Relevant bibliographies by topics / Proton transporter

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Academic literature on the topic 'Proton transporter'

Author: Grafiati
Published: 4 June 2021
Last updated: 17 February 2022

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Journal articles on the topic "Proton transporter"

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Milanick, M. A., and R. B. Gunn. "Proton inhibition of chloride exchange: asynchrony of band 3 proton and anion transport sites?" American Journal of Physiology-Cell Physiology 250, no. 6 (June 1, 1986): C955—C969. http://dx.doi.org/10.1152/ajpcell.1986.250.6.c955.

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The inhibition of chloride exchange at 0 degrees C by protons at the cytoplasmic and the extracellular surface of the band 3 protein of human erythrocytes was measured between pH 4.6 and 7.6. At constant external pH and chloride concentration, internal protons were a mixed inhibitor of chloride flux, with the apparent pK2 = 6.1 for protonation of the inward-facing empty transporter conformation and the apparent pK3 = 5.7 for protonation of the chloride-transporter complex. The activation of chloride exchange by external chloride was inhibited by internal protons, and internal protonation of the externally facing empty conformation had a pK1 = 6.1. External protons were also a mixed inhibitor of chloride exchange with the apparent pK1 = 5.0 for the empty outward-facing transporter conformation. Because of the pHo dependence of self-inhibition, the value of pK3 on the outside for chloride could not be accurately determined, but the apparent pK3 for protonation of the iodide-transporter complex on the extracellular surface was 4.9. The data support a mechanism with a single proton binding site that can alternatively have access to the cytoplasmic and extracellular solutions. It appears that this proton binding and transport site can be coupled to the single anion transport site for cotransport, but the two sites can be on opposite sides of the membrane at the same time and thus can be asynchronously transported by conformational changes of band 3.
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Becker, Holger M., and Joachim W. Deitmer. "Transport Metabolons and Acid/Base Balance in Tumor Cells." Cancers 12, no. 4 (April 7, 2020): 899. http://dx.doi.org/10.3390/cancers12040899.

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Solid tumors are metabolically highly active tissues, which produce large amounts of acid. The acid/base balance in tumor cells is regulated by the concerted interplay between a variety of membrane transporters and carbonic anhydrases (CAs), which cooperate to produce an alkaline intracellular, and an acidic extracellular, environment, in which cancer cells can outcompete their adjacent host cells. Many acid/base transporters form a structural and functional complex with CAs, coined “transport metabolon”. Transport metabolons with bicarbonate transporters require the binding of CA to the transporter and CA enzymatic activity. In cancer cells, these bicarbonate transport metabolons have been attributed a role in pH regulation and cell migration. Another type of transport metabolon is formed between CAs and monocarboxylate transporters, which mediate proton-coupled lactate transport across the cell membrane. In this complex, CAs function as “proton antenna” for the transporter, which mediate the rapid exchange of protons between the transporter and the surroundings. These transport metabolons do not require CA catalytic activity, and support the rapid efflux of lactate and protons from hypoxic cancer cells to allow sustained glycolytic activity and cell proliferation. Due to their prominent role in tumor acid/base regulation and metabolism, transport metabolons might be promising drug targets for new approaches in cancer therapy.
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Sacher, A., A. Cohen, and N. Nelson. "Properties of the mammalian and yeast metal-ion transporters DCT1 and Smf1p expressed in Xenopus laevis oocytes." Journal of Experimental Biology 204, no. 6 (March 15, 2001): 1053–61. http://dx.doi.org/10.1242/jeb.204.6.1053.

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Transition metals are essential for many metabolic processes, and their homeostasis is crucial for life. Metal-ion transporters play a major role in maintaining the correct concentrations of the various metal ions in living cells. Little is known about the transport mechanism of metal ions by eukaryotic cells. Some insight has been gained from studies of the mammalian transporter DCT1 and the yeast transporter Smf1p by following the uptake of various metal ions and from electrophysiological experiments using Xenopus laevis oocytes injected with RNA copies (c-RNA) of the genes for these transporters. Both transporters catalyze the proton-dependent uptake of divalent cations accompanied by a ‘slippage’ phenomenon of different monovalent cations unique to each transporter. Here, we further characterize the transport activity of DCT1 and Smf1p, their substrate specificity and their transport properties. We observed that Zn(2+) is not transported through the membrane of Xenopus laevis oocytes by either transporter, even though it inhibits the transport of the other metal ions and enables protons to ‘slip’ through the DCT1 transporter. A special construct (Smf1p-s) was made to enhance Smf1p activity in oocytes to enable electrophysiological studies of Smf1p-s-expressing cells. 54Mn(2+) uptake by Smf1p-s was measured at various holding potentials. In the absence of Na(+) and at pH 5.5, metal-ion uptake was not affected by changes in negative holding potentials. Elevating the pH of the medium to 6.5 caused metal-ion uptake to be influenced by the holding potential: ion uptake increased when the potential was lowered. Na(+) inhibited metal-ion uptake in accordance with the elevation of the holding potential. A novel clutch mechanism of ion slippage that operates via continuously variable stoichiometry between the driving-force pathway (H(+)) and the transport pathway (divalent metal ions) is proposed. The possible physiological advantages of proton slippage through DCT1 and of Na(+) slippage through Smf1p are discussed.
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Sharma, Neha, Nanda G. Aduri, Anna Iqbal, Bala K. Prabhala, and Osman Mirza. "Peptide Selectivity of the Proton-Coupled Oligopeptide Transporter from Neisseria meningitidis." Journal of Molecular Microbiology and Biotechnology 26, no. 5 (2016): 312–19. http://dx.doi.org/10.1159/000447129.

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Peptide transport in living organisms is facilitated by either primary transport, hydrolysis of ATP, or secondary transport, cotransport of protons. In this study, we focused on investigating the ligand specificity of the <i>Neisseria meningitidis</i> proton-coupled oligopeptide transporter (NmPOT). It has been shown that the gene encoding this transporter is upregulated during infection. NmPOT conformed to the typical chain length preference as observed in prototypical transporters of this family. In contrast to prototypical transporters, it was unable to accommodate a positively charged peptide residue at the C-terminus position of the substrate peptide. Sequence analysis of the active site of NmPOT displayed a distinctive aromatic patch, which has not been observed in any other transporters from this family. This aromatic patch may be involved in providing NmPOT with its atypical preferences. This study provides important novel information towards understanding how these transporters recognize their substrates.
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Cheeseman, Chris. "GLUT7: a new intestinal facilitated hexose transporter." American Journal of Physiology-Endocrinology and Metabolism 295, no. 2 (August 2008): E238—E241. http://dx.doi.org/10.1152/ajpendo.90394.2008.

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The very last member of the SLC2A gene family of facilitated hexose transporters to be cloned was SLC2A7 (hGLUT7). It has been assigned to the class II of the GLUT family on the basis of sequence similarity, and its closest family member is GLUT5, an intestinal fructose transporter. GLUT7 is primarily expressed in the small intestine and colon, although mRNA has been detected in the testis and prostate as well. The protein is expressed in the apical membrane of the small intestine and colon, and it has a high affinity (<0.5 mM) for glucose and fructose. The abundance of the protein in the small intestine does change in parallel with the dietary carbohydrate. However, the distribution of GLUT7 along the small intestine does not entirely match with the availability of glucose and fructose, suggesting that the physiological substrate for this transporter has yet to be identified. Unlike GLUT13, the proton-coupled myoinositol transporter (HMIT), there is no evidence for the coupling of protons to the hexose movement via GLUT7. One area of study in which GLUT7 has provided a useful comparison with GLUT1 has been in the development of the hypothesis that the facilitated hexose transporters may have a selectivity filter at the exofacial opening of the translocation pore, which helps to determine which hexoses can be transported. If substantiated, the elucidation of this mechanism may prove useful in the design of hexose analogs for use in cancer imaging and therapeutics.
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Adibi, SA. "Intestinal Oligopeptide Transporter: From Hypothesis to Cloning." Physiology 11, no. 3 (June 1, 1996): 133–37. http://dx.doi.org/10.1152/physiologyonline.1996.11.3.133.

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Several decades ago it was hypothesized that there is an active intestinal oligopeptide transporter that allows large-scale absorption of dipeptides and tripeptides. After a period of uncertainty, this hypothesis was recently validated by the cloning of an intestinal oligopeptide transporter that appears to belong to a superfamily of proton-dependent transporters.
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Groeneveld, Maarten, Ruud G. J. Detert Oude Weme, Ria H. Duurkens, and Dirk Jan Slotboom. "Biochemical Characterization of the C4-Dicarboxylate Transporter DctA from Bacillus subtilis." Journal of Bacteriology 192, no. 11 (April 2, 2010): 2900–2907. http://dx.doi.org/10.1128/jb.00136-10.

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ABSTRACT Bacterial secondary transporters of the DctA family mediate ion-coupled uptake of C4-dicarboxylates. Here, we have expressed the DctA homologue from Bacillus subtilis in the Gram-positive bacterium Lactococcus lactis. Transport of dicarboxylates in vitro in isolated membrane vesicles was assayed. We determined the substrate specificity, the type of cotransported ions, the electrogenic nature of transport, and the pH and temperature dependence patterns. DctA was found to catalyze proton-coupled symport of the four C4-dicarboxylates from the Krebs cycle (succinate, fumurate, malate, and oxaloacetate) but not of other mono- and dicarboxylates. Because (i) succinate-proton symport was electrogenic (stimulated by an internal negative membrane potential) and (ii) the divalent anionic form of succinate was recognized by DctA, at least three protons must be cotransported with succinate. The results were interpreted in the light of the crystal structure of the homologous aspartate transporter GltPh from Pyrococcus horikoshii.
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Dastvan, Reza, Axel W. Fischer, Smriti Mishra, Jens Meiler, and Hassane S. Mchaourab. "Protonation-dependent conformational dynamics of the multidrug transporter EmrE." Proceedings of the National Academy of Sciences 113, no. 5 (January 19, 2016): 1220–25. http://dx.doi.org/10.1073/pnas.1520431113.

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The small multidrug transporter from Escherichia coli, EmrE, couples the energetically uphill extrusion of hydrophobic cations out of the cell to the transport of two protons down their electrochemical gradient. Although principal mechanistic elements of proton/substrate antiport have been described, the structural record is limited to the conformation of the substrate-bound state, which has been shown to undergo isoenergetic alternating access. A central but missing link in the structure/mechanism relationship is a description of the proton-bound state, which is an obligatory intermediate in the transport cycle. Here we report a systematic spin labeling and double electron electron resonance (DEER) study that uncovers the conformational changes of EmrE subsequent to protonation of critical acidic residues in the context of a global description of ligand-induced structural rearrangements. We find that protonation of E14 leads to extensive rotation and tilt of transmembrane helices 1–3 in conjunction with repacking of loops, conformational changes that alter the coordination of the bound substrate and modulate its access to the binding site from the lipid bilayer. The transport model that emerges from our data posits a proton-bound, but occluded, resting state. Substrate binding from the inner leaflet of the bilayer releases the protons and triggers alternating access between inward- and outward-facing conformations of the substrate-loaded transporter, thus enabling antiport without dissipation of the proton gradient.
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Sigal, Nadejda, Shahar Molshanski-Mor, and Eitan Bibi. "No Single Irreplaceable Acidic Residues in the Escherichia coli Secondary Multidrug Transporter MdfA." Journal of Bacteriology 188, no. 15 (August 1, 2006): 5635–39. http://dx.doi.org/10.1128/jb.00422-06.

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ABSTRACT The largest family of solute transporters (major facilitator superfamily [MFS]) includes proton-motive-force-driven secondary transporters. Several characterized MFS transporters utilize essential acidic residues that play a critical role in the energy-coupling mechanism during transport. Surprisingly, we show here that no single acidic residue plays an irreplaceable role in the Escherichia coli secondary multidrug transporter MdfA.
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Zulkifli, Mohammad, and Anand Kumar Bachhawat. "Identification of residues critical for proton-coupled glutathione translocation in the yeast glutathione transporter, Hgt1p." Biochemical Journal 474, no. 11 (May 16, 2017): 1807–21. http://dx.doi.org/10.1042/bcj20161063.

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The proton gradient acts as the driving force for the transport of many metabolites across fungal and plant plasma membranes. Identifying the mechanism of proton relay is critical for understanding the mechanism of transport mediated by these transporters. We investigated two strategies for identifying residues critical for proton-dependent substrate transport in the yeast glutathione transporter, Hgt1p, a member of the poorly understood oligopeptide transporter family of transporters. In the first strategy, we tried to identify the pH-independent mutants that could grow at higher pH when dependant on glutathione transport. Screening a library of 269 alanine mutants of the transmembrane domains (TMDs) along with a random mutagenesis strategy yielded two residues (E135K on the cusp of TMD2 and N710S on TMD12) that permitted growth on glutathione at pH 8.0. Further analysis revealed that these residues were not involved in proton symport even though they conferred better transport at a higher pH. The second strategy involved a knowledge-driven approach, targeting 31 potential residues based on charge, conservation and location. Mutation of these residues followed by functional and biochemical characterization revealed E177A, Y193A, D335A, Y374A, H445A and R554A as being defective in proton transport. Further analysis enabled possible roles of these residues to be assigned in proton relay. The implications of these findings in relation to Hgt1p and the suitability of these strategic approaches for identifying such residues are discussed.
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Dissertations / Theses on the topic "Proton transporter"

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Bapna, Akanksha. "Drug and proton translocation by the multidrug transporter LmrP." Thesis, University of Cambridge, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.613705.

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Khadilkar, Aswad S. "Manipulations of Sucrose/Proton Symporters and Proton-pumping Pyrophosphatase Lead to Enhanced Phloem Transport But Have Contrasting Effects on Plant Biomass." Thesis, University of North Texas, 2015. https://digital.library.unt.edu/ark:/67531/metadc801879/.

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Delivery of photoassimilate, mainly sucrose (Suc) from photoautotrophic source leaves provides the substrate for the growth and maintenance of sink tissues such as roots, storage tissues, flowers and fruits, juvenile organs, and seeds. Phloem loading is the energized process of accumulating solute in the sieve element/companion cell complex of source leaf phloem to generate the hydrostatic pressure that drives long-distance transport. In many plants this is catalyzed by Suc/Proton (H+) symporters (SUTs) which are energized by the proton motive force (PMF). Overexpression of SUTs was tested as means to enhance phloem transport and plant productivity. Phloem specific overexpression of AtSUC2 in wild type (WT) tobacco resulted in enhanced Suc loading and transport, but against the hypothesis, plants were stunted and accumulated carbohydrates in the leaves, possibly due to lack of sufficient energy to support enhanced phloem transport. The energy for SUT mediated phloem loading is provided from the PMF, which is ultimately supplied by the oxidation of a small proportion of the loaded photoassimilates. It was previously shown that inorganic pyrophosphate (PPi) is necessary for this oxidation and overexpressing a proton-pumping pyrophosphatase (AVP1) enhanced both shoot and root growth, and augmented several energized processes like nutrient acquisition and stress responses. We propose that AVP1 localizes to the PM of phloem cells and uses PMF to synthesize PPi rather than hydrolyze it, and in doing so, maintains PPi levels for efficient Suc oxidation and ATP production. Enhanced ATP production in turn strengthens the PMF via plasma membrane (PM) ATPase, increasing phloem energization and phloem transport. Phloem-specific and constitutive AVP1 overexpressing lines showed increased growth and more efficiently moved carbohydrates to sink organs compared to WT. This suggested changes in metabolic flux but diagnostic metabolites of central metabolism did not show changes in steady state levels. This research focuses on fundamental aspects of carbon utilization and transport, and has a strong applied component, since increased H+-PPase activity enhances plant biomass, nutrient up-take capacities, and stress tolerance for as yet not fully characterized reasons.
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Wege, Stefanie. "Structure, function and regulation of the nitrate/proton transporter AtCLCa in arabidopsis thaliana." Paris 11, 2010. http://www.theses.fr/2010PA112146.

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AtCLCa chez Arabidopsis thaliana appartient à la famille de transporteurs d’anions appelés ‘ChLoride Channel’ (CLC). AtCLCa est plus sélectif pour le nitrate que pour le chlorure. C’est un antiporteur NO3-/H+ à l’origine de l’accumulation du nitrate dans la vacuole. La différence de sélectivité est due à un simple changement d’un acide aminé. Nous avons pu montrer que le changement de cet acide aminé transforme AtCLCa en un transporteur de chlorure et est incapable de réaliser sa fonction dans l’accumulation de nitrate dans la vacuole in planta. De plus, nous avons démontré que AtCLCa est directement régulé par la liaison de l’ATP et que cet effet est influencé par le rapport ATP/AMP, l’AMP supprimant l’effet de l’ATP. Ceci suggère que la régulation de AtCLCa est dépendante du statut énergétique de la cellule. En supplément, nous avons aussi montré que cette protéine est régulée par phosphorylation dans sa partie N-terminale. Nous avons identifié une classe de protéines, les SnRKs, qui sont capables de phosphoryler AtCLCa in vitro et d’interagir avec AtCLCa in vivo. SnRK1. 1 et SnRK2. 6. SnRK1. 1 est exprimée de manière ubiquitaire dans la plante et peut inhiber l’activité de la nitrate réductase. Des études d’expression GUS montrent que AtCLCa est exprimé au travers de la plante (comme SnRK1. 1) mais une forte expression observée dans les cellules de garde comme pour SnRK2. 6. Des analyses phénotypiques des mutants nuls clca démontrent la fonction de AtCLCa non seulement dans l’accumulation du nitrate mais aussi dans les mouvements stomatiques. Ces résultats suggèrent une possible interaction dans les cellules de garde de la kinase SnRK2. 6 et ATCLCa in planta
The Arabidopsis thaliana CLCa belongs to the ChLoride Channel (CLC) family of anion transport proteins. AtCLCa is most selective for nitrate and not for chloride. It mediates the accumulation of nitrate into the vacuole by a NO3-/H+ exchanger mechanism. The difference in selectivity is accompanied by a single amino acid difference. We could show that an exchange of this amino acid turns AtCLCa into a chloride transporter and abolishes its function of nitrate accumulation in planta. Furthermore, we could show that AtCLCa is directly regulated by ATP and that this effect is influenced by the ATP/AMP ratio, as AMP abolished the effect of ATP, suggesting an energy-state dependent regulation of AtCLCa in the cell. Additionally to the regulation of AtCLCa by nucleotides, we could also show that it is regulated by phosphorylation on its N-terminus. We identified a specific class of kinases, the SnRKs, which are able to phosphorylate AtCLCa in vitro and interact with it in vivo. We focused on two candidate kinases within this family, SnRK1. 1 and SnRK2. 6. SnRK1. 1 can inhibit the nitrate reductase. Therefore, the activity of SnRK1. 1 is connected to nitrate metabolism, like the activity of AtCLCa. SnRK2. 6 is strongly expressed in stomata guard cells and GUS expression studies showed that AtCLCa is expressed throughout the plant (like SnRK1. 1), but shows a particular high expression in stomata guard cells like SnRK2. 6. Subsequent phenotype analyses of clca knock-out mutants demonstrated a role of AtCLCa not only in nitrate accumulation but also in stomata movement, suggesting a possible interaction of the guard cell kinase SnRK2. 6 and AtCLCa in planta
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Martínez, Molledo María [Verfasser], and Christian [Akademischer Betreuer] Löw. "Multispecific substrate recognition in a Proton-Dependent Oligopeptide Transporter / María Martínez Molledo ; Betreuer: Christian Löw." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2019. http://d-nb.info/1175584835/34.

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Li, Dan. "Novel Protein Materials based on Bacterial Efflux Pumps." University of Cincinnati / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1304692634.

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Hodin, Julie. "Le couplage nitrate/proton au sein de l’échangeur AtClCa est essentiel à la physiologie de la plante en réponse aux fluctuations environnementales." Thesis, Université Paris-Saclay (ComUE), 2018. http://www.theses.fr/2018SACLS181/document.

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Chez les plantes, le nitrate est un élément essentiel mais sa disponibilité dans le sol est fluctuante. Il est donc stocké dans la vacuole grâce à un échangeur nitrate/proton appelé AtClCa. La famille de protéines ClCs comporte à la fois des échangeurs mais aussi des canaux suggérés comme issus de l’évolution des échangeurs par une conversion mécanistique. Chez Arabidopsis thaliana, seuls des ClCs échangeurs assurent la gestion du nitrate. Deux glutamates très conservés, E203 et E270 dans AtClCa, sont essentiels pour le transport des protons chez les ClCs échangeurs. La mutation du résidu E203 en une alanine, un acide aminé non protonable (E203A) a permis de produire artificiellement une telle conversion mécanistique. Afin de mieux comprendre l’importance physiologique du mécanisme d’échange, une analyse a été conduite sur des plantes exprimant la forme mutée d’AtClCa pour ce glutamate. Chez ces plantes, le stockage vacuolaire est fortement réduit au profit d’une importante assimilation accroissant la teneur en protéines. En dépit de cela, elles présentent un défaut de production de biomasse résultant en grande partie d’une perturbation de l’homéostasie hydrique. Elles sont également plus sensibles aux stress hydrique et probablement azoté. La conservation d’un échangeur est donc requise pour croitre en dépit des fluctuations environnementales. En parallèle, la mutation E270A a été introduite en plante afin d’étudier son importance sur la physiologie d’Arabidopsis. Une analyse préliminaire de la biomasse et des contenus en nitrate et eau de plantes exprimant la forme mutée de ce glutamate est donc présentée dans la seconde partie de cette thèse
Nitrate is a major element for plant but its availability is very fluctuant in soils. Then, it is stored in vacuoles thanks to a nitrate/proton exchanger named AtClCa. In ClCs, exchangers but also channels were identified, the latest were suggested to be evolved from exchanger in which a mechanistic switch happened. In Arabidopsis thaliana, only exchangers are involved in nitrate management. Two conserved glutamate, E203 and E270 in AtClCa, are essential for protons transport in ClCs exchangers. The mutation of E203 into an alanine, a non-protonable amino acid (E203A) artificially produces such a mechanistic switch. To better understand the physiological importance of this exchange mechanism, a study was conducted in plants expressing the mutated form of AtClCa for this glutamate. In those plants, the vacuolar storage is highly restricted whereas the assimilation is favoured and the protein content increased. Despite that, the biomass production is decreased mostly because of a hydric homeostasis disruption. Those plants are also more sensitive to hydric and probably nitrogenous stress. The exchanger conservation is then required for plant growth whatever the environmental fluctuations. In parallel, the mutation E270A was introduced in planta to study its physiological importance. A preliminary analysis of plant biomass and nitrate and water contents was then performed in plants expressing the E270A mutated form of AtClCa and the results are presented in the second part of the manuscript
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Peterson, Emily. "Proteoliposome Proton Flux Assays Establish Net Conductance, pH-Sensitivity, and Functional Integrity of a Novel Truncate of the M2 Ion "Channel" of Influenza A." BYU ScholarsArchive, 2010. https://scholarsarchive.byu.edu/etd/2420.

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A novel truncate of Influenza A M2 protein (residues 22-62), incorporated into a uniquely tailored proteoliposome proton uptake assay, demonstrated proton flux more characteristic of an ion transporter than a traditional ion "channel." The liposome paradigm was essential for testing the conductance activity of this M2 truncate at a range of extraphysiological pHs appropriate for channel vs. transport function determination. In addition to transporter-typical proton flux, M2(22-62) showed the key characteristics of functional integrity: selective proton uptake into liposomes and block of uptake by amantadine. Two sets of proteoliposome proton flux assays were carried out, Set 1 at pH values of 6.5, 6.0. 5.5, 5.0, and 4.5; Set 2 at pH values of 6.25, 6.0, 5.75, 5.5, 5.25, 5.0, and 4.75. Observed flux rates followed a proton transport saturation curve similar to that observed in mouse erythroleukemia cells1. Proton transport was maximal at pH 5.5 in Set 1 (139 H+/second/tetramer) and at pH 5.75 in Set 2 (43 H+/second/tetramer). Amantadine block was strongest at pH 5.5 in Set 1 and 6.25 in Set 2, and apparent desensitization of the protein severely reduced proton flux and amantadine sensitivity below pH 5.5 in both sets of experiments. Decreased external pH increased proton uptake with an apparent pKa of 6 (Set 1) or 6.5 (Set 2). These data indicate acid activation of M2(22-62) between pH 5.5-6, optimal amantadine block between pH 5.5-6.25, and a loss of peptide functionality between pH 5.9-4.7.
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Forrest, Lucy R. "Simulation studies of proton channels and transporters." Thesis, University of Oxford, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365828.

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Zhang, Lejie. "Fluorescent Visualization of Cellular Proton Fluxes." eScholarship@UMMS, 2018. https://escholarship.umassmed.edu/gsbs_diss/999.

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Proton fluxes through plasma membranes are essential for regulating intracellular and extracellular pH and mediating co-transport of metabolites and ions. Although conventional electrical measurements are highly sensitive and precise for proton current detection, they provide limited specificity and spatial information. My thesis focuses on developing optical approaches to visualize proton fluxes from ion channels and transporters. It has been demonstrated that channel-mediated acid extrusion causes proton depletion at the inner surface of the plasma membrane. Yet, proton dynamics at the extracellular microenvironment are still unclear. In Chapter II, we developed an optical approach to directly measure pH change in this nanodomain by covalently attaching small-molecule, fluorescent proton sensors to the cell’s glycocalyx using glyco-engineering and copper free ‘click’ chemistry. The extracellularly facing sensors enable real-time detection of proton accumulation and depletion at the plasma membrane, providing an indirect readout of channel and transporter activity that correlated with whole-cell proton current. Moreover, the proton wavefront emanating from one cell was readily visible as it crossed over nearby cells. The transport of monocarboxylates, such as lactate and pyruvate is critical for energy metabolism and is mainly mediated by proton-coupled monocarboxylate transporters (MCT1-MCT4). Although pH electrodes and intracellular fluorescent pH sensors have been widely used for measuring the transport of proton-coupled MCTs, they are unable to monitor the subcellular activities and may underestimate the transport rate due to cell’s volume and intracellular buffering. In Chapter III, we used the Chapter II approach to visualize proton-coupled transport by MCT1-transfected HEK293T cells and observed proton depletion followed by a recovery upon extracellular perfusion of L-lactate or pyruvate. In addition, we identified a putative MCT, CG11665/Hrm that is essential for autophagy during cell death in Drosophila. The results demonstrate that Hrm is a bona fide proton-coupled monocarboxylate transporter that transports pyruvate faster than lactate. Although the approach developed in Chapter II enables visualization of proton fluxes from ion channels and transporters, it’s not applicable in some cell types which cannot incorporate unnatural sialic acid precursors into their glycocalyx, such as INS-1 cells and cardiomyocytes. To address this, in Chapter IV we developed a pH-sensitive, fluorescent WGA conjugate, WGA-pHRho that binds to endogenous glycocalyx. Compared to the results in Chapter II and III, cell surface-attached WGA-pHRho has similar fluorescent signals in response to proton fluxes from proton channel Hv1, omega mutant Shaker-IR R362H and MCT1. With WGA-pHRho, we were able to label the plasma membrane of INS-cells and cardiomyocytes and visualized the transport activity of MCT1 in these cells. Taken together, these findings provide news insights into proton dynamics at the extracellular environment and provide new optical tools to visualize proton fluxes from ion channels and transporters. Moreover, the modularity of the approaches makes them adaptable to study any transport events at the plasma membrane in cells, tissues, and organisms.
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Samsudin, Mohd Firdaus. "Improving oral drug delivery : computational studies of proton dependent oligopeptide transporters : computational studies of peptide transporters." Thesis, University of Oxford, 2015. https://ora.ox.ac.uk/objects/uuid:ce400815-fd55-49dc-8f43-3f620d3e132e.

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Proton dependent oligopeptide transporters (POTs) play a central role in nitrogen homeostasis by coupling the uptake of dipeptides and tripeptides to the proton electrochemical gradient across the plasma membrane. In human, members of this transporter family, PepT1 and PepT2, are critical modulators of drug pharmacokinetics as they facilitate the uptake and retention of numerous orally administered drugs including the β-lactam antibiotics. Rationally designing drugs to target these transporters is therefore an attractive approach to improving bioavailability. To this end, the binding of peptides to a bacterial homolog, PepTSt, was modelled based on recently determined crystal structures. A range of computational methods to predict the free energy of binding were evaluated and a hybrid approach, where the end-point methods were used to classify peptides into strong and poor binders and a theoretically exact method for refinement, was able to accurately predict ligand affinities. This approach was utilised to investigate the substrate preference of PepTSt and the results were validated using in vitro transport assays. To extend this study to the human peptide transporters, homology models of PepT1 and PepT2 were built using the crystal structures of PepTSo and mouse and rat extracellular domains (ECDs) as the templates. Essential residues as proposed by various mutational studies align well with the binding cavity, suggesting that the models are structurally sound. Applying the free energy methods to predict the affinities of peptides and drugs to the homology model of PepT1, however, resulted in discrepancies with experimental data, highlighting the importance of a high-resolution crystal structure in binding affinity predictions. Based on the results for PepTSt, a binding model for peptide prodrugs and β-lactam antibiotics to the human PepT1 was proposed. Overall, this thesis provides a framework for future computational studies using free energy methods to understand drug interactions with pharmaceutically relevant transporters.
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Books on the topic "Proton transporter"

1

Nelson, Nathan. Organellar proton-ATPases. New York: Springer-Verlag, 1995.

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Borka, D. Channeling of protons through carbon nanotubes. Hauppauge, N.Y: Nova Science Publishers, 2011.

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Tripathi, Ratikanta. Proton-nucleus elastic cross sections using two-body in-medium scattering amplitudes. Hampton, Va: National Aeronautics and Space Administration, Langley Research Center, 2001.

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Tripathi, Ratikanta. Proton-nucleus elastic cross sections using two-body in-medium scattering amplitudes. Hampton, Va: National Aeronautics and Space Administration, Langley Research Center, 2001.

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Tripathi, Ratikanta. Proton-nucleus elastic cross sections using two-body in-medium scattering amplitudes. Hampton, Va: National Aeronautics and Space Administration, Langley Research Center, 2001.

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Tripathi, Ratikanta. Proton-nucleus elastic cross sections using two-body in-medium scattering amplitudes. Hampton, Va: National Aeronautics and Space Administration, Langley Research Center, 2001.

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author, Mak M. W., ed. Machine learning for protein subcellular localization prediction. Boston: De Gruyter, 2015.

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R, Westwood Olwyn M., ed. Protein targeting and secretion. Oxford, OX: IRL Press at Oxford University Press, 1991.

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Richard, Zimmermann. Protein transport into the endoplasmic reticulum. Austin, Tex: Landes Bioscience, 2009.

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An introduction to the passage of energetic particles through matter. Boca Raton: Taylor & Francis, 2007.

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Book chapters on the topic "Proton transporter"

1

Postis, Vincent L. G., and Stephen A. Baldwin. "Membrane Transport Proteins: The Proton-Dependentë­±Oligopeptide Transporter Family." In Encyclopedia of Biophysics, 1489–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_744.

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Cha, Hi-jea, and Klaas Martinus Pos. "Cooperative Transport Mechanism and Proton-Coupling in the Multidrug Efflux Transporter Complex ArcAB-TolC." In Springer Series in Biophysics, 207–32. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-53839-1_9.

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Reames, Donald V. "Hydrogen Abundances and Shock Waves." In Solar Energetic Particles, 187–219. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-66402-2_9.

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AbstractHow well do protons fit into the abundance patterns of the other elements? Protons have Q = 1 and A/Q = 1 at all temperatures of interest. When does their relative abundance fit on the power law in A/Q defined by the elements with A/Q > 2? For small “pure” impulsive events, protons fit well, but for larger CME-associated impulsive events, where shock waves boost the intensities, protons are enhanced a factor of order ten by addition of seed protons from the ambient plasma. During most large gradual SEP events with strong shock waves, protons again fit the power law, but with weaker or quasi-perpendicular shock waves, dominated by residual impulsive seed particle abundances at high Z, again protons are enhanced. Proton enhancements occur when moderately weak shock waves happen to sample a two-component seed population with dominant protons from the ambient coronal plasma and impulsive suprathermal ions at high Z; thus proton-enhanced events are a surprising new signature of shock acceleration in jets. A/Q measures the rigidity dependence of both acceleration and transport but does not help us distinguish the two. Energy-spectral indices and abundances are correlated for most gradual events but not when impulsive ions are present; thus we end with powerful new correlations that probe both acceleration and transport.
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Torres, A., S. A. Newton, B. Crompton, A. Borzutzky, E. J. Neufeld, L. Notarangelo, and G. T. Berry. "CSF 5-Methyltetrahydrofolate Serial Monitoring to Guide Treatment of Congenital Folate Malabsorption Due to Proton-Coupled Folate Transporter (PCFT) Deficiency." In JIMD Reports, 91–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/8904_2015_445.

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Matherly, Larry H., Ndeye Diop-Bove, and I. David Goldman. "Biological Role, Properties, and Therapeutic Applications of the Reduced Folate Carrier (RFC-SLC19A1) and the Proton-Coupled Folate Transporter (PCFT-SLC46A1)." In Targeted Drug Strategies for Cancer and Inflammation, 1–34. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-8417-3_1.

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Nagle, John F. "Proton Transport in Condensed Matter." In NATO ASI Series, 17–28. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3444-0_2.

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Sauer, Norbert. "Proton-Sugar Co-transporters in Plants." In Transport and Receptor Proteins of Plant Membranes, 67–75. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3442-6_6.

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King, G. F., and C. A. R. Boyd. "Proton NMR Studies of Transmembrane Solute Transport." In Cell Membrane Transport, 297–323. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4757-9601-8_16.

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Harikumar, P., and John P. Reeves. "The Lysosomal Proton Pump." In New Insights into Cell and Membrane Transport Processes, 61–74. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5062-0_4.

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Romero-Castañon, Tatiana, and W. Mérida. "Water Transport through Proton Exchange Membranes." In THERMEC 2006 Supplement, 310–14. Stafa: Trans Tech Publications Ltd., 2006. http://dx.doi.org/10.4028/0-87849-429-4.310.

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Conference papers on the topic "Proton transporter"

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Dutta, Prashanta, and Jin Liu. "A Bioinspired Active Micropump." In ASME 2015 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/imece2015-52411.

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A preliminary design concept is provided for a bioinspired active micropump. The proposed micropump uses light energy to activate the transporter proteins (bacteriorhodopsin protein and sucrose/sugar transporter proteins), which create an osmotic pressure gradient and drive the fluid flow. The purpose of the bacteriorhodopsin protein is to pump proton from the pumping section to the sucrose source for a proton gradient. This proton gradient is used by the sucrose transporter proteins to transport sugar molecules from the sucrose solution chamber to the pumping channel, which generates an osmotic pressure in the pumping section. A numerical model is used to evaluate the performance of the micropump where the concentrations of proton and sucrose molecules are calculated using the conservation of chemical species equations. The fluid flow and pressure field are calculated from momentum and mass conservation equations. Simulation results predict that the micropump is capable of generating a pressure head that is comparable to other non-mechanical pumps. The proposed bioinspired self-sustained micropump will be most effective at low flow rate.
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Sundaresan, Vishnu Baba, and Donald J. Leo. "Modeling and Characterization of a Chemomechanical Actuator Based on Protein Transporters." In ASME 2007 International Mechanical Engineering Congress and Exposition. ASMEDC, 2007. http://dx.doi.org/10.1115/imece2007-43712.

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Plants and animal cells are naturally occurring actuators that exhibit force and motion driven by fluid transport through the cell membrane. The protein transporters embedded in the cell membrane serve as the selective gateway for ion and fluid transport. The actuator presented in this work generates force and deformation from mass transport through an artificial membrane with protein transporters extracted from plant cell membranes. The artificial membrane is formed from purified 1-Palmitoyl-2-Oleoyl-sn-Glycero-3-[Phospho-L-Serine] (Sodium Salt) (POPS), 1-Palmitoyl-2-Oleoyl-sn-Glycero-3-Phosphoethanolamine (POPE) lipids and supported on a porous substrate. The protein transporter used in the actuator membrane is a proton-sucrose cotransporter, SUT4, extracted from yeast cells that genetically modified to grow the cotransporter in their cell membranes. The SUT4 transporter conducts proton and sucrose from the side of the membrane with higher concentration and carries water molecules across the membrane. It is observed from transport characterization experiments that fluid flux through the membrane varies with the applied sucrose concentration and hence is chosen as the control stimulus in the actuator. A modified four-state facilitated diffusion model is applied to the transport characterization data to compute the two characteristic parameters for fluid transport, saturation concentration and translocation rate, through the membrane. The flux rate through the membrane is observed to increase with the concentration till a particular value and saturates at a higher concentration. The concentration at which the flux rate through the membrane saturates is referred to as the saturation concentration. The saturation concentration for the actuator is experimentally found to be 6±0.6mM sucrose on the side with lower pH. The corresponding maximum translocation rate is found to be 9.6±1.2 nl/μ.cm2.min. The maximum steady state deformation produced by the actuator is observed at 30 mM sucrose that corresponds to a force of 0.89 mN.
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Freeman, Eric, Lisa Mauck Weiland, and Wilson S. Meng. "Computational Study of Inclusion Burst via the Proton Sponge Hypothesis." In ASME 2010 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. ASMEDC, 2010. http://dx.doi.org/10.1115/smasis2010-3756.

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Biological proteins embedded in either a biological or an engineered membrane will actively maintain electrochemical balance across that membrane through transport of fluid and charge. While membrane studies are often planar, in nature they typically take the form of inclusions (∼spherical). Study and ultimately manipulation of the protein transporter types and density, and interior/exterior states of these inclusions lend insight into burst mechanisms appropriate to a broad array of engineering and biological applications, such as intracellular burst release of a vaccine. To explore these phenomena the governing equations of each transporter, as well as the membrane state are established. The result is a model requiring the simultaneous solution of a stiff system of differential equations. Presented is the computational solution of this system of equations for a specific burst scenario — the hypothesis that a proton sponge may be employed to expedite intracellular burst release of a DNA vaccine is explored.
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Hou, Zhanjun, M. Roy Wilson, Lucas Wilson, Sita Kugel Desmoulin, Jenny Huang, and Larry H. Matherly. "Abstract 783: Identification of structural determinants of human proton-coupled folate transporter oligomerization." 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.am2014-783.

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Raghavan, Sudhir, Aleem Gangjee, and Larry H. Matherly. "Abstract 1362: Novel proton coupled folate transporter (PCFT) and reduced folate carrier (RFC) pharmacophore models for development of transporter-selective antifolates." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1362.

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Sze, Tsun-kay Jackie, Jin Liu, and Prashanta Dutta. "Numerical Modeling of Fluidic Pumping in Micronetworks of Plants." In ASME 2013 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/imece2013-64826.

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Plant transport mechanisms are of interest in developing micropump for engineering devices. We present a two-dimensional phloem loading and transport model incorporating protein level mechanics with cellular level fluid mechanics. Governing Navier-Stokes, continuity, and Nernst-Planck equations are numerically solved to determine fluid flow and sugar transport. Phloem loading mechanics for active loading is incorporated through a six-state proton sucrose pump kinetic model. The influence of binding rates constants, concentrations, and membrane electrical potential differences on resulting sucrose transport is studied. Numerical results show that increasing rates of the sucrose transporter will noticeably increase outflow. Simulation result also show that a lower leaf sieve sucrose concentration improves outflow. In addition, a more negative membrane electrical potential difference will increase outflow. This numerical model offers insight on parameters that may be significant for implementing plant transport mechanisms in microfluidic devices.
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Giovannetti, Elisa, Paolo A. Zucali, Yehuda G. Assaraf, Niccola Funel, Maria Gemelli, Michal Stark, Leticia G. Leon, et al. "Abstract 4335: Role of proton-coupled folate transporter expression in resistance of mesothelioma patients treated with pemetrexed." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4335.

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Kucheryavykh, Yuriy, Jescelica Ortiz-Rivera, Michael Inyushin, Luis Cubano, Moraima Morales-Cruz, Alejandra Cruz-Montañez, Kai Griebenow, and Lilia Kucheryavykh. "Abstract 2179: Targeted delivery of nanoparticulate cytochrome c into GL261 glioma cells through the proton-coupled folate transporter." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-2179.

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Hou, Zhanjun, Carrie O'Connor, Steve Orr, and Larry H. Matherly. "Abstract 5491: Identification of transcriptional controls responsible for differential gene expression of the proton-coupled folate transporter in human solid tumors." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-5491.

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Jewel, Yead, Prashanta Dutta, and Jin Liu. "Coarse-Grained Molecular Dynamics Simulations of Sugar Transport Across Lactose Permease." In ASME 2015 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/imece2015-52337.

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Sugar (one of the critical nutrition elements for all life forms) transport across the cell membranes play essential roles in a wide range of living organism. One of the most important active transport (against the sugar concentration) mechanisms is facilitated by the transmembrane transporter proteins, such as the Escherichia coli lactose permease (LacY) proteins. Active transport of sugar molecules with LacY proteins requires a proton gradient and a sequence of complicated protein conformational changes. However, the exact molecular mechanisms and the protein structural information involved in the transport process are largely unknown. All atom atomistic simulations are able to provide full details but are limited to relative small length and time scales due to the computational cost. The protein conformational changes during sugar transport across LacY are large scale structural reorganization and inaccessible to all atom simulations. In this work, we investigate the molecular mechanisms and conformational changes during sugar transport using coarse-grained molecular dynamics (CGMD) simulations. In our coarse-grained force field, we follow the procedures developed by Han et al. [1, 2], in which the protein model is united-atom based and each heavy atom together with the attached hydrogen atoms is represented by one site, then the protein force filed is coupled with the MARTINI [3] water and lipid force fields. This hybrid force field takes the advantage of the efficiency of MARTINI force field for the environment (water and lipid), while retaining the detailed conformational information for the proteins. Specifically, we develop the new force fields for interactions between sugar molecules and protein by matching the potential of mean force between all-atom and coarse-grained models. Then we validate our force field by comparing the potential of mean force for a glucose interaction with a carbohydrate binding protein from our new force field, with the results from all atom simulations. After validation, we implement the force field for sugar transport across LacY proteins. Through our simulations we are able to capture the formation/breakage of the important hydrogen bonds and salt bridges, which are crucial to the overall conformational changes of LacY.
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Reports on the topic "Proton transporter"

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Jones, Kevin W. Making Neutrons (and Protons): An Overview of the LANSCE Accelerator, Proton Storage Ring and Beam Transport Systems. Office of Scientific and Technical Information (OSTI), February 2017. http://dx.doi.org/10.2172/1343697.

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Tsoupas, N., L. Ahrens, P. Pile, P. Thieberger, and M. M. Murray. Beam Transport of 4 GeV Protons from AGS to the Proton Interrogation Target of the Neutrino Line (Z_line) and Effect of the Air on the Transported Beam. Office of Scientific and Technical Information (OSTI), October 2008. http://dx.doi.org/10.2172/939992.

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Tsoupas N., L. Ahrens, P. Pile, P. Thieberger, and M. M. Murray. Beam Transport of 4 GeV Protons from AGS to the Proton Interrogation Target of the Neutrino line (Z_line) and Effect of the Air on the Transported Beam. Office of Scientific and Technical Information (OSTI), October 2008. http://dx.doi.org/10.2172/1061916.

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Gregory A. Voth. Mechanism of Proton Transport in Proton Exchange Membranes: Insights from Computer Simulation. Office of Scientific and Technical Information (OSTI), November 2010. http://dx.doi.org/10.2172/993502.

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Yue, J., and A. J. Epstein. Proton Transport on Modified Sulfonated Polyaniline Electrodes. Fort Belvoir, VA: Defense Technical Information Center, June 1992. http://dx.doi.org/10.21236/ada254917.

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Lamb, J. D., J. S. Bradshaw, and R. M. Izatt. Novel macrocyclic carriers for proton-coupled liquid membrane transport. Office of Scientific and Technical Information (OSTI), July 1992. http://dx.doi.org/10.2172/6957516.

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Frischknecht, Amalie Lucile, Eric G. Sorte, Todd M. Alam, Cy Fujimoto, Lauren J. Abbott, Jennifer A. Clark, and Cassandria Eloise Poirier. Understanding Morphology and Proton Transport in Sulfonated Poly(Phenylenes). Office of Scientific and Technical Information (OSTI), September 2018. http://dx.doi.org/10.2172/1529590.

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Lamb, J. D. Novel macrocyclic carriers for proton-coupled liquid membrane transport. Office of Scientific and Technical Information (OSTI), June 1991. http://dx.doi.org/10.2172/6110290.

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Schumaker, Karen S. Calcium-Mediated Regulation of Proton-Coupled Sodium Transport - Final Report. Office of Scientific and Technical Information (OSTI), October 2013. http://dx.doi.org/10.2172/1097278.

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Lamb, J. D., R. M. Izatt, J. S. Bradshaw, and R. B. Shirts. Novel macrocyclic carriers for proton-coupled liquid membrane transport. Final report. Office of Scientific and Technical Information (OSTI), August 1996. http://dx.doi.org/10.2172/418398.

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