Relevant bibliographies by topics / M2 protein

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

Academic literature on the topic 'M2 protein'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "M2 protein"

1

Sansom, Mark S. P., and Ian D. Kerr. "Influenza virus M2 protein: a molecular modelling study of the ion channel." "Protein Engineering, Design and Selection" 6, no. 1 (1993): 65–74. http://dx.doi.org/10.1093/protein/6.1.65.

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Gabbard, J., N. Velappan, R. Di Niro, J. Schmidt, C. A. Jones, S. M. Tompkins, and A. R. M. Bradbury. "A humanized anti-M2 scFv shows protective in vitro activity against influenza." Protein Engineering Design and Selection 22, no. 3 (October 16, 2008): 189–98. http://dx.doi.org/10.1093/protein/gzn070.

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Li, Dongsheng, David A. Jans, Phillip G. Bardin, Jayesh Meanger, John Mills, and Reena Ghildyal. "Association of Respiratory Syncytial Virus M Protein with Viral Nucleocapsids Is Mediated by the M2-1 Protein." Journal of Virology 82, no. 17 (June 25, 2008): 8863–70. http://dx.doi.org/10.1128/jvi.00343-08.

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ABSTRACT Cytoplasmic inclusions in respiratory syncytial virus-infected cells comprising viral nucleocapsid proteins (L, N, P, and M2-1) and the viral genome are sites of viral transcription. Although not believed to be necessary for transcription, the matrix (M) protein is also present in these inclusions, and we have previously shown that M inhibits viral transcription. In this study, we have investigated the mechanisms for the association of the M protein with cytoplasmic inclusions. Our data demonstrate for the first time that the M protein associates with cytoplasmic inclusions via an interaction with the M2-1 protein. The M protein colocalizes with M2-1 in the cytoplasm of cells expressing only the M and M2-1 proteins and directly interacts with M2-1 in a cell-free binding assay. Using a cotransfection system, we confirmed that the N and P proteins are sufficient to form cytoplasmic inclusions and that M2-1 localizes to these inclusions; additionally, we show that M associates with cytoplasmic inclusions only in the presence of the M2-1 protein. Using truncated mutants, we show that the N-terminal 110 amino acids of M mediate the interaction with M2-1 and the subsequent association with nucleocapsids. The interaction of M2-1 with M and, in particular, the N-terminal region of M may represent a target for novel antivirals that block the association of M with nucleocapsids, thereby inhibiting virus assembly.
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Gupta, Vibhor, and Rameshwar N. K. Bamezai. "Human pyruvate kinase M2: A multifunctional protein." Protein Science 19, no. 11 (October 26, 2010): 2031–44. http://dx.doi.org/10.1002/pro.505.

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Parks, G. D., J. D. Hull, and R. A. Lamb. "Transposition of domains between the M2 and HN viral membrane proteins results in polypeptides which can adopt more than one membrane orientation." Journal of Cell Biology 109, no. 5 (November 1, 1989): 2023–32. http://dx.doi.org/10.1083/jcb.109.5.2023.

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The influenza A virus M2 polypeptide is a small integral membrane protein that does not contain a cleaved signal sequence, but is unusual in that it assumes the membrane orientation of a class I integral membrane protein with an NH2-terminal ectodomain and a COOH-terminal cytoplasmic tail. To determine the domains of M2 involved in specifying membrane orientation, hybrid genes were constructed and expressed in which regions of the M2 protein were linked to portions of the paramyxovirus HN and SH proteins, two class II integral membrane proteins that adopt the opposite orientation in membranes from M2. A hybrid protein (MgMH) consisting of the M2 NH2-terminal and membrane-spanning domains linked precisely to the HN COOH-terminal ectodomain was found in cells in two forms: integrated into membranes in the M2 topology or completely translocated across the endoplasmic reticulum membrane and ultimately secreted from the cell. The finding of a soluble form suggested that in this hybrid protein the anchor function of the M2 signal/anchor domain can be overridden. A second hybrid which contained the M2 NH2 terminus linked to the HN signal anchor and ectodomain (MgHH) was found in both the M2 and the HN orientation, suggesting that the M2 NH2 terminus was capable of reversing the topology of a class II membrane protein. The exchange of the M2 signal/anchor domain with that of SH resulted in a hybrid protein which assumed only the M2 topology. Thus, all these data suggest that the NH2-terminal 24 residues to M2 are important for directing the unusual membrane topology of the M2 protein. These data are discussed in relationship to the loop model for insertion of proteins into membranes and the role of charged residues as a factor in determining orientation.
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Wang, J. F., and K. C. Chou. "Insights from studying the mutation-induced allostery in the M2 proton channel by molecular dynamics." Protein Engineering Design and Selection 23, no. 8 (June 22, 2010): 663–66. http://dx.doi.org/10.1093/protein/gzq040.

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Mintaev, Ramil R., Andrei V. Alexeevski, and Larisa V. Kordyukova. "Co-evolution analysis to predict protein–protein interactions within influenza virus envelope." Journal of Bioinformatics and Computational Biology 12, no. 02 (April 2014): 1441008. http://dx.doi.org/10.1142/s021972001441008x.

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Interactions between integral membrane proteins hemagglutinin (HA), neuraminidase (NA), M2 and membrane-associated matrix protein M1 of influenza A virus are thought to be crucial for assembly of functionally competent virions. We hypothesized that the amino acid residues located at the interface of two different proteins are under physical constraints and thus probably co-evolve. To predict co-evolving residue pairs, the EvFold ( http://evfold.org ) program searching the (nontransitive) Direct Information scores was applied for large samplings of amino acid sequences from Influenza Research Database ( http://www.fludb.org/ ). Having focused on the HA, NA, and M2 cytoplasmic tails as well as C-terminal domain of M1 (being the less conserved among the protein domains) we captured six pairs of correlated positions. Among them, there were one, two, and three position pairs for HA–M2, HA–M1, and M2–M1 protein pairs, respectively. As expected, no co-varying positions were found for NA–HA, NA–M1, and NA–M2 pairs obviously due to high conservation of the NA cytoplasmic tail. The sum of frequencies calculated for two major amino acid patterns observed in pairs of correlated positions was up to 0.99 meaning their high to extreme evolutionary sustainability. Based on the predictions a hypothetical model of pair-wise protein interactions within the viral envelope was proposed.
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Chen, Benjamin J., George P. Leser, David Jackson, and Robert A. Lamb. "The Influenza Virus M2 Protein Cytoplasmic Tail Interacts with the M1 Protein and Influences Virus Assembly at the Site of Virus Budding." Journal of Virology 82, no. 20 (August 13, 2008): 10059–70. http://dx.doi.org/10.1128/jvi.01184-08.

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ABSTRACT The cytoplasmic tail of the influenza A virus M2 proton-selective ion channel has been shown to be important for virus replication. Previous analysis of M2 cytoplasmic tail truncation mutants demonstrated a defect in incorporation of viral RNA (vRNA) into virions, suggesting a role for M2 in the recruitment of M1-vRNA complexes. To further characterize the effect of the M2 cytoplasmic tail mutations on virus assembly and budding, we constructed a series of alanine substitution mutants of M2 with mutations in the cytoplasmic tail, from residues 71 to 97. Mutant proteins M2-Mut1 and M2-Mut2, with mutations of residues 71 to 73 and 74 to 76, respectively, appeared to have the greatest effect on virus-like particle and virus budding, showing a defect in M1 incorporation. Mutant viruses containing M2-Mut1 and M2-Mut2 failed to replicate in multistep growth analyses on wild-type (wt) MDCK cells and were able to form plaques only on MDCK cells stably expressing wt M2 protein. Compared to wt M2 protein, M2-Mut1 and M2-Mut2 were unable to efficiently coimmunoprecipitate with M1. Furthermore, statistical analysis of planar sheets of membrane from cells infected by virus containing M2-Mut1 revealed a reduction in M1-hemagglutinin (HA) and M2-HA clustering as well as a severe loss of clustering between M1 and M2. These results suggest an essential, direct interaction between the cytoplasmic tail of M2 and M1 that promotes the recruitment of the internal viral proteins and vRNA to the plasma membrane for efficient virus assembly to occur.
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Rossman, Jeremy S., Xianghong Jing, George P. Leser, Victoria Balannik, Lawrence H. Pinto, and Robert A. Lamb. "Influenza Virus M2 Ion Channel Protein Is Necessary for Filamentous Virion Formation." Journal of Virology 84, no. 10 (March 10, 2010): 5078–88. http://dx.doi.org/10.1128/jvi.00119-10.

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ABSTRACT Influenza A virus buds from cells as spherical (∼100-nm diameter) and filamentous (∼100 nm × 2 to 20 μm) virions. Previous work has determined that the matrix protein (M1) confers the ability of the virus to form filaments; however, additional work has suggested that the influenza virus M2 integral membrane protein also plays a role in viral filament formation. In examining the role of the M2 protein in filament formation, we observed that the cytoplasmic tail of M2 contains several sites that are essential for filament formation. Additionally, whereas M2 is a nonraft protein, expression of other viral proteins in the context of influenza virus infection leads to the colocalization of M2 with sites of virus budding and lipid raft domains. We found that an amphipathic helix located within the M2 cytoplasmic tail is able to bind cholesterol, and we speculate that M2 cholesterol binding is essential for both filament formation and the stability of existing viral filaments.
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Santiago, Luis, and Ravinder Abrol. "Understanding G Protein Selectivity of Muscarinic Acetylcholine Receptors Using Computational Methods." International Journal of Molecular Sciences 20, no. 21 (October 24, 2019): 5290. http://dx.doi.org/10.3390/ijms20215290.

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The neurotransmitter molecule acetylcholine is capable of activating five muscarinic acetylcholine receptors, M1 through M5, which belong to the superfamily of G-protein-coupled receptors (GPCRs). These five receptors share high sequence and structure homology; however, the M1, M3, and M5 receptor subtypes signal preferentially through the Gαq/11 subset of G proteins, whereas the M2 and M4 receptor subtypes signal through the Gαi/o subset of G proteins, resulting in very different intracellular signaling cascades and physiological effects. The structural basis for this innate ability of the M1/M3/M5 set of receptors and the highly homologous M2/M4 set of receptors to couple to different G proteins is poorly understood. In this study, we used molecular dynamics (MD) simulations coupled with thermodynamic analyses of M1 and M2 receptors coupled to both Gαi and Gαq to understand the structural basis of the M1 receptor’s preference for the Gαq protein and the M2 receptor’s preference for the Gαi protein. The MD studies showed that the M1 and M2 receptors can couple to both Gα proteins such that the M1 receptor engages with the two Gα proteins in slightly different orientations and the M2 receptor engages with the two Gα proteins in the same orientation. Thermodynamic studies of the free energy of binding of the receptors to the Gα proteins showed that the M1 and M2 receptors bind more strongly to their cognate Gα proteins compared to their non-cognate ones, which is in line with previous experimental studies on the M3 receptor. A detailed analysis of receptor–G protein interactions showed some cognate-complex-specific interactions for the M2:Gαi complex; however, G protein selectivity determinants are spread over a large overlapping subset of residues. Conserved interaction between transmembrane helices 5 and 6 far away from the G-protein-binding receptor interface was found only in the two cognate complexes and not in the non-cognate complexes. An analysis of residues implicated previously in G protein selectivity, in light of the cognate and non-cognate structures, shaded a more nuanced role of those residues in affecting G protein selectivity. The simulation of both cognate and non-cognate receptor–G protein complexes fills a structural gap due to difficulties in determining non-cognate complex structures and provides an enhanced framework to probe the mechanisms of G protein selectivity exhibited by most GPCRs.
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Dissertations / Theses on the topic "M2 protein"

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Duff, Kevin Campbell. "Biophysical studies on influenza A M2 protein." Thesis, University of Edinburgh, 1993. http://hdl.handle.net/1842/19707.

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The influenza A M2 protein and, in particular, the proposed transmembrane domain, has been implicated in viral infectivity at two stges in the replicative cycle: viral uncoating and assembly. An identical function has been proposed for the protein at both points of interest, that is, that M2 acts as a proton channel. In order to work, this hypothesis assumes that M2 possesses a transmembrane domain, presumably in a α-helical conformation, that this domain orientates in a prescribed manner across the bilayer and that, indeed, M2 is able to translocate protons across the aforementioned bilayer. This thesis examines these assumptions experimentally using a synthetic, 25 amino acid peptide representing the proposed transmembrane domain of M2. The work described herein may be divided into three main areas, each employing a separate biophysical technique. Circular dichroism was employed to assign an α-helical secondary structure to the M2 peptide. Neutron diffraction orientated this region precisely in the bilayer. Electrophysiological techniques observed directly, for the first time in viruses, proton translocation. The effects of amantadine, the only drug prescribed for use against influenza A infections, in each of these structural asnd functional investigations has also been recorded, providing revealing insights into the drug's efficacy. M2 has structural analogs in other enveloped viruses and work such as that reported in this thesis may reveal a common pathway of viral infectivity for groups of enveloped viruses, therefore allowing the possibility of broad-spectrum drug therapies.
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Hayhurst, Andrew. "Studies on the influenza A virus M2 protein." Thesis, Imperial College London, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.250090.

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Carpenter, Timothy S. "Simulation studies of the influenza M2 channel protein." Thesis, University of Oxford, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.504314.

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Rocher, Crystal. "Bone Morphogenetic Protein-7 (BMP-7) Polarizes Monocytes into M2 Macrophages." Master's thesis, University of Central Florida, 2013. http://digital.library.ucf.edu/cdm/ref/collection/ETD/id/5849.

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Atherosclerosis is an inflammatory disease in which an accumulation of fatty acids and cholesterol occurs to form a plaque in small and large arteries. Monocyte polarization to classic M1 macrophages or alternative M2 macrophages is an important area of research that can determine the severity of disease progression. BMP-7 is a key growth factor responsible for directing differentiation of mesenchymal stem cells into brown fat cells, suggesting a role of BMP-7 in cellular plasticity; however, its role in monocyte polarization is yet to be revealed. In the current study, we hypothesize that monocyte treatment with BMP-7 will significantly result in increased polarization of monocytes into M2 macrophages and increased expression of anti-inflammatory cytokines. To that effect, we have established a stress induced cell culture system with monocytes (THP-1 cells) and apoptotic conditioned medium (ACM), simulating injury, to understand the effects of BMP-7 on M2 macrophage polarization from monocytes. Our data demonstrates that the BMP type 2 receptor (BMPR2) is found on monocytes and its activation is significantly (p<0.05) increased in both monocytes and M2 macrophages following treatment with BMP-7. Furthermore, a significant (p<0.05) increase of M2 macrophages in the BMP-7 treated group was shown following immunostaining with CD206 and arginase-1, two M2 macrophage markers, whereas a significant (p<0.05) decrease of iNOS expression, an M1 macrophage marker, was shown. Moreover, treatment with BMP-7 resulted in significantly (p<0.05) increased expression of IL-10 and IL-1ra, two anti-inflammatory cytokines, but significantly (p<0.05) decreased levels of the pro-inflammatory cytokines, MCP-1, IL-6 and TNF-?. We also hypothesize that polarization of monocytes to M2 macrophages occurs through activation of SMAD1/5/8 and PI3K-Akt-mTOR pathways. Upon BMP-7 binding to its receptor, BMPR2, activation of SMAD1/5/8 occurs which then activates the p85 subunit of PI3K resulting in downstream activation of Akt and mTOR. Our data shows that following treatment with BMP-7, expression of p-SMAD1/5/8, p-PI3K, p-Akt and p-mTOR is significantly (p<0.05) increased compared to controls whereas p-PTEN, an inhibitor of the PI3K pathway, is significantly (p<0.05) decreased in the BMP-7 treated group compared to controls. In conclusion, our data reveals that BMP-7 polarizes monocytes into M2 macrophages and it achieves this through activation of the PI3K-Akt-mTOR pathway, which will have significant applications for atherosclerosis treatment.
M.S.
Masters
Molecular Biology and Microbiology
Medicine
Biotechnology
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Tanner, Sian Jean. "Structure and function of human respiratory sncytial virus M2-1 protein." Thesis, University of Leeds, 2013. http://etheses.whiterose.ac.uk/5897/.

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The M2-1 protein of the important pathogen human respiratory syncytial virus is a transcription antiterminator that is essential for viral gene expression. We present the X-ray crystal structure of full-length M2-1 protein in its native tetrameric form at a resolution of 2.52 Å. The structure reveals M2-1 forms a disk-like assembly with tetramerisation driven by a long helix forming a four-helix bundle at its center, further stabilised by contact between the zinc finger and adjacent protomers. The tetramerisation helix is linked to a core domain responsible for RNA binding activity by a flexible loop on which lie two functionally critical serine residues, 58 and 61, that are phosphorylated during infection. The identity of these residues was confirmed by mass spectrometric analysis of M2-1 protein expressed in baculovirus-assisted insect cell culture. The crystal structure of a phosphomimetic M2-1 variant, S58DS61D revealed altered charge density surrounding this flexible loop, although loop position was unaffected. Structure guided mutagenesis identified residues that contributed to RNA binding and antitermination activity, revealing a strong correlation between these two activities, and further defining the role of phosphorylation in M2-1 antitermination activity. The data presented here identify surfaces critical for M2-1 function that may be targeted by anti-viral compounds, and allow us to propose a possible model for M2-1 function during respiratory syncytial virus transcription.
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Aloia, Amanda Louise, and amanda aloia@hotmail com. "Expression, Purification and Crystallisation Studies with the M2 Muscarinic and H1 Histamine Receptors." Flinders University. Biological Sciences, 2008. http://catalogue.flinders.edu.au./local/adt/public/adt-SFU20080709.132140.

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This thesis describes the expression of three human seven transmembrane receptors: the M2 Muscarinic; H1 Histamine and 5HT2A Serotonin receptors, in the baculovirus/insect cell expression system. Purification trials werre conducted on the M2 Muscarinic and H1 Histamine receptors. Preliminary crystallisation attempts were made with the H1 receptor.
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Liao, Shu-Yu Ph D. Massachusetts Institute of Technology. "Structure and dynamics of full-length M2 protein of influenza A virus from solid-state NMR." Thesis, Massachusetts Institute of Technology, 2017. http://hdl.handle.net/1721.1/113974.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Chemistry, 2017.
Cataloged from PDF version of thesis.
Includes bibliographical references.
Solid-state nuclear magnetic resonance (SSNMR) has been frequently used to elucidate the structure and dynamics of membrane proteins and fibrils that are difficult to characterize by Xray crystallography or solution NMR. This thesis focuses on the structure determination and the proton conduction mechanism of the full-length matrix protein 2 (M2) of influenza A virus. The M2 membrane protein can be separated into three domains: an N-terminal ectodomain (1-2 1), an cc-helical transmembrane domain (TM) (22-46) connected to an amphipathic helix (AH) and a Cterminal cytoplasmic tail (63-97). The TM domain of M2 is responsible for proton conduction ant the ectodomain has been the target for vaccine development. The cytoplasmic tail has been implicated in M2 interaction with other viral proteins from mutagenesis studies. Given the importance of both N- and C-termini, it is essential to determine the structure and the dynamics of M2FL. Furthermore, we are interested in how the cytoplasmic tail affects proton conduction and the interaction of the anti-viral drug amantadine with M2 in the presence of the C-terminus. Using uniformly ¹³C, ¹⁵N-labeled M2FL, our water-selected 2D ¹³C-¹³C correlation experiment indicated that N- and C- termini are on the surface of the lipid bilayer moreover combining with chemical shift prediction, we determined that these two domains are mostly disordered. Deleting the ectodomain of M2FL (M2(21-97)) proved that a small [beta]-strand is located at the N-terminus only in the DMPC-bound state. The M2 conformation is found to be cholesterol-dependent since [beta]-strand is not found in cholesterol-rich membranes. M2(21-97) shows cationic histidine at higher pH, in contrast to M2TM, indicating that the cytoplasmic tail shifts the His37 pKa equilibria. Quantification of the ¹⁵N intensities revealed two pKa's as opposed to of four in M2TM suggesting cooperative proton binding. A possible explanation is that the large number of positively charged residues in the cytoplasmic tail facilitates proton conduction. The cytoplasmic tail was also found to restore drug-binding as amantadine no longer binds to M2(21-61) a in virus-mimetic membrane. These results have extended our understanding of the influence of the cytoplasmic domain on the structure and proton conduction of M2.
by Shu-Yu Liao.
Ph. D.
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Suharni. "Proteoliposome-based selection of a recombinant antibody fragment against the human M2 muscarinic acetylcholine receptor." Kyoto University, 2015. http://hdl.handle.net/2433/195961.

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Karlsson, Susann. "T-Cell Protein Tyrosine Phosphatase, a Regulator of the PDGF Signaling Pathway." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-107674.

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Andreas, Loren B. "Structure and function of the Influenza membrane protein M2 by magic angle spinning NMR and dynamic nuclear polarization." Thesis, Massachusetts Institute of Technology, 2014. http://hdl.handle.net/1721.1/87466.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Chemistry, 2014.
Cataloged from PDF version of thesis. Vita.
Includes bibliographical references.
Determination of the 3D structure of membrane proteins is a frontier that is rapidly being explored due to the importance of membrane proteins in regulating cellular processes and because they are the target of many drugs. In addition, measuring and understanding how these proteins interact with ligands and other molecules is of critical importance to the design of the next generation of therapeutic agents. With this motivation, we report new methods for the structural characterization of proteins using magic angle spinning (MAS) nuclear magnetic resonance (NMR) applied to the membrane protein M2 from Influenza A, a small helical transmembrane proton transporter that is the target of adamantane based inhibitors but which is now drug resistant due primarily to the point mutation S31N. The development of techniques that boost the sensitivity of NMR are key to its extension to larger molecules such as membrane proteins, and two such methods, dynamic nuclear polarization (DNP) and proton detection, are applied herein. We report the measurement of the distance between the amine of the inhibitor rimantadine and the pore of M2 using DNP. We have applied recoupling techniques to assign the spectra and measure internuclear distances in the drug resistant S31N mutant of M2 in lipid bilayers. Attenuation of strong proton dipole couplings with 60 kHz spinning has allowed us to detect well-resolved proton spectra, and with the higher receptivity of protons, we measured interhelical distances with a methyl-methyl 4D spectrum. Synthesis of the information resulted in a high resolution structure of S3 IN M2.
by Loren B. Andreas.
Ph. D.
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Books on the topic "M2 protein"

1

Mosser, Valerie A. Expression and G protein coupling of the M2 muscarinic acetylcholine receptor in Sf9 insect cells. 1999.

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Badimon, Lina, and Gemma Vilahur. Atherosclerosis and thrombosis. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199687039.003.0040_update_001.

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Atherosclerosis is the main underlying cause of heart disease. The continuous exposure to cardiovascular risk factors induces endothelial activation/dysfunction which enhances the permeability of the endothelial layer and the expression of cytokines/chemokines and adhesion molecules. This results in the accumulation of lipids (low-density lipoprotein particles) in the intimal layer and the triggering of an inflammatory response. Accumulated low-density lipoprotein particles attached to the extracellular matrix suffer modifications and become pro-atherogenic, enhancing leucocyte recruitment and further transmigration across the endothelium into the intima. Infiltrated pro-atherogenic monocytes (mainly Mon2) differentiate into macrophages which acquire a specialized phenotypic polarization (protective/M1 or harmful/M2), depending on the stage of the atherosclerosis progression. Once differentiated, macrophages upregulate pattern recognition receptors capable of engulfing modified low-density lipoprotein, leading to foam cell formation. Foam cells release growth factors and cytokines that promote vascular smooth muscle cell migration into the intima, which then internalize low-density lipoproteins via low-density lipoprotein receptor-related protein-1 receptors becoming foam cells. As the plaque evolves, the number of vascular smooth muscle cells decline, whereas the presence of fragile/haemorrhagic neovessels and calcium deposits increases, promoting plaque destabilization. Disruption of this atherosclerotic lesion exposes thrombogenic surfaces rich in tissue factor that initiate platelet adhesion, activation, and aggregation, as well as thrombin generation. Platelets also participate in leucocyte and progenitor cell recruitment are likely to mediate atherosclerosis progression. Recent data attribute to microparticles a modulatory effect in the overall atherothrombotic process and evidence their potential use as systemic biomarkers of thrombus growth. This chapter reviews our current understanding of the pathophysiological mechanisms involved in atherogenesis, highlights platelet contribution to thrombosis and atherosclerosis progression, and provides new insights into how atherothrombosis may be prevented and modulated.
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Badimon, Lina, and Gemma Vilahur. Atherosclerosis and thrombosis. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199687039.003.0040_update_002.

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Atherosclerosis is the main underlying cause of heart disease. The continuous exposure to cardiovascular risk factors induces endothelial activation/dysfunction which enhances the permeability of the endothelial layer and the expression of cytokines/chemokines and adhesion molecules. This results in the accumulation of lipids (low-density lipoprotein particles) in the intimal layer and the triggering of an inflammatory response. Accumulated low-density lipoprotein particles attached to the extracellular matrix suffer modifications and become pro-atherogenic, enhancing leucocyte recruitment and further transmigration across the endothelium into the intima. Infiltrated pro-atherogenic monocytes (mainly Mon2) differentiate into macrophages which acquire a specialized phenotypic polarization (protective/M1 or harmful/M2), depending on the stage of the atherosclerosis progression. Once differentiated, macrophages upregulate pattern recognition receptors capable of engulfing modified low-density lipoprotein, leading to foam cell formation. Foam cells release growth factors and cytokines that promote vascular smooth muscle cell migration into the intima, which then internalize low-density lipoproteins via low-density lipoprotein receptor-related protein-1 receptors becoming foam cells. As the plaque evolves, the number of vascular smooth muscle cells decline, whereas the presence of fragile/haemorrhagic neovessels and calcium deposits increases, promoting plaque destabilization. Disruption of this atherosclerotic lesion exposes thrombogenic surfaces rich in tissue factor that initiate platelet adhesion, activation, and aggregation, as well as thrombin generation. Platelets also participate in leucocyte and progenitor cell recruitment are likely to mediate atherosclerosis progression. Recent data attribute to microparticles a modulatory effect in the overall atherothrombotic process and evidence their potential use as systemic biomarkers of thrombus growth. This chapter reviews our current understanding of the pathophysiological mechanisms involved in atherogenesis, highlights platelet contribution to thrombosis and atherosclerosis progression, and provides new insights into how atherothrombosis may be prevented and modulated.
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Book chapters on the topic "M2 protein"

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Muniyandi, Selvaraj, Georgia Pangratiou, Thomas A. Edwards, and John N. Barr. "Structure and Function of the Human Respiratory Syncytial Virus M2–1 Protein." In Subcellular Biochemistry, 245–60. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-8456-0_11.

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Jardon, Eduardo V., Peter J. Bond, and Martin B. Ulmschneider. "Ab Initio Folding of Glycophorin A and Acetylcholine M2 Transmembrane Segments Via Simplified Environment Molecular Simulations." In Physical Biology of Proteins and Peptides, 115–39. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-21687-4_7.

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Gerace, Erica, and Danesh Moazed. "Affinity Pull-Down of Proteins Using Anti-FLAG M2 Agarose Beads." In Laboratory Methods in Enzymology: Protein Part D, 99–110. Elsevier, 2015. http://dx.doi.org/10.1016/bs.mie.2014.11.010.

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Badimon, Lina, and Gemma Vilahur. "Atherosclerosis and thrombosis." In The ESC Textbook of Intensive and Acute Cardiovascular Care, edited by Marco Tubaro, Pascal Vranckx, Eric Bonnefoy-Cudraz, Susanna Price, and Christiaan Vrints, 447–62. Oxford University Press, 2021. http://dx.doi.org/10.1093/med/9780198849346.003.0037.

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Atherosclerosis is the main underlying cause of heart disease. The continuous exposure to cardiovascular risk factors induces endothelial activation/dysfunction which enhances the permeability of the endothelial layer and the expression of cytokines/chemokines and adhesion molecules. This results in the accumulation of lipids (low-density lipoprotein particles) in the intimal layer and the triggering of an inflammatory response. Accumulated low-density lipoprotein particles attached to the extracellular matrix suffer modifications and become pro-atherogenic, enhancing leucocyte recruitment and further transmigration across the endothelium into the intima. Infiltrated pro-atherogenic monocytes (mainly Mon2) differentiate into macrophages which acquire a specialized phenotypic polarization (protective/M1 or harmful/M2), depending on the stage of the atherosclerosis progression. Once differentiated, macrophages upregulate pattern recognition receptors capable of engulfing modified low-density lipoprotein, leading to foam cell formation. Foam cells release growth factors and cytokines that promote vascular smooth muscle cell migration into the intima, which then internalize low-density lipoproteins via low-density lipoprotein receptor-related protein-1 receptors becoming foam cells. As the plaque evolves, the number of vascular smooth muscle cells decline, whereas the presence of fragile/haemorrhagic neovessels and calcium deposits increases, promoting plaque destabilization. Disruption of this atherosclerotic lesion exposes thrombogenic surfaces rich in tissue factor that initiate platelet adhesion, activation, and aggregation, as well as thrombin generation. Platelets also participate in leucocyte and progenitor cell recruitment are likely to mediate atherosclerosis progression. Recent data attribute to extracellular vesicles (mainly microvesicles) a role in all stages of atherosclerosis development and evidence their potential use as systemic biomarkers of thrombus growth. This chapter reviews our current understanding of the pathophysiological mechanisms involved in atherogenesis, highlights platelet contribution to thrombosis and atherosclerosis progression, and provides new insights into how atherothrombosis may be prevented and modulated.
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"Mitigating Impacts of Natural Hazards on Fishery Ecosystems." In Mitigating Impacts of Natural Hazards on Fishery Ecosystems, edited by LaDon Swann. American Fisheries Society, 2008. http://dx.doi.org/10.47886/9781934874011.ch4.

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<em>Abstract</em>.—Gulf of Mexico marshes have been found to support more than 80 species of fish, 60 species of birds, and many reptile, mammal, and invertebrate species (Stout 1984). In addition to the ecological services provided by salt marshes, the 2005 hurricanes in the Gulf of Mexico raised public awareness of the ability of intertidal marshes to reduce personal property damage from storm surges. Since marshes can be destroyed through natural or anthropogenic processes, methods to protect these areas are being developed; one such method is the use of “living shorelines.” Living shorelines serve multiple roles by controlling erosion, maintaining natural coastal processes, and sustaining biodiversity through land-use management, soft armoring, or combinations of soft and semihard armoring techniques. Living shorelines provide a viable alternative to common hardened structures such as bulkheads, stone revetments, and seawalls. One type of living shoreline was used at Saw Grass Point Salt Marsh on Dauphin Island, Alabama. Dauphin Island’s Fort Gaines Harbor was constructed in the 1950s by removing approximately 3 ha from Saw Grass Point Salt Marsh. The harbor now serves as one of Dauphin Island’s two primary access points for recreational and commercial boats to the Gulf of Mexico. Chronic erosion has resulted in the loss of 0.5 ha of the remaining marsh. This saline tidal marsh is of significant ecological importance and is one of only two on Dauphin Island. In 2004, a community-based restoration grant was used to protect and restore the marsh through the use of exposed nearshore precast concrete breakwaters called Coastal Havens. These structures function as detached breakwaters to minimize the effect of storm surge and boat wake through wave attenuation; they also provide suitable substrate for oyster colonization. These structures were selected over other erosion control technologies, including vertical bulkheads, rock or wooden sills, and headlands. In April 2005, 182 units were installed in two interlocking rows parallel to the east perimeter of the marsh in water approximately 1.3 m deep. Oyster density on the coastal havens, measured 19 months postinstallation, was 205 oysters/m2. Measurements behind the breakwater indicate some sediment accretion. The project cost was approximately US$335/m to protect 162 m of shoreline. The dual function of these structures has controlled the erosion behind the breakwater and has provided habitat for a wide array of National Oceanic and Atmospheric Administration trust resources, including locally important species such as spotted seatrout (also known as speckled trout) <em>Cynoscion nebulosus</em>, blue crabs <em>Callinectes sapidus </em>and Gulf stone crabs <em>Menippe adina</em>, eastern oyster <em>Crassostrea virginica</em>, red drum <em>Sciaenops ocellatus</em>, southern flounder <em>Paralichthys lethostigma</em>, and various species of commercially important shrimp (brown shrimp <em>Farfantepenaeus aztecus</em>, pink shrimp <em>F. duorarum</em>, and white shrimp <em>Litopenaeus setiferus</em>).
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Conference papers on the topic "M2 protein"

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"An effective molecular blockers of ion channel of M2 protein as anti-influenza A drug." In Bioinformatics of Genome Regulation and Structure/ Systems Biology. institute of cytology and genetics siberian branch of the russian academy of science, Novosibirsk State University, 2020. http://dx.doi.org/10.18699/bgrs/sb-2020-387.

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Wang, W., Y. Guo, H. Xing, and G. Tai. "Abstract P6-09-04: M2 macrophages induced by mammary carcinoma are switched to M1 macrophages by Escherichia coli maltose-binding protein." In Abstracts: Thirty-Sixth Annual CTRC-AACR San Antonio Breast Cancer Symposium - Dec 10-14, 2013; San Antonio, TX. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/0008-5472.sabcs13-p6-09-04.

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Fukui, S., N. Iwamoto, R. Masuyama, K. Kosai, K. Yanagihara, and A. Kawakami. "FRI0017 A novel concept of M1 and M2 monocytes in rheumatoid arthritis: pro-inflammatory monocyte polarization imbalance, anti-citrullinated protein antibody and osteoclastogenesis." In Annual European Congress of Rheumatology, 14–17 June, 2017. BMJ Publishing Group Ltd and European League Against Rheumatism, 2017. http://dx.doi.org/10.1136/annrheumdis-2017-eular.2083.

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Ding, Q., M. Wang, R. Hu, A. B. B. Carter, and P. Che. "Zinc Finger Protein 36 Homolog Regulates Pro-Fibrotic Responses and Lung Fibrosis Through Lysyl Oxidase Like 2 and Pyruvate Kinase Muscle Isozyme M2." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a2259.

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SPRUOGIS, Vidmantas, Anželika DAUTARTĖ, Romualdas ZEMECKIS, Edmundas BARTKEVIČIUS, and Aida STIKLIENĖ. "THE INFLUENCE OF BIOORGANIC PREPARATIONS ON THE PRODUCTIVITY OF CONVENTIONALY GROWN WINTER WHEAT ACTIVATING AND SAVING THE USE OF SYNTHETIC CHEMICALS." In RURAL DEVELOPMENT. Aleksandras Stulginskis University, 2018. http://dx.doi.org/10.15544/rd.2017.080.

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The influence of Raskila bioorganic fertilisers on the productivity of conventional winter wheat ‘Olivin’, was investigated in order to stimulate and save synthetic herbicide Arrat and fungicide Tango Super for spring spraying. Scheme of treatment: 1. Control; 2. Winter wheat sprayed (BBCH 20-29) with fertilizer Raskila 3 l ha-1; 3. Winter wheat sprayed (BBCH 20-29) with Arrat 0.2 kg ha-1+Tango super 1.5 l ha-1; 4. Winter wheat sprayed (BBCH 20-29) with Arrat 0.2 kg ha-1+Tango super 1.5 l ha-1+Raskila 3.0 l ha-1; 5. Winter wheat sprayed (BBCH 20-29) with Arrat 0.1 kg ha-1+Tango super 0.75 l ha-1+Raskila 3.0 l ha-1. The best result in the period of 2014-2016 was received after application of the following combination in spring: Arrat + Tango super + Raskila. This combination allows to reduce the rate of pesticides in half (50%), the differences compared to control are significant, statistically reliable. A statistically significant increase in the following winter wheat ‘Olivin’ quality parameters was found: protein 13.1-14.8%, gluten 24.3-29.7%, number of falls 228-292 s, starch 65.7-70.0%. Application of Raskila fertilizers has raised the grain quality class. The best results were in variants 3 and 4, where the I class of grain quality was achieved. Combination of Raskila fertilisers and pesticides: herbicide Arrat and fungicide Tango super statistically significantly increased the following winter wheat ‘Olivin’ characteristics - plant height 101.2-104.2 cm, ear length 6.9-7.1 cm, grain number per ear 28,96- 30.02, grain yield 6.71-7.03 t ha-1. Application of Raskila fertilizer 1.0 l ha-1 and herbicide Arrat 0.1 kg ha-1 decreased the number of weeds from 62.5 to 57.6 units per m2 and the weed weight decreased from 41.30 to 33.70 g m2. Stronger wheat crop overshadowed weeds better. Combination of Raskila and Tango super reduced the prevalence and severity of diseases in winter wheat such as Septoria spp., Pyrenophora tritici-repentis, Erysiphe graminis, powdery rust (Puccinia recondita).
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WAJIMA, T. "THROMBOCYTOPENIA IN ACQUIRED IMMUNE DEFICIENCY SYNDRGME(AIDS)-RELATED COMPLEXES:RESOLUTION DURING HERPES VIRAL INFECTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644145.

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Immune thrombocytopenia has been recognized as a major hematologic manifestation associated with the acquired immune deficiency syndrome(AIDS) and AIDS-related complexes. The mechanism of thrombocytopenia in human immune deficiency virus infection is probably multifactorial.. The role of platelet-associated immuno-globulin(PAIgG)and circulating immune complexes(CIC) in mediating thrombocytopenia is controversial.. We experienced a case in which immune thrombocytopenia in AIDS-related complexes resolved during herpes zoster infection. A 37 y.o. white homosexual male with AIDS-related complexes and thrombocytopenia presented a 4-day history of painful, violaceous, non-pruritic vesicles which started on the right arm and hand, which then progressed to the chest wall, abdomen, back, and left arm. Peripheral lymphadenop-athy and splenomegaly was not noted. On admission WBG 13.5 Hct 40.8, platelet 46,000, Tzanck smear of vesicles revealed herpetic type giant cells. HTLV-III pos., Helper/suppressor T-cell ratio 0.3, Total protein 7.9 gm%, . Alb 3.95gm% IgG 1740 mg%, IgA 157 mg IgM 91.2 mg, Monospot neg., HBsAg Neg., HBsAb pos., HBcAb pos., VDRL neg. Before this admission, immune thrombocytopenia was documented by increased levels of PAIgG, CIC, bone marrow magakaryocytic hyperplasia, peripheral thrombocytopenia with giant platelets, absence of splenomegaly, and response to prednisone. He was treated with Acyclovir 250 mg/m2 1-hr infusion Q8h for 9 days ;to control the spread of his herpes infection. Recovery of thrombocytopenia wasobserved during herpes zo.ster infection. The platelet count rose to 158,000 and sustained over 4- weeks. Duringnormalization of platelet count thelevel of GIC (assayed by Raji cells, reference ranges, less than 12) droppedfrom 300 to less than 12 and PAIgG(fluorescence-activated flow cytometric assay, reference ranges, less than 1.5 RF) was markedly decreased from 90 to 2.9 When herpes infection had subsided the platelet count again decreased. These findings suggestthat PAIgG and GIG were contributing factors to immune thrombocytopenia and that herpes viral infection and Acyclovir altered this immunologically mediated thrombocytopenia in AIDS-related complexes.
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Jubery, Talukder Zaki, Anmiv S. Prabhu, Min Jun Kim, and Prashanta Dutta. "Modeling and Simulation of Translocation Phenomenon in a Solid State Nanopore for Nanoparticle Separation." In ASME 2010 International Mechanical Engineering Congress and Exposition. ASMEDC, 2010. http://dx.doi.org/10.1115/imece2010-38742.

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Solid state nanopore is a potential candidate for separation of nanoparticles or biomolecules such as proteins, DNA, and RNA. However, efficient separation of particles through nanopores is a challenging task as a number of factors such as externally applied voltage, size and charge density of particle, size and charge density of membrane pore, and the concentration of bulk electrolyte influence the translocation behavior of nanoparticles through pores. This paper uses a mathematical model based on Poisson–Nernst–Plank equations along with Navier-Stokes equations to systematically study these factors. Membrane pore surface charge is found to be a vital parameter in this seperation process. Numerical results reveal that efficient separation of high density lipoprotein (HDL) from low density lipoprotein (LDL) in a 0.2 M KCL solution (resembling blood buffer) through a 150 nm pore is possible if the pore surface charge density is around −4.0 mC/m2.
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Li, Yongqiang, Jennifer Quincy, Scott W. Case, David A. Dillard, Michael Budinski, and Yeh-Hung Lai. "Using a Knife Slitting Test to Characterize the Fracture Resistance of Proton Exchange Membranes." In ASME 2006 4th International Conference on Fuel Cell Science, Engineering and Technology. ASMEDC, 2006. http://dx.doi.org/10.1115/fuelcell2006-97096.

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Through-the-thickness flaws or “pinholes” in proton exchange membranes (PEM) can lead to gas crossover, reducing fuel cell efficiency, accelerating degradation, and raising safety issues. The multi-physics process that causes these flaws is not fully understood, but stress state, environmental exposure, and cyclic operation may all be contributing factors. Fracture mechanics has proven to be useful in characterizing degradation of many materials, including polymers subjected to environmental challenges. Although unclear if pinhole formation can be successfully characterized and predicted from a fracture perspective, this study continues our prior work to characterize PEMs in such a manner. Because of the lack of constraint, thin films often exhibit very high fracture energies and large plastic zones, features that are not consistent with observations of PEM failures. In an effort to obtain the fracture energy with very little dissipation, knife-slitting tests were conducted to reduce the crack tip plasticity. With modifications made to the systems used by Wang and Gent (1994) and by Dillard et al (2005), a slitter that maintains a constant tearing angle during the slitting process was developed. While fracture energies on the order of 104J/m2 were measured with double edge notched test samples, and on the order of 103J/m2 were measured with trouser tear samples, the knife slit test resulted in fracture energies as low as several hundred J/m2. An environmental chamber was used to enclose the slitting process so experiments at elevated temperature and moisture levels could be conducted. The relevance of these fracture energies to observed PEM failures in operating fuel cells is not fully understood. Nonetheless, the ability to obtain fracture energies approaching the intrinsic fracture energy of these ductile membranes is believed to be useful in studying what appear to be more brittle fracture modes that have been observed in PEMs.
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LaManna, Jacob, and Satish G. Kandlikar. "Investigation of Water Vapor Diffusivity Through GDL of a PEMFC." In ASME 2009 International Mechanical Engineering Congress and Exposition. ASMEDC, 2009. http://dx.doi.org/10.1115/imece2009-11425.

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Water transport through the gas diffusion layer (GDL) of a proton exchange membrane (PEM) fuel cell is of critical importance in the operation of the fuel cell. In this study, the transport of water vapor through the GDL is investigated. A one-dimensional, single-phase heat and mass transfer model is developed to investigate the diffusivity of water vapor through the GDL of a PEMFC. An experimental apparatus is developed to induce water vapor gradients across the GDL while varying humidity levels and flow rates comparable to actual fuel cell operational conditions. Experimental data is then used to extract an effective water vapor diffusivity from the numerical model. Effective diffusivity was found to be 0.104×10−4 m2/s and the overall mass transfer coefficient was found to be 0.019 m/s at a temperature of 40°C.
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Tabuchi, Yuichiro, and Norio Kubo. "The Impact of Rib/Channel, Water and Heat Transport on Limiting Current Density." In ASME 2008 6th International Conference on Fuel Cell Science, Engineering and Technology. ASMEDC, 2008. http://dx.doi.org/10.1115/fuelcell2008-65201.

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Proton exchange membrane fuel cells (PEMFCs) are regarded as a promising alternative clean power source for automotive applications. Key to the acceptance of PEMFCs for automobiles are cost reduction and power density for compactness. In order to meet these requirements, further improvement of cell performance is required. In particular, under higher current density operation, water and heat transport in PEMFC have strong effects on cell performance. In this study, the impact of Rib/Channel dimensions, heat and water transport on cell performance under high current density is investigated using the multiphase mixture model (M2 model), and the limiting current density is evaluated using a uniform test cell with 10cm2 active area and 24 straight channels. Limiting current densities were measured under different oxygen concentrations at 70°C and 70% relative humidity at both sides. In order to neglect the effect of liquid water in channels and the distribution of oxygen and hydrogen concentrations along the flow channel, large flow rates were introduced at both sides. Experimental results show a nonlinear relation between oxygen concentration in the channel and limiting current density. Numerically it is found that this nonlinear trend is caused by liquid water in the Rib region. In addition, it is also found that not only liquid water, but also heat transport and water transport through the membrane significantly affect the limiting current density. Finally, it is concluded that the combination analysis using limiting current experiments of uniform cell system and M2 model is very useful for fundamental understanding and for fuel cell design optimization.
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