753 research outputs found

    Co3O4 Nanocrystals on Graphene as a Synergistic Catalyst for Oxygen Reduction Reaction

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    Catalysts for oxygen reduction and evolution reactions are at the heart of key renewable energy technologies including fuel cells and water splitting. Despite tremendous efforts, developing oxygen electrode catalysts with high activity at low costs remains a grand challenge. Here, we report a hybrid material of Co3O4 nanocrystals grown on reduced graphene oxide (GO) as a high-performance bi-functional catalyst for oxygen reduction reaction (ORR) and oxygen evolution reaction (OER). While Co3O4 or graphene oxide alone has little catalytic activity, their hybrid exhibits an unexpected, surprisingly high ORR activity that is further enhanced by nitrogen-doping of graphene. The Co3O4/N-doped graphene hybrid exhibits similar catalytic activity but superior stability to Pt in alkaline solutions. The same hybrid is also highly active for OER, making it a high performance non-precious metal based bi-catalyst for both ORR and OER. The unusual catalytic activity arises from synergetic chemical coupling effects between Co3O4 and graphene.Comment: published in Nature Material

    A search for the decay modes B+/- to h+/- tau l

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    We present a search for the lepton flavor violating decay modes B+/- to h+/- tau l (h= K,pi; l= e,mu) using the BaBar data sample, which corresponds to 472 million BBbar pairs. The search uses events where one B meson is fully reconstructed in one of several hadronic final states. Using the momenta of the reconstructed B, h, and l candidates, we are able to fully determine the tau four-momentum. The resulting tau candidate mass is our main discriminant against combinatorial background. We see no evidence for B+/- to h+/- tau l decays and set a 90% confidence level upper limit on each branching fraction at the level of a few times 10^-5.Comment: 15 pages, 7 figures, submitted to Phys. Rev.

    Evidence for an excess of B -> D(*) Tau Nu decays

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    Based on the full BaBar data sample, we report improved measurements of the ratios R(D(*)) = B(B -> D(*) Tau Nu)/B(B -> D(*) l Nu), where l is either e or mu. These ratios are sensitive to new physics contributions in the form of a charged Higgs boson. We measure R(D) = 0.440 +- 0.058 +- 0.042 and R(D*) = 0.332 +- 0.024 +- 0.018, which exceed the Standard Model expectations by 2.0 sigma and 2.7 sigma, respectively. Taken together, our results disagree with these expectations at the 3.4 sigma level. This excess cannot be explained by a charged Higgs boson in the type II two-Higgs-doublet model. We also report the observation of the decay B -> D Tau Nu, with a significance of 6.8 sigma.Comment: Expanded section on systematics, text corrections, improved the format of Figure 2 and included the effect of the change of the Tau polarization due to the charged Higg

    Search for the decay modes D^0 → e^+e^-, D^0 → ÎŒ^+ÎŒ^-, and D^0 → e^±Ό∓

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    We present searches for the rare decay modes D^0→e^+e^-, D^0→Ό^+ÎŒ^-, and D^0→e^±Ό^∓ in continuum e^+e^-→cc events recorded by the BABAR detector in a data sample that corresponds to an integrated luminosity of 468  fb^(-1). These decays are highly Glashow–Iliopoulos–Maiani suppressed but may be enhanced in several extensions of the standard model. Our observed event yields are consistent with the expected backgrounds. An excess is seen in the D^0→Ό^+ÎŒ^- channel, although the observed yield is consistent with an upward background fluctuation at the 5% level. Using the Feldman–Cousins method, we set the following 90% confidence level intervals on the branching fractions: B(D^0→e^+e^-)<1.7×10^(-7), B(D^0→Ό^+ÎŒ^-) within [0.6,8.1]×10^(-7), and B(D^0→e^±Ό^∓)<3.3×10^(-7)

    Study of the reaction e^{+}e^{-} -->J/psi\pi^{+}\pi^{-} via initial-state radiation at BaBar

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    We study the process e+e−→J/ψπ+π−e^+e^-\to J/\psi\pi^{+}\pi^{-} with initial-state-radiation events produced at the PEP-II asymmetric-energy collider. The data were recorded with the BaBar detector at center-of-mass energies 10.58 and 10.54 GeV, and correspond to an integrated luminosity of 454 fb−1\mathrm{fb^{-1}}. We investigate the J/ψπ+π−J/\psi \pi^{+}\pi^{-} mass distribution in the region from 3.5 to 5.5 GeV/c2\mathrm{GeV/c^{2}}. Below 3.7 GeV/c2\mathrm{GeV/c^{2}} the ψ(2S)\psi(2S) signal dominates, and above 4 GeV/c2\mathrm{GeV/c^{2}} there is a significant peak due to the Y(4260). A fit to the data in the range 3.74 -- 5.50 GeV/c2\mathrm{GeV/c^{2}} yields a mass value 4244±54244 \pm 5 (stat) ±4 \pm 4 (syst)MeV/c2\mathrm{MeV/c^{2}} and a width value 114−15+16114 ^{+16}_{-15} (stat)±7 \pm 7(syst)MeV\mathrm{MeV} for this state. We do not confirm the report from the Belle collaboration of a broad structure at 4.01 GeV/c2\mathrm{GeV/c^{2}}. In addition, we investigate the π+π−\pi^{+}\pi^{-} system which results from Y(4260) decay

    Observation and study of baryonic B decays: B -> D(*) p pbar, D(*) p pbar pi, and D(*) p pbar pi pi

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    We present a study of ten B-meson decays to a D(*), a proton-antiproton pair, and a system of up to two pions using BaBar's data set of 455x10^6 BBbar pairs. Four of the modes (B0bar -> D0 p anti-p, B0bar -> D*0 p anti-p, B0bar -> D+ p anti-p pi-, B0bar -> D*+ p anti-p pi-) are studied with improved statistics compared to previous measurements; six of the modes (B- -> D0 p anti-p pi-, B- -> D*0 p anti-p pi-, B0bar -> D0 p anti-p pi- pi+, B0bar -> D*0 p anti-p pi- pi+, B- -> D+ p anti-p pi- pi-, B- -> D*+ p anti-p pi- pi-) are first observations. The branching fractions for 3- and 5-body decays are suppressed compared to 4-body decays. Kinematic distributions for 3-body decays show non-overlapping threshold enhancements in m(p anti-p) and m(D(*)0 p) in the Dalitz plots. For 4-body decays, m(p pi-) mass projections show a narrow peak with mass and full width of (1497.4 +- 3.0 +- 0.9) MeV/c2, and (47 +- 12 +- 4) MeV/c2, respectively, where the first (second) errors are statistical (systematic). For 5-body decays, mass projections are similar to phase space expectations. All results are preliminary.Comment: 28 pages, 90 postscript figures, submitted to LP0

    Search for rare quark-annihilation decays, B --> Ds(*) Phi

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    We report on searches for B- --> Ds- Phi and B- --> Ds*- Phi. In the context of the Standard Model, these decays are expected to be highly suppressed since they proceed through annihilation of the b and u-bar quarks in the B- meson. Our results are based on 234 million Upsilon(4S) --> B Bbar decays collected with the BABAR detector at SLAC. We find no evidence for these decays, and we set Bayesian 90% confidence level upper limits on the branching fractions BF(B- --> Ds- Phi) Ds*- Phi)<1.2x10^(-5). These results are consistent with Standard Model expectations.Comment: 8 pages, 3 postscript figues, submitted to Phys. Rev. D (Rapid Communications

    Evidence for the h_b(1P) meson in the decay Upsilon(3S) --> pi0 h_b(1P)

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    Using a sample of 122 million Upsilon(3S) events recorded with the BaBar detector at the PEP-II asymmetric-energy e+e- collider at SLAC, we search for the hb(1P)h_b(1P) spin-singlet partner of the P-wave chi_{bJ}(1P) states in the sequential decay Upsilon(3S) --> pi0 h_b(1P), h_b(1P) --> gamma eta_b(1S). We observe an excess of events above background in the distribution of the recoil mass against the pi0 at mass 9902 +/- 4(stat.) +/- 2(syst.) MeV/c^2. The width of the observed signal is consistent with experimental resolution, and its significance is 3.1sigma, including systematic uncertainties. We obtain the value (4.3 +/- 1.1(stat.) +/- 0.9(syst.)) x 10^{-4} for the product branching fraction BF(Upsilon(3S)-->pi0 h_b) x BF(h_b-->gamma eta_b).Comment: 8 pages, 4 postscript figures, submitted to Phys. Rev. D (Rapid Communications

    Involvement of the exomer complex in the polarized transport of Ena1 required for Saccharomyces cerevisiae survival against toxic cations

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    [EN] Exomer is an adaptor complex required for the direct transport of a selected number of cargoes from the trans-Golgi network (TGN) to the plasma membrane in Saccharomyces cerevisiae However, exomer mutants are highly sensitive to increased concentrations of alkali metal cations, a situation that remains unexplained by the lack of transport of any known cargoes. Here we identify several HAL genes that act as multicopy suppressors of this sensitivity and are connected to the reduced function of the sodium ATPase Ena1. Furthermore, we find that Ena1 is dependent on exomer function. Even though Ena1 can reach the plasma membrane independently of exomer, polarized delivery of Ena1 to the bud requires functional exomer. Moreover, exomer is required for full induction of Ena1 expression after cationic stress by facilitating the plasma membrane recruitment of the molecular machinery involved in Rim101 processing and activation of the RIM101 pathway in response to stress. Both the defective localization and the reduced levels of Ena1 contribute to the sensitivity of exomer mutants to alkali metal cations. Our work thus expands the spectrum of exomer-dependent proteins and provides a link to a more general role of exomer in TGN organization.We acknowledge Emma Keck for English language revision. We also thank members of the Translucent group, J. Arino, J. Ramos, and L. Yenush, for many useful discussions throughout this work and especially L. Yenush for her generous gift of strains and reagents. The help of O. Vincent was essential for developing the work involving RIM101. We also thank R. Valle for her technical assistance at the CR Laboratory. M. Trautwein is acknowledged for data acquisition and discussions during the early stages of the project. C.A. is supported by a USAL predoctoral fellowship. Work at the Spang laboratory was supported by the University of Basel and the Swiss National Science Foundation (31003A-141207 and 310030B-163480). C.R. was supported by grant SA073U14 from the Regional Government of Castilla y Leon and by grant BFU2013-48582-C2-1-P from the CICYT/FEDER Spanish program. J.M.M. acknowledges the financial support from Universitat Politecnica de Valencia project PAID-06-10-1496.Anton, C.; Zanolari, B.; Arcones, I.; Wang, C.; Mulet, JM.; Spang, A.; Roncero, C. (2017). Involvement of the exomer complex in the polarized transport of Ena1 required for Saccharomyces cerevisiae survival against toxic cations. Molecular Biology of the Cell. 28(25):3672-3685. https://doi.org/10.1091/mbc.E17-09-0549S367236852825Ariño, J., Ramos, J., & Sychrová, H. (2010). Alkali Metal Cation Transport and Homeostasis in Yeasts. Microbiology and Molecular Biology Reviews, 74(1), 95-120. doi:10.1128/mmbr.00042-09Bard, F., & Malhotra, V. (2006). The Formation of TGN-to-Plasma-Membrane Transport Carriers. Annual Review of Cell and Developmental Biology, 22(1), 439-455. doi:10.1146/annurev.cellbio.21.012704.133126Barfield, R. M., Fromme, J. C., & Schekman, R. (2009). The Exomer Coat Complex Transports Fus1p to the Plasma Membrane via a Novel Plasma Membrane Sorting Signal in Yeast. Molecular Biology of the Cell, 20(23), 4985-4996. doi:10.1091/mbc.e09-04-0324Bonifacino, J. S. (2014). Adaptor proteins involved in polarized sorting. Journal of Cell Biology, 204(1), 7-17. doi:10.1083/jcb.201310021Bonifacino, J. S., & Glick, B. S. (2004). The Mechanisms of Vesicle Budding and Fusion. Cell, 116(2), 153-166. doi:10.1016/s0092-8674(03)01079-1Bonifacino, J. S., & Lippincott-Schwartz, J. (2003). Coat proteins: shaping membrane transport. Nature Reviews Molecular Cell Biology, 4(5), 409-414. doi:10.1038/nrm1099Carlson, M., & Botstein, D. (1982). Two differentially regulated mRNAs with different 5â€Č ends encode secreted and intracellular forms of yeast invertase. Cell, 28(1), 145-154. doi:10.1016/0092-8674(82)90384-1Costanzo, M., Baryshnikova, A., Bellay, J., Kim, Y., Spear, E. D., Sevier, C. S., 
 Mostafavi, S. (2010). The Genetic Landscape of a Cell. Science, 327(5964), 425-431. doi:10.1126/science.1180823De Matteis, M. A., & Luini, A. (2008). Exiting the Golgi complex. Nature Reviews Molecular Cell Biology, 9(4), 273-284. doi:10.1038/nrm2378De Nadal, E., Clotet, J., Posas, F., Serrano, R., Gomez, N., & Arino, J. (1998). The yeast halotolerance determinant Hal3p is an inhibitory subunit of the Ppz1p Ser/Thr protein phosphatase. Proceedings of the National Academy of Sciences, 95(13), 7357-7362. doi:10.1073/pnas.95.13.7357Drubin, D. G., & Nelson, W. J. (1996). Origins of Cell Polarity. Cell, 84(3), 335-344. doi:10.1016/s0092-8674(00)81278-7Fell, G. L., Munson, A. M., Croston, M. A., & Rosenwald, A. G. (2011). Identification of Yeast Genes Involved in K+Homeostasis: Loss of Membrane Traffic Genes Affects K+Uptake. G3&amp;#58; Genes|Genomes|Genetics, 1(1), 43-56. doi:10.1534/g3.111.000166Ferrando, A., Kron, S. J., Rios, G., Fink, G. R., & Serrano, R. (1995). Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3. Molecular and Cellular Biology, 15(10), 5470-5481. doi:10.1128/mcb.15.10.5470Forsmark, A., Rossi, G., Wadskog, I., Brennwald, P., Warringer, J., & Adler, L. (2011). Quantitative Proteomics of Yeast Post-Golgi Vesicles Reveals a Discriminating Role for Sro7p in Protein Secretion. Traffic, 12(6), 740-753. doi:10.1111/j.1600-0854.2011.01186.xGaber, R. F., Styles, C. A., & Fink, G. R. (1988). TRK1 encodes a plasma membrane protein required for high-affinity potassium transport in Saccharomyces cerevisiae. Molecular and Cellular Biology, 8(7), 2848-2859. doi:10.1128/mcb.8.7.2848Galindo, A., Calcagno-Pizarelli, A. M., Arst, H. N., & Penalva, M. A. (2012). An ordered pathway for the assembly of fungal ESCRT-containing ambient pH signalling complexes at the plasma membrane. Journal of Cell Science, 125(7), 1784-1795. doi:10.1242/jcs.098897Goldstein, A. L., & McCusker, J. H. (1999). Three new dominant drug resistance cassettes for gene disruption inSaccharomyces cerevisiae. Yeast, 15(14), 1541-1553. doi:10.1002/(sici)1097-0061(199910)15:143.0.co;2-kHayashi, M., Fukuzawa, T., Sorimachi, H., & Maeda, T. (2005). Constitutive Activation of the pH-Responsive Rim101 Pathway in Yeast Mutants Defective in Late Steps of the MVB/ESCRT Pathway. Molecular and Cellular Biology, 25(21), 9478-9490. doi:10.1128/mcb.25.21.9478-9490.2005Herrador, A., Herranz, S., Lara, D., & Vincent, O. (2009). Recruitment of the ESCRT Machinery to a Putative Seven-Transmembrane-Domain Receptor Is Mediated by an Arrestin-Related Protein. Molecular and Cellular Biology, 30(4), 897-907. doi:10.1128/mcb.00132-09Herrador, A., Livas, D., Soletto, L., Becuwe, M., LĂ©on, S., & Vincent, O. (2015). Casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge. Molecular Biology of the Cell, 26(11), 2128-2138. doi:10.1091/mbc.e14-11-1552Herranz, S., Rodriguez, J. M., Bussink, H.-J., Sanchez-Ferrero, J. C., Arst, H. N., Penalva, M. A., & Vincent, O. (2005). Arrestin-related proteins mediate pH signaling in fungi. Proceedings of the National Academy of Sciences, 102(34), 12141-12146. doi:10.1073/pnas.0504776102Hoya, M., Yanguas, F., Moro, S., Prescianotto-Baschong, C., Doncel, C., de LeĂłn, N., 
 Valdivieso, M.-H. (2016). Traffic Through theTrans-Golgi Network and the Endosomal System Requires Collaboration Between Exomer and Clathrin Adaptors in Fission Yeast. Genetics, 205(2), 673-690. doi:10.1534/genetics.116.193458Huranova, M., Muruganandam, G., Weiss, M., & Spang, A. (2016). Dynamic assembly of the exomer secretory vesicle cargo adaptor subunits. EMBO reports, 17(2), 202-219. doi:10.15252/embr.201540795Kung, L. F., Pagant, S., Futai, E., D’Arcangelo, J. G., Buchanan, R., Dittmar, J. C., 
 Miller, E. A. (2011). Sec24p and Sec16p cooperate to regulate the GTP cycle of the COPII coat. The EMBO Journal, 31(4), 1014-1027. doi:10.1038/emboj.2011.444Lamb, T. M., & Mitchell, A. P. (2003). The Transcription Factor Rim101p Governs Ion Tolerance and Cell Differentiation by Direct Repression of the Regulatory Genes NRG1 and SMP1 in Saccharomyces cerevisiae. Molecular and Cellular Biology, 23(2), 677-686. doi:10.1128/mcb.23.2.677-686.2003Lamb, T. M., Xu, W., Diamond, A., & Mitchell, A. P. (2000). Alkaline Response Genes ofSaccharomyces cerevisiaeand Their Relationship to theRIM101Pathway. Journal of Biological Chemistry, 276(3), 1850-1856. doi:10.1074/jbc.m008381200Madrid, R., GĂłmez, M. J., Ramos, J., & Rodrı́guez-Navarro, A. (1998). Ectopic Potassium Uptake intrk1 trk2Mutants ofSaccharomyces cerevisiaeCorrelates with a Highly Hyperpolarized Membrane Potential. Journal of Biological Chemistry, 273(24), 14838-14844. doi:10.1074/jbc.273.24.14838Maresova, L., & Sychrova, H. (2004). Physiological characterization of Saccharomyces cerevisiae kha1 deletion mutants. Molecular Microbiology, 55(2), 588-600. doi:10.1111/j.1365-2958.2004.04410.xMarquĂ©s, M. C., Zamarbide-ForĂ©s, S., Pedelini, L., Llopis-Torregrosa, V., & Yenush, L. (2015). A functional Rim101 complex is required for proper accumulation of the Ena1 Na+-ATPase protein in response to salt stress in Saccharomyces cerevisiae. FEMS Yeast Research, 15(4). doi:10.1093/femsyr/fov017Mulet, J. M., Leube, M. P., Kron, S. J., Rios, G., Fink, G. R., & Serrano, R. (1999). A Novel Mechanism of Ion Homeostasis and Salt Tolerance in Yeast: the Hal4 and Hal5 Protein Kinases Modulate the Trk1-Trk2 Potassium Transporter. Molecular and Cellular Biology, 19(5), 3328-3337. doi:10.1128/mcb.19.5.3328Mulet, J. M., & Serrano, R. (2002). Simultaneous determination of potassium and rubidium content in yeast. Yeast, 19(15), 1295-1298. doi:10.1002/yea.909MurguĂ­a, J. R., BellĂ©s, J. M., & Serrano, R. (1996). The YeastHAL2Nucleotidase Is anin VivoTarget of Salt Toxicity. Journal of Biological Chemistry, 271(46), 29029-29033. doi:10.1074/jbc.271.46.29029Obara, K., & Kihara, A. (2014). Signaling Events of the Rim101 Pathway Occur at the Plasma Membrane in a Ubiquitination-Dependent Manner. Molecular and Cellular Biology, 34(18), 3525-3534. doi:10.1128/mcb.00408-14Paczkowski, J. E., & Fromme, J. C. (2014). Structural Basis for Membrane Binding and Remodeling by the Exomer Secretory Vesicle Cargo Adaptor. Developmental Cell, 30(5), 610-624. doi:10.1016/j.devcel.2014.07.014Paczkowski, J. E., Richardson, B. C., & Fromme, J. C. (2015). Cargo adaptors: structures illuminate mechanisms regulating vesicle biogenesis. Trends in Cell Biology, 25(7), 408-416. doi:10.1016/j.tcb.2015.02.005Paczkowski, J. E., Richardson, B. C., Strassner, A. M., & Fromme, J. C. (2012). The exomer cargo adaptor structure reveals a novel GTPase-binding domain. The EMBO Journal, 31(21), 4191-4203. doi:10.1038/emboj.2012.268Parsons, A. B., Brost, R. L., Ding, H., Li, Z., Zhang, C., Sheikh, B., 
 Boone, C. (2003). Integration of chemical-genetic and genetic interaction data links bioactive compounds to cellular target pathways. Nature Biotechnology, 22(1), 62-69. doi:10.1038/nbt919Peñalva, M. A., Lucena-Agell, D., & Arst, H. N. (2014). Liaison alcaline: Pals entice non-endosomal ESCRTs to the plasma membrane for pH signaling. Current Opinion in Microbiology, 22, 49-59. doi:10.1016/j.mib.2014.09.005RĂ­os, G., Cabedo, M., Rull, B., Yenush, L., Serrano, R., & Mulet, J. M. (2013). Role of the yeast multidrug transporter Qdr2 in cation homeostasis and the oxidative stress response. FEMS Yeast Research, 13(1), 97-106. doi:10.1111/1567-1364.12013RIOS, G., FERRANDO, A., & SERRANO, R. (1997). Mechanisms of Salt Tolerance Conferred by Overexpression of theHAL1 Gene inSaccharomyces cerevisiae. Yeast, 13(6), 515-528. doi:10.1002/(sici)1097-0061(199705)13:63.0.co;2-xRitz, A. M., Trautwein, M., Grassinger, F., & Spang, A. (2014). The Prion-like Domain in the Exomer-Dependent Cargo Pin2 Serves as a trans-Golgi Retention Motif. Cell Reports, 7(1), 249-260. doi:10.1016/j.celrep.2014.02.026Rockenbauch, U., Ritz, A. M., Sacristan, C., Roncero, C., & Spang, A. (2012). The complex interactions of Chs5p, the ChAPs, and the cargo Chs3p. Molecular Biology of the Cell, 23(22), 4402-4415. doi:10.1091/mbc.e11-12-1015Roncero, C. (2002). The genetic complexity of chitin synthesis in fungi. Current Genetics, 41(6), 367-378. doi:10.1007/s00294-002-0318-7Rothfels, K., Tanny, J. C., Molnar, E., Friesen, H., Commisso, C., & Segall, J. (2005). Components of the ESCRT Pathway, DFG16, and YGR122w Are Required for Rim101 To Act as a Corepressor with Nrg1 at the Negative Regulatory Element of the DIT1 Gene of Saccharomyces cerevisiae. Molecular and Cellular Biology, 25(15), 6772-6788. doi:10.1128/mcb.25.15.6772-6788.2005Santos, B., & Snyder, M. (1997). Targeting of Chitin Synthase 3 to Polarized Growth Sites in Yeast Requires Chs5p and Myo2p. Journal of Cell Biology, 136(1), 95-110. doi:10.1083/jcb.136.1.95Sato, M., Dhut, S., & Toda, T. (2005). New drug-resistant cassettes for gene disruption and epitope tagging inSchizosaccharomyces pombe. Yeast, 22(7), 583-591. doi:10.1002/yea.1233Schekman, R., & Orci, L. (1996). Coat Proteins and Vesicle Budding. Science, 271(5255), 1526-1533. doi:10.1126/science.271.5255.1526Sopko, R., Huang, D., Preston, N., Chua, G., Papp, B., Kafadar, K., 
 Andrews, B. (2006). Mapping Pathways and Phenotypes by Systematic Gene Overexpression. Molecular Cell, 21(3), 319-330. doi:10.1016/j.molcel.2005.12.011Spang, A. (2008). Membrane traffic in the secretory pathway. Cellular and Molecular Life Sciences, 65(18), 2781-2789. doi:10.1007/s00018-008-8349-yStarr, T. L., Pagant, S., Wang, C.-W., & Schekman, R. (2012). Sorting Signals That Mediate Traffic of Chitin Synthase III between the TGN/Endosomes and to the Plasma Membrane in Yeast. PLoS ONE, 7(10), e46386. doi:10.1371/journal.pone.0046386Trautwein, M., Schindler, C., Gauss, R., Dengjel, J., Hartmann, E., & Spang, A. (2006). Arf1p, Chs5p and the ChAPs are required for export of specialized cargo from the Golgi. The EMBO Journal, 25(5), 943-954. doi:10.1038/sj.emboj.7601007Trilla, J. A., DurĂĄn, A., & Roncero, C. (1999). Chs7p, a New Protein Involved in the Control of Protein Export from the Endoplasmic Reticulum that Is Specifically Engaged in the Regulation of Chitin Synthesis in Saccharomyces cerevisiae. Journal of Cell Biology, 145(6), 1153-1163. doi:10.1083/jcb.145.6.1153Valdivia, R. H., Baggott, D., Chuang, J. S., & Schekman, R. W. (2002). The Yeast Clathrin Adaptor Protein Complex 1 Is Required for the Efficient Retention of a Subset of Late Golgi Membrane Proteins. Developmental Cell, 2(3), 283-294. doi:10.1016/s1534-5807(02)00127-2Wadskog, I., Forsmark, A., Rossi, G., Konopka, C., Öyen, M., Goksör, M., 
 Adler, L. (2006). The Yeast Tumor Suppressor Homologue Sro7p Is Required for Targeting of the Sodium Pumping ATPase to the Cell Surface. Molecular Biology of the Cell, 17(12), 4988-5003. doi:10.1091/mbc.e05-08-0798Wang, C.-W., Hamamoto, S., Orci, L., & Schekman, R. (2006). Exomer: a coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast. Journal of Cell Biology, 174(7), 973-983. doi:10.1083/jcb.200605106Weiskoff, A. M., & Fromme, J. C. (2014). Distinct N-terminal regions of the exomer secretory vesicle cargo Chs3 regulate its trafficking itinerary. Frontiers in Cell and Developmental Biology, 2. doi:10.3389/fcell.2014.00047Yahara, N., Ueda, T., Sato, K., & Nakano, A. (2001). Multiple Roles of Arf1 GTPase in the Yeast Exocytic and Endocytic Pathways. Molecular Biology of the Cell, 12(1), 221-238. doi:10.1091/mbc.12.1.221Yenush, L., Merchan, S., Holmes, J., & Serrano, R. (2005). pH-Responsive, Posttranslational Regulation of the Trk1 Potassium Transporter by the Type 1-Related Ppz1 Phosphatase. Molecular and Cellular Biology, 25(19), 8683-8692. doi:10.1128/mcb.25.19.8683-8692.2005Yenush, L. (2002). The Ppz protein phosphatases are key regulators of K+ and pH homeostasis: implications for salt tolerance, cell wall integrity and cell cycle progression. The EMBO Journal, 21(5), 920-929. doi:10.1093/emboj/21.5.920Zanolari, B., Rockenbauch, U., Trautwein, M., Clay, L., Barral, Y., & Spang, A. (2011). Transport to the plasma membrane is regulated differently early and late in the cell cycle in Saccharomyces cerevisiae. Journal of Cell Science, 124(7), 1055-1066. doi:10.1242/jcs.07237
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