupled Receptors, 27–39. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4684-1407-3_3.

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Kodama, Takao. "Energetics of Myosin ATP Hydrolysis by Calorimetry." In The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery, 103–11. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-8459-1_7.

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Lowe, D. J., G. A. Ashby, M. Brune, H. Knights, M. R. Webb, and R. N. F. Thorneley. "ATP Hydrolysis and Energy Transduction by Nitrogenase." In Nitrogen Fixation: Fundamentals and Applications, 103–8. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0379-4_14.

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Labahn, A., and P. Gräber. "Uni-Site ATP Hydrolysis Catalyzed by the ATP-Synthase from Chloroplasts." In Current Research in Photosynthesis, 1943–46. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_445.

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Mo, Jinyao, and Joseph A. Duncan. "Assessing ATP Binding and Hydrolysis by NLR Proteins." In Methods in Molecular Biology, 153–68. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-523-1_12.

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Slooten, Luit, and Saskia Vandenbranden. "ATP-Synthesis and ATP-hydrolysis in Well-Coupled Proteoliposomes Incorporating Rhodospirillum rubrum F0F1." In Current Research in Photosynthesis, 2055–58. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_471.

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Schmidt, Günter, and Peter Gräber. "The Rate of ATP Synthesis and ATP Hydrolysis Catalyzed by Reconstituted CFoF1 Liposomes." In Progress in Photosynthesis Research, 91–94. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-017-0516-5_20.

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Moreno-Sánchez, Rafael, M. Teresa Espinosa-García, and J. Carlos Raya. "Control of Respiration and ATP Hydrolysis in Uncoupled Mitochondria." In Integration of Mitochondrial Function, 297–304. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2551-0_26.

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Curtin, N. A., T. G. West, M. A. Ferenczi, Z. H. He, Y. B. Sun, M. Irving, and R. C. Woledge. "Rate of Actomyosin ATP Hydrolysis Diminishes During Isometric Contraction." In Advances in Experimental Medicine and Biology, 613–26. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9029-7_54.

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Conference papers on the topic "ATP hydrolysis"

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Sikimic, J., J. Bryan, P. Krippeit-Drews, and G. Drews. "ATP triggers Katp channel opening without hydrolysis." In Diabetes Kongress 2019 – 54. Jahrestagung der DDG. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1688110.

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Shropshire, Daniel B., Jaime Benavides, and Jean X. Jiang. "Abstract P3-01-27: Ectonucleotidase ATP hydrolysis facilitates breast cancer bone metastasis." In Abstracts: 2019 San Antonio Breast Cancer Symposium; December 10-14, 2019; San Antonio, Texas. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.sabcs19-p3-01-27.

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Giurgiutiu, Victor, Luke Matthews, Donald J. Leo, and Vishnu Baba Sundaresan. "Concepts for Power and Energy Analysis in Nastic Structures." In ASME 2005 International Mechanical Engineering Congress and Exposition. ASMEDC, 2005. http://dx.doi.org/10.1115/imece2005-82786.

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Nastic structures are potentially high-energy density smart materials that will be capable of achieving controllable deformation and shape change due to internal microactuation that functions on principles found in the biological process of nastic motion. In plants, nastic motion is accomplished through osmotic pressure changes causing a respective increase or decrease in cell volume, thereby causing net movement. In nastic structures, osmotic pressure is increased by moving fluid from low concentration to high concentration areas by means of active transport, powered by adenosine triphosphate (ATP) hydrolysis. Power analysis involves calculating possible ranges of actuation as a result of interior pressure exchanges and hydraulic flux rates which will determine the speed of actuation. Because pressure inside the actuating cylinder is uniform, the cylinder undergoes deformation in all the three dimensions. Predicting the work-energy balance involves considering the factors that determine the total volumetric change, including cylinder wall expansion, surface bulging and stretching, and outside forces that oppose the actuation. The hydraulic flux rates determine both the force magnitude and the actuation speed. Energy analysis considers the pressure variation range needed to accomplish the desired actuation deflection, and the energy required for active transport mechanisms to move the volume of fluid into the nastic actuator. Nonlinear effects are present, as the pressure inside the actuation cylinder increases, it takes more energy for active transport to continue moving fluid into it. The chemical reaction of ATP hydrolysis supplies the energy for active transport, which is related to the ratio of the reactants, to the products, as well as to the pH level. As the pH lowers, more energy is released through ATP hydrolysis. Therefore, as pH decreases, ATP Hydrolysis releases more energy, enabling active transport to move more fluid into the actuation cylinder, thereby increasing the internal osmotic pressure and causing material deformation work and actuation.
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Wang, Chong, Silvia D. Gonzales, Weiyong Gu, and C. Y. Charles Huang. "Accumulation of Extracellular ATP in Porcine Nucleus Pulposus." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80671.

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There are many reasons for people to miss work; one of the leading contributors is low back pain (LBP), which is believed to affect 80% of the population at some point during their lifetime. Suffering from back pain is the chief complaint of 5% of people who visit the doctor in the US [1]. The total medical cost related to low back pain in the US exceeds 100 billion dollars every year [2]. The cause of LBP is still unclear. However, recent studies revealed that intervertebral disc (IVD) degeneration is closely related to LBP [3]. IVD transfers loads and allows the spine to move through torsion, bending or compression [4–6]. There are two main anatomic regions in IVD: nucleus pulposus (NP) and annulus fibrosis (AF). The loss of notochordal cells in the NP region has been associated with the initiation of disc degeneration [7]. Our recent studies demonstrated that the adenosine triphosphate (ATP) production of notochordal NP cells was much higher than that of the AF cells while mechanical loading promoted ATP release from IVD cells [8]. Extracellular ATP (eATP) is a powerful signaling molecule that can mediate a wide variety of biological responses, such as cell metabolism, survival, and growth by binding to the purinergic receptors: G protein coupled receptor (P2Y) or ligand-gated ionotropic receptor (P2X) [9]. In addition, eATP is often rapidly hydrolyzed by several families of ectonucleotidases [10–12]. The by-products of eATP hydrolysis include inorganic pyrophosphate (PPi) and phosphate (Pi) which are closely related to mineral crystal formation and tissue calcification [12–15]. PPi and Pi released from eATP hydrolysis may contribute to endplate calcification which has been associated with disc degeneration. However, eATP accumulation in the IVD has not been studied yet. Therefore, the objective of this study was to investigate the accumulative level of eATP in the NP region of porcine IVD using a novel optical ATP sensor.
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Bidone, Tamara C., Marco A. Deriu, Giacomo Di Benedetto, Diana Massai, and Umberto Morbiducci. "Insights Into the Molecular Mechanisms of Actin Dynamics: A Multiscale Modeling Approach." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53417.

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Actin dynamics, which is at the basis of many fundamental cellular processes as cell migration [1], is governed by the self-assembly and disassembly of actin monomers (G-actin) that, in turn, are determined by the kinetics of ATP hydrolysis and by the local concentrations of Mg2+ and Ca2+ [2]. During cell migration, interactions of the actin filaments (F-actin) with different nucleotide-cation complexes induce local topological rearrangements, because the filament building G-actins undergo conformational shifts between multiple equilibrium states separated by low-energy barriers. For example, the structural rearrangements of the DNase-I binding loop (residues 38–52) in subdomain 2 are driven by ATP hydrolysis and the changes in the conformation of subdomain 4 are induced by the presence of a tightly-bound Mg2+ or Ca2+ ion (Figure 1a). These conformational shifts alter the cross-linking between monomers, varying the contact surfaces among adjacent inter- and intrasubdomains of G-actin, and reflect on the overall properties of F-actin.
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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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Anderson, W. H., M. Quibrera, W. K. O'Neal, M. B. Drummond, N. E. Alexis, I. Barjaktarevic, D. Couper, et al. "Accelerated ATP Hydrolysis in Airway Surface Liquid (ASL) Provides a Mechanism for Mucus Dehydration in Chronic Bronchitis." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a3847.

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Aprodu, Iuliana, Alfonso Gautieri, Franco M. Montevecchi, Alberto Redaelli, and Monica Soncini. "What Molecular Dynamics Simulations Can Tell Us About Mechanical Properties of Kinesin and Its Interaction With Tubulin." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176316.

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Kinesin is a processive molecular motor found in various cells including neurons, that transports membrane-bound vesicles and organelles along the microtubule. Kinesin typically consists of three distinct domains: two large globular heads that attach to the microtubule, a central coiled region, and a light-chain that attaches to the cellular cargo. The metabolic energy that drives kinesins is provided in the form of ATP. The energy released by ATP hydrolysis is converted into direct movement after kinesin binds strongly to the microtubule. Two mechanisms were proposed to explain the movement of kinesin along microtubules: the “hand over hand” model in which the two heads alternate in the role of leading and the “inchworm” model in which one head always leads.
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Chiang, T. M., R. J. H. Wojcikiewicz, A. H. Kang, and J. N. Fain. "PHOSPHORYLATION OF THE OUTER SURFACE OF PLATELETS ENHANCES THE EFFECTS OF COLLAGEN ON PLATELET AGGREGATION, ATP RELEASE, CALCIUM TRANSLOCATION AND PHOSPHOINOSITIDE HYDROLYSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644477.

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We have recently isolated and purified from human plasma two isomeric forms of protein kinase, both of which can phosphorylate the outer surface proteins of human platelets. One of the proteins phosphorylated is the platelet collagen receptor. The phosphorylation of the outer surface proteins of human platelets increased their functional responsiveness to collagen. Collagen-stimulated platelet aggregation, release of ATP and calcium translocation were all enhanced by pretreatment with plasma protein kinase in the presence of ATP. The mechanism by which phosphorylated platelets become hypersensitive to collagen is not established. In the present study, we have used [3H]myo-inositol-labeled human platelets to investigate the possible role of phosphoinositide metabolism in mediating this hypersensitivity. Formation of inositol mono-, bis-, and trisphosphate in response to collagen was more pronounced in phosphorylated platelets than controls. these results indicate that enhanced phosphoinositide hydrolysis in phosphorylated platelets correlate with the increased functional responses to collagen.
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Ma, Na, Ping Liu, Chao Chen, Aili Zhang, and Lisa X. Xu. "Thermal Environmental Effect on Breast Tumor Growth." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206229.

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Tissue hypoxia is a common and important feature of rapidly growing malignant tumors and their metastases. Tumor cells mainly depend on energy production thru anaerobic glycolysis rather than aerobic oxidative phosphorylation in mitochondria [1]. Intervening the tumor metabolic process via thermal energy infusion is worthy attempting. And hyperthermia, mildly elevated local temperature above the body temperature, is one of such kind. Previously, after being heated for a short period of time, tumor glucose and lactate level increased and ATP level decreased, which suggested energy metabolism was modified following hyperthermia through increased ATP hydrolysis, intensified glycolysis and impaired oxidative phosphorylation [2]. Many researchers designed experiments to determine thermal dose in hyperthermia [3], but few focused on the relationship between tumor and energy, especially for a long-term local hyperthermia treatment. One clinical trial indicated the effective long-term hyperthermo-therapy for maintaining performance status, symptomatic improvement, and prolongation of survival time in patients with peritoneal dissemination [4].
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