Cohen, J. D., Cadena del Castillo, C. E., Kaech, A., Spang, A. and Sundaram, M. (2021) “The C. elegans PTCHD homolog PTR-4 is required for proper organization of the pre-cuticular apical extracellular matrix”. bioRxiv. doi: 10.1101/2021.03.30.437696.   
Laborenz, J., Bykov, Y. S., Knöringer, K., Räschle, M., Filker, S., Prescianotto-Baschong, C., Spang, A., Tatsuta, T., Langer, T., Storchová, Z., Schuldiner, M. and Herrmann, J. M. (2021) “The ER protein Ema19 facilitates the degradation of non-imported mitochondrial precursor proteins”, Molecular Biology of the Cell, 32(8), pp. 664–674/mbcE20110748. doi: 10.1091/mbc.E20-11-0748.   
Tishinov, K. and Spang, A. (2020) “Decapping complex is essential for functional P-body formation and is buffered by nuclear localization”. bioRxiv. doi: 10.1101/2020.09.07.285700.   edoc | Open Access
Wu, Y., Boulogne, C., Carle, S., Podinovskaia, M., Barth, H., Spang, A., Cintrat, J.-C., Gillet, D. and Barbier, J. (2020) “Regulation of endo-lysosomal pathway and autophagic flux by broad-spectrum anti-pathogen inhibitor ABMA”, The FEBS journal. Wiley, 287(15), pp. 3184–3199. doi: 10.1111/febs.15201.   edoc | Open Access
Solinger, J. A., Rashid, H.-O., Prescianotto-Baschong, C. and Spang, A. (2020) “FERARI is required for Rab11-dependent endocytic recycling”, Nature Cell Biology. Nature Publishing Group, 22, pp. 213–224. doi: 10.1038/s41556-019-0456-5.   edoc | Open Access
Kochan, D. Z., Mawer Julia S. P., Tishinov, K., Parekh, S., Massen, J., Graef, M., Spang, A. and Tessarz, P. (2020) “The RNA-binding protein Puf5 buffers mRNA levels against chromatin-mediated changes in nascent transcription”, bioRxiv, preprint, pp. 1–27. doi: 10.1101/2020.08.13.249912.   
Cadena del Castillo, C. E., Hannich, J. T., Kaech, A., Chiyoda, H., Fukuyama, M., Færgeman, N. J., Riezman, H. and Spang, A. (2019) “Patched regulates lipid homeostasis by controlling cellular cholesterol levels”. bioRxiv. doi: 10.1101/816256.   edoc | Open Access
Manchalu, S., Mittal, N., Spang, A. and Jansen, R.-P. (2019) “Local translation of yeast ERG4 mRNA at the endoplasmic reticulum requires the brefeldin A resistance protein Bfr1”, RNA. RNA Society, 25(12), pp. 1661–1672. doi: 10.1261/rna.072017.119.   edoc | Open Access
Laborenz, J., Hansen, K., Prescianotto-Baschong, C., Spang, A. and Herrmann, J. M. (2019) “In vitro import experiments with semi-intact cells suggest a role of the Sec61 paralog Ssh1 in mitochondrial biogenesis”, Biological Chemistry. de Gruyter, 400(9), pp. 1229–1240. doi: 10.1515/hsz-2019-0196.   edoc
Arakel, E. C., Huranova, M., Estrada, A. F., Rau, E.-M., Spang, A. and Schwappach, B. (2019) “Dissection of GTPase activating proteins reveals functional asymmetry in the COPI coat”, Journal of cell science. Company of Biologists, ahead of print, pp. 1–54. doi: 10.1242/jcs.232124.   edoc | Open Access
Stahl, T., Hümmer, S., Ehrenfeuchter, N., Mittal, N., Fucile, G. and Spang, A. (2019) “Asymmetric distribution of glucose transporter mRNA provides a growth advantage in yeast”, The EMBO journal. EMBO Press, 38(10), p. e100373. doi: 10.15252/embj.2018100373.   edoc | Open Access
Spang, A. (2018) “The endoplasmic reticulum-the caring mother of the cell”, Current Opinion in Cell Biology. Elsevier, 53, pp. 92–96. doi: 10.1016/   edoc | Open Access
Podinovskaia, M. and Spang, A. (2018) “The Endosomal Network: Mediators and Regulators of Endosome Maturation”, Progress in molecular and subcellular biology, 57, pp. 137–149. doi: 10.1007/978-3-319-96704-2_1.   edoc
Spang, A. and Mayor, S. (2018) “Editorial Overview: Membranes and organelles: rethinking membrane structure, function and compartments”, Current opinion in cell biology, 53, pp. A1-A3. doi: 10.1016/   edoc
Wang, C., Weidner, J. and Spang, A. (2018) “Preparation of Sequencing RNA Libraries through Chemical Cross-linking Coupled to Affinity Purification (cCLAP) in Saccharomyces cerevisiae”, Bio-protocol. Bio-Protocol, 8(19), pp. 3029–3029. doi: 10.21769/BioProtoc.3029.   edoc | Open Access
Hansen, K. G., Aviram, N., Laborenz, J., Bibi, C., Meyer, M., Spang, A., Schuldiner, M. and Herrmann, J. M. (2018) “An ER surface retrieval pathway safeguards the import of mitochondrial membrane proteins in yeast”, Science. American Association for the Advancement of Science, 361(6407), pp. 1118–1122. doi: 10.1126/science.aar8174.   edoc | Open Access
Ramirez-Macias, I., Barlow, L. D., Anton, C., Spang, A., Roncero, C. and Dacks, J. B. (2018) “Evolutionary cell biology traces the rise of the exomer complex in Fungi from an ancient eukaryotic component”, Scientific Reports. Nature Publishing Group, 8(1), p. 11154. doi: 10.1038/s41598-018-29416-4.   edoc | Open Access
Wang, C., Schmich, F., Srivatsa, S., Weidner, J., Beerenwinkel, N. and Spang, A. (2018) “Context-dependent deposition and regulation of mRNAs in P-bodies”, eLife. eLife Sciences Publications , 7, p. e29815. doi: 10.7554/eLife.29815.   edoc | Open Access
Spang, A. (2017) “Die Zelle: Dorf oder Stadt?”, in Füglister, K. M., Hicklin, M., and Mäser, P. (eds.) natura obscura 200 Naturforschende - 200 Naturphänomene - 200 Jahre Naturforschende Gesellschaft in Basel. Basel: Schwabe AG, pp. 186–187.   edoc
Anton, C., Zanolari, B., Arcones, I., Wang, C., Mulet, J. M., Spang, A. and 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. American Society for Cell Biology, 28(25), pp. 3672–3685. doi: 10.1091/mbc.E17-09-0549.   edoc | Open Access
Spang, A. (2017) “Cell biology: Bulky tether proteins aid membrane fusion”, Nature. Nature Publishing Group , 551, pp. 576–577. doi: 10.1038/nature24754.   edoc
Stevens, J. and Spang, A. (2017) “Attenuation of N-glycosylation causes polarity and adhesion defects in the C. elegans embryo”, Journal of Cell Science. Company of Biologists, 130(7), pp. 1224–1331. doi: 10.1242/jcs.189316.   edoc | Open Access
Hoya, M., Yanguas, F., Moro, S., Prescianotto-Baschong, C., Doncel, C., de León, N., Curto, M.- Ángeles, Spang, A. and Valdivieso, M.-H. (2017) “Traffic Through the Trans-Golgi Network and the Endosomal System Requires Collaboration Between Exomer and Clathrin Adaptors in Fission Yeast”, Genetics. Genetics Society of America, 205(2), pp. 673–690. doi: 10.1534/genetics.116.193458.   edoc
Mittal, N., Guimaraes, J. C., Gross, T., Schmidt, A., Vina-Vilaseca, A., Nedialkova, D. D., Aeschimann, F., Leidel, S. A., Spang, A. and Zavolan, M. (2017) “The Gcn4 transcription factor reduces protein synthesis capacity and extends yeast lifespan”, Nature Communications. Nature Publishing Group, 8(457), pp. 1–12. doi: 10.1038/s41467-017-00539-y.   edoc | Open Access
Spang, A. (2016) “‘Das Meer in uns’”. Switzerland: SRF 2. Available at:   
Pagliuso, A., Tham, T. N., Stevens, J. K., Lagache, T., Persson, R., Salles, A., Olivo-Marin, J.-C., Oddos, S., Spang, A., Cossart, P. and Stavru, F. (2016) “A role for septin 2 in Drp1-mediated mitochondrial fission”, EMBO Reports. Nature Publishing Group, 17(6), pp. 858–873. doi: 10.15252/embr.201541612.   edoc
Ackema, K. B., Prescianotto-Baschong, C., Hench, J., Wang, S. C., Chia, Z. H., Mergentaler, H., Bard, F., Frank, S. and Spang, A. (2016) “Sar1, a Novel Regulator of ER-Mitochondrial Contact Sites”, PLoS ONE. Public Library of Science, 11(4), p. e0154280. doi: 10.1371/journal.pone.0154280.   edoc | Open Access
Huranova, M., Muruganandam, G., Weiss, M. and Spang, A. (2016) “Dynamic assembly of the exomer secretory vesicle cargo adaptor subunits”, EMBO Reports. Nature Publishing Group, 17(2), pp. 202–219. doi: 10.15252/embr.201540795.   edoc
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., Adhihetty, P. J., Adler, S. G., Agam, G., Agarwal, R., Aghi, M. K., Agnello, M., Agostinis, P., Aguilar, P. V., Aguirre-Ghiso, J., Airoldi, E. M., Ait-Si-Ali, S., Akematsu, T., Akporiaye, E. T., Al-Rubeai, M., Albaiceta, G. M., Albanese, C., Albani, D., Albert, M. L., Aldudo, J., Algül, H., Alirezaei, M., Alloza, I., Almasan, A., Almonte-Beceril, M., Alnemri, E. S., Alonso, C., Altan-Bonnet, N., Altieri, D. C., Alvarez, S., Alvarez-Erviti, L., Alves, S., Amadoro, G., Amano, A., Amantini, C., Ambrosio, S., Amelio, I., Amer, A. O., Amessou, M., Amon, A., An, Z., Anania, F. A., Andersen, S. U., Andley, U. P., Andreadi, C. K., Andrieu-Abadie, N., Anel, A., Ann, D. K., Anoopkumar-Dukie, S., Antonioli, M., Aoki, H., Apostolova, N., Aquila, S., Aquilano, K., Araki, K., Arama, E., Aranda, A., Araya, J., Arcaro, A., Arias, E., Arimoto, H., Ariosa, A. R., Armstrong, J. L., Arnould, T., Arsov, I., Asanuma, K., Askanas, V., Asselin, E., Atarashi, R., Atherton, S. S., Atkin, J. D., Attardi, L. D., Auberger, P., Auburger, G., Aurelian, L., Autelli, R., Avagliano, L., Avantaggiati, M. L., Avrahami, L., Awale, S., Azad, N., Bachetti, T., Backer, J. M., Bae, D.-H., Bae, J.-S., Bae, O.-N., Bae, S. H., Baehrecke, E. H., Baek, S.-H., Baghdiguian, S., Bagniewska-Zadworna, A., Bai, H., Bai, J., Bai, X.-Y., Bailly, Y., Balaji, K. N., Balduini, W., Ballabio, A., Balzan, R., Banerjee, R., Bánhegyi, G., Bao, H., Barbeau, B., Barrachina, M. D., Barreiro, E., Bartel, B., Bartolomé, A., Bassham, D. C., Bassi, M. T., Bast, R. C., Basu, A., Batista, M. T., Batoko, H., Battino, M., Bauckman, K., Baumgarner, B. L., Bayer, K. U., Beale, R., Beaulieu, J.-F., Beck, G. R., Becker, C., Beckham, J. D., Bédard, P.-A., Bednarski, P. J., Begley, T. J., Behl, C., Behrends, C., Behrens, G. M., Behrns, K. E., Bejarano, E., Belaid, A., Belleudi, F., Bénard, G., Berchem, G., Bergamaschi, D., Bergami, M., Berkhout, B., Berliocchi, L., Bernard, A., Bernard, M., Bernassola, F., Bertolotti, A., Bess, A. S., Besteiro, S., Bettuzzi, S., Bhalla, S., Bhattacharyya, S., Bhutia, S. K., Biagosch, C., Bianchi, M. W., Biard-Piechaczyk, M., Billes, V., Bincoletto, C., Bingol, B., Bird, S. W., Bitoun, M., Bjedov, I., Blackstone, C., Blanc, L., Blanco, G. A., Blomhoff, H. K., Boada-Romero, E., Böckler, S., Boes, M., Boesze-Battaglia, K., Boise, L. H., Bolino, A., Boman, A., Bonaldo, P., Bordi, M., Bosch, J., Botana, L. M., Botti, J., Bou, G., Bouché, M., Bouchecareilh, M., Boucher, M.-J., Boulton, M. E., Bouret, S. G., Boya, P., Boyer-Guittaut, M., Bozhkov, P. V., Brady, N., Braga, V. M., Brancolini, C., Braus, G. H., Bravo-San Pedro, J. M., Brennan, L. A., Bresnick, E. H., Brest, P., Bridges, D., Bringer, M.-A., Brini, M., Brito, G. C., Brodin, B., Brookes, P. S., Brown, E. J., Brown, K., Broxmeyer, H. E., Bruhat, A., Brum, P. C., Brumell, J. H., Brunetti-Pierri, N., Bryson-Richardson, R. J., Buch, S., Buchan, A. M., Budak, H., Bulavin, D. V., Bultman, S. J., Bultynck, G., Bumbasirevic, V., Burelle, Y., Burke, R. E., Burmeister, M., Bütikofer, P., Caberlotto, L., Cadwell, K., Cahova, M., Cai, D., Cai, J., Cai, Q., Calatayud, S., Camougrand, N., Campanella, M., Campbell, G. R., Campbell, M., Campello, S., Candau, R., Caniggia, I., Cantoni, L., Cao, L., Caplan, A. B., Caraglia, M., Cardinali, C., Cardoso, S. M., Carew, J. S., Carleton, L. A., Carlin, C. R., Carloni, S., Carlsson, S. R., Carmona-Gutierrez, D., Carneiro, L. A., Carnevali, O., Carra, S., Carrier, A., Carroll, B., Casas, C., Casas, J., Cassinelli, G., Castets, P., Castro-Obregon, S., Cavallini, G., Ceccherini, I., Cecconi, F., Cederbaum, A. I., Ceña, V., Cenci, S., Cerella, C., Cervia, D., Cetrullo, S., Chaachouay, H., Chae, H.-J., Chagin, A. S., Chai, C.-Y., Chakrabarti, G., Chamilos, G., Chan, E. Y., Chan, M. T., Chandra, D., Chandra, P., Chang, C.-P., Chang, R. C.-C., Chang, T. Y., Chatham, J. C., Chatterjee, S., Chauhan, S., Che, Y., Cheetham, M. E., Cheluvappa, R., Chen, C.-J., Chen, G., Chen, G.-C., Chen, G., Chen, H., Chen, J. W., Chen, J.-K., Chen, M., Chen, M., Chen, P., Chen, Q., Chen, Q., Chen, S.-D., Chen, S., Chen, S. S.-L., Chen, W., Chen, W.-J., Chen, W. Q., Chen, W., Chen, X., Chen, Y.-H., Chen, Y.-G., Chen, Y., Chen, Y., Chen, Y., Chen, Y.-J., Chen, Y.-Q., Chen, Y., Chen, Z., Chen, Z., Cheng, A., Cheng, C. H., Cheng, H., Cheong, H., Cherry, S., Chesney, J., Cheung, C. H. A., Chevet, E., Chi, H. C., Chi, S.-G., Chiacchiera, F., Chiang, H.-L., Chiarelli, R., Chiariello, M., Chieppa, M., Chin, L.-S., Chiong, M., Chiu, G. N., Cho, D.-H., Cho, S.-G., Cho, W. C., Cho, Y.-Y., Cho, Y.-S., Choi, A. M., Choi, E.-J., Choi, E.-K., Choi, J., Choi, M. E., Choi, S.-I., Chou, T.-F., Chouaib, S., Choubey, D., Choubey, V., Chow, K.-C., Chowdhury, K., Chu, C. T., Chuang, T.-H., Chun, T., Chung, H., Chung, T., Chung, Y.-L., Chwae, Y.-J., Cianfanelli, V., Ciarcia, R., Ciechomska, I. A., Ciriolo, M. R., Cirone, M., Claerhout, S., Clague, M. J., Clària, J., Clarke, P. G., Clarke, R., Clementi, E., Cleyrat, C., Cnop, M., Coccia, E. M., Cocco, T., Codogno, P., Coers, J., Cohen, E. E., Colecchia, D., Coletto, L., Coll, N. S., Colucci-Guyon, E., Comincini, S., Condello, M., Cook, K. L., Coombs, G. H., Cooper, C. D., Cooper, J. M., Coppens, I., Corasaniti, M. T., Corazzari, M., Corbalan, R., Corcelle-Termeau, E., Cordero, M. D., Corral-Ramos, C., Corti, O., Cossarizza, A., Costelli, P., Costes, S., Cotman, S. L., Coto-Montes, A., Cottet, S., Couve, E., Covey, L. R., Cowart, L. A., Cox, J. S., Coxon, F. P., Coyne, C. B., Cragg, M. S., Craven, R. J., Crepaldi, T., Crespo, J. L., Criollo, A., Crippa, V., Cruz, M. T., Cuervo, A. M., Cuezva, J. M., Cui, T., Cutillas, P. R., Czaja, M. J., Czyzyk-Krzeska, M. F., Dagda, R. K., Dahmen, U., Dai, C., Dai, W., Dai, Y., Dalby, K. N., Dalla Valle, L., Dalmasso, G., D’Amelio, M., Damme, M., Darfeuille-Michaud, A., Dargemont, C., Darley-Usmar, V. M., Dasarathy, S., Dasgupta, B., Dash, S., Dass, C. R., Davey, H. M., Davids, L. M., Dávila, D., Davis, R. J., Dawson, T. M., Dawson, V. L., Daza, P., de Belleroche, J., de Figueiredo, P., de Figueiredo, R. C. B. Q., de la Fuente, J., De Martino, L., De Matteis, A., De Meyer, G. R., De Milito, A., De Santi, M., de Souza, W., De Tata, V., De Zio, D., Debnath, J., Dechant, R., Decuypere, J.-P., Deegan, S., Dehay, B., Del Bello, B., Del Re, D. P., Delage-Mourroux, R., Delbridge, L. M., Deldicque, L., Delorme-Axford, E., Deng, Y., Dengjel, J., Denizot, M., Dent, P., Der, C. J., Deretic, V., Derrien, B., Deutsch, E., Devarenne, T. P., Devenish, R. J., Di Bartolomeo, S., Di Daniele, N., Di Domenico, F., Di Nardo, A., Di Paola, S., Di Pietro, A., Di Renzo, L., DiAntonio, A., Díaz-Araya, G., Díaz-Laviada, I., Diaz-Meco, M. T., Diaz-Nido, J., Dickey, C. A., Dickson, R. C., Diederich, M., Digard, P., Dikic, I., Dinesh-Kumar, S. P., Ding, C., Ding, W.-X., Ding, Z., Dini, L., Distler, J. H., Diwan, A., Djavaheri-Mergny, M., Dmytruk, K., Dobson, R. C., Doetsch, V., Dokladny, K., Dokudovskaya, S., Donadelli, M., Dong, X. C., Dong, X., Dong, Z., Donohue, T. M., Doran, K. S., D’Orazi, G., Dorn, G. W., Dosenko, V., Dridi, S., Drucker, L., Du, J., Du, L.-L., Du, L., du Toit, A., Dua, P., Duan, L., Duann, P., Dubey, V. K., Duchen, M. R., Duchosal, M. A., Duez, H., Dugail, I., Dumit, V. I., Duncan, M. C., Dunlop, E. A., Dunn, W. A., Dupont, N., Dupuis, L., Durán, R. V., Durcan, T. M., Duvezin-Caubet, S., Duvvuri, U., Eapen, V., Ebrahimi-Fakhari, D., Echard, A., Eckhart, L., Edelstein, C. L., Edinger, A. L., Eichinger, L., Eisenberg, T., Eisenberg-Lerner, A., Eissa, N. T., El-Deiry, W. S., El-Khoury, V., Elazar, Z., Eldar-Finkelman, H., Elliott, C. J., Emanuele, E., Emmenegger, U., Engedal, N., Engelbrecht, A.-M., Engelender, S., Enserink, J. M., Erdmann, R., Erenpreisa, J., Eri, R., Eriksen, J. L., Erman, A., Escalante, R., Eskelinen, E.-L., Espert, L., Esteban-Martínez, L., Evans, T. J., Fabri, M., Fabrias, G., Fabrizi, C., Facchiano, A., Færgeman, N. J., Faggioni, A., Fairlie, W. D., Fan, C., Fan, D., Fan, J., Fang, S., Fanto, M., Fanzani, A., Farkas, T., Faure, M., Favier, F. B., Fearnhead, H., Federici, M., Fei, E., Felizardo, T. C., Feng, H., Feng, Y., Feng, Y., Ferguson, T. A., Fernández, Álvaro F., Fernandez-Barrena, M. G., Fernandez-Checa, J. C., Fernández-López, A., Fernandez-Zapico, M. E., Feron, O., Ferraro, E., Ferreira-Halder, C. V., Fesus, L., Feuer, R., Fiesel, F. C., Filippi-Chiela, E. C., Filomeni, G., Fimia, G. M., Fingert, J. H., Finkbeiner, S., Finkel, T., Fiorito, F., Fisher, P. B., Flajolet, M., Flamigni, F., Florey, O., Florio, S., Floto, R. A., Folini, M., Follo, C., Fon, E. A., Fornai, F., Fortunato, F., Fraldi, A., Franco, R., Francois, A., François, A., Frankel, L. B., Fraser, I. D., Frey, N., Freyssenet, D. G., Frezza, C., Friedman, S. L., Frigo, D. E., Fu, D., Fuentes, J. M., Fueyo, J., Fujitani, Y., Fujiwara, Y., Fujiya, M., Fukuda, M., Fulda, S., Fusco, C., Gabryel, B., Gaestel, M., Gailly, P., Gajewska, M., Galadari, S., Galili, G., Galindo, I., Galindo, M. F., Galliciotti, G., Galluzzi, L., Galluzzi, L., Galy, V., Gammoh, N., Gandy, S., Ganesan, A. K., Ganesan, S., Ganley, I. G., Gannagé, M., Gao, F.-B., Gao, F., Gao, J.-X., García Nannig, L., García Véscovi, E., Garcia-Macía, M., Garcia-Ruiz, C., Garg, A. D., Garg, P. K., Gargini, R., Gassen, N. C., Gatica, D., Gatti, E., Gavard, J., Gavathiotis, E., Ge, L., Ge, P., Ge, S., Gean, P.-W., Gelmetti, V., Genazzani, A. A., Geng, J., Genschik, P., Gerner, L., Gestwicki, J. E., Gewirtz, D. A., Ghavami, S., Ghigo, E., Ghosh, D., Giammarioli, A. M., Giampieri, F., Giampietri, C., Giatromanolaki, A., Gibbings, D. J., Gibellini, L., Gibson, S. B., Ginet, V., Giordano, A., Giorgini, F., Giovannetti, E., Girardin, S. E., Gispert, S., Giuliano, S., Gladson, C. L., Glavic, A., Gleave, M., Godefroy, N., Gogal, R. M., Gokulan, K., Goldman, G. H., Goletti, D., Goligorsky, M. S., Gomes, A. V., Gomes, L. C., Gomez, H., Gomez-Manzano, C., Gómez-Sánchez, R., Gonçalves, D. A., Goncu, E., Gong, Q., Gongora, C., Gonzalez, C. B., Gonzalez-Alegre, P., Gonzalez-Cabo, P., González-Polo, R. A., Goping, I. S., Gorbea, C., Gorbunov, N. V., Goring, D. R., Gorman, A. M., Gorski, S. M., Goruppi, S., Goto-Yamada, S., Gotor, C., Gottlieb, R. A., Gozes, I., Gozuacik, D., Graba, Y., Graef, M., Granato, G. E., Grant, G. D., Grant, S., Gravina, G. L., Green, D. R., Greenhough, A., Greenwood, M. T., Grimaldi, B., Gros, F., Grose, C., Groulx, J.-F., Gruber, F., Grumati, P., Grune, T., Guan, J.-L., Guan, K.-L., Guerra, B., Guillen, C., Gulshan, K., Gunst, J., Guo, C., Guo, L., Guo, M., Guo, W., Guo, X.-G., Gust, A. A., Gustafsson, Åsa B., Gutierrez, E., Gutierrez, M. G., Gwak, H.-S., Haas, A., Haber, J. E., Hadano, S., Hagedorn, M., Hahn, D. R., Halayko, A. J., Hamacher-Brady, A., Hamada, K., Hamai, A., Hamann, A., Hamasaki, M., Hamer, I., Hamid, Q., Hammond, E. M., Han, F., Han, W., Handa, J. T., Hanover, J. A., Hansen, M., Harada, M., Harhaji-Trajkovic, L., Harper, J. W., Harrath, A. H., Harris, A. L., Harris, J., Hasler, U., Hasselblatt, P., Hasui, K., Hawley, R. G., Hawley, T. S., He, C., He, C. Y., He, F., He, G., He, R.-R., He, X.-H., He, Y.-W., He, Y.-Y., Heath, J. K., Hébert, M.-J., Heinzen, R. A., Helgason, G. V., Hensel, M., Henske, E. P., Her, C., Herman, P. K., Hernández, A., Hernandez, C., Hernández-Tiedra, S., Hetz, C., Hiesinger, P. 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K., Salvaterra, P. M., Salvioli, R., Samali, A., Sanchez, A. M., Sánchez-Alcázar, J. A., Sanchez-Prieto, R., Sandri, M., Sanjuan, M. A., Santaguida, S., Santambrogio, L., Santoni, G., Dos Santos, C. N., Saran, S., Sardiello, M., Sargent, G., Sarkar, P., Sarkar, S., Sarrias, M. R., Sarwal, M. M., Sasakawa, C., Sasaki, M., Sass, M., Sato, K., Sato, M., Satriano, J., Savaraj, N., Saveljeva, S., Schaefer, L., Schaible, U. E., Scharl, M., Schatzl, H. M., Schekman, R., Scheper, W., Schiavi, A., Schipper, H. M., Schmeisser, H., Schmidt, J., Schmitz, I., Schneider, B. E., Schneider, E. M., Schneider, J. L., Schon, E. A., Schönenberger, M. J., Schönthal, A. H., Schorderet, D. F., Schröder, B., Schuck, S., Schulze, R. J., Schwarten, M., Schwarz, T. L., Sciarretta, S., Scotto, K., Scovassi, A. I., Screaton, R. A., Screen, M., Seca, H., Sedej, S., Segatori, L., Segev, N., Seglen, P. O., Seguí-Simarro, J. M., Segura-Aguilar, J., Seki, E., Sell, C., Seiliez, I., Semenkovich, C. F., Semenza, G. L., Sen, U., Serra, A. L., Serrano-Puebla, A., Sesaki, H., Setoguchi, T., Settembre, C., Shacka, J. J., Shajahan-Haq, A. N., Shapiro, I. M., Sharma, S., She, H., Shen, C.-K. J., Shen, C.-C., Shen, H.-M., Shen, S., Shen, W., Sheng, R., Sheng, X., Sheng, Z.-H., Shepherd, T. G., Shi, J., Shi, Q., Shi, Q., Shi, Y., Shibutani, S., Shibuya, K., Shidoji, Y., Shieh, J.-J., Shih, C.-M., Shimada, Y., Shimizu, S., Shin, D. W., Shinohara, M. L., Shintani, M., Shintani, T., Shioi, T., Shirabe, K., Shiri-Sverdlov, R., Shirihai, O., Shore, G. C., Shu, C.-W., Shukla, D., Sibirny, A. A., Sica, V., Sigurdson, C. J., Sigurdsson, E. M., Sijwali, P. S., Sikorska, B., Silveira, W. A., Silvente-Poirot, S., Silverman, G. A., Simak, J., Simmet, T., Simon, A. K., Simon, H.-U., Simone, C., Simons, M., Simonsen, A., Singh, R., Singh, S. V., Singh, S. K., Sinha, D., Sinha, S., Sinicrope, F. A., Sirko, A., Sirohi, K., Sishi, B. J., Sittler, A., Siu, P. M., Sivridis, E., Skwarska, A., Slack, R., Slaninová, I., Slavov, N., Smaili, S. S., Smalley, K. S., Smith, D. R., Soenen, S. J., Soleimanpour, S. A., Solhaug, A., Somasundaram, K., Son, J. H., Sonawane, A., Song, C., Song, F., Song, H. K., Song, J.-X., Song, W., Soo, K. Y., Sood, A. K., Soong, T. W., Soontornniyomkij, V., Sorice, M., Sotgia, F., Soto-Pantoja, D. R., Sotthibundhu, A., Sousa, M. J., Spaink, H. P., Span, P. N., Spang, A., Sparks, J. D., Speck, P. G., Spector, S. A., Spies, C. D., Springer, W., Clair, D. S., Stacchiotti, A., Staels, B., Stang, M. T., Starczynowski, D. T., Starokadomskyy, P., Steegborn, C., Steele, J. W., Stefanis, L., Steffan, J., Stellrecht, C. M., Stenmark, H., Stepkowski, T. M., Stern, S. T., Stevens, C., Stockwell, B. R., Stoka, V., Storchova, Z., Stork, B., Stratoulias, V., Stravopodis, D. J., Strnad, P., Strohecker, A. M., Ström, A.-L., Stromhaug, P., Stulik, J., Su, Y.-X., Su, Z., Subauste, C. S., Subramaniam, S., Sue, C. M., Suh, S. W., Sui, X., Sukseree, S., Sulzer, D., Sun, F.-L., Sun, J., Sun, J., Sun, S.-Y., Sun, Y., Sun, Y., Sun, Y., Sundaramoorthy, V., Sung, J., Suzuki, H., Suzuki, K., Suzuki, N., Suzuki, T., Suzuki, Y. J., Swanson, M. S., Swanton, C., Swärd, K., Swarup, G., Sweeney, S. T., Sylvester, P. W., Szatmari, Z., Szegezdi, E., Szlosarek, P. W., Taegtmeyer, H., Tafani, M., Taillebourg, E., Tait, S. W., Takacs-Vellai, K., Takahashi, Y., Takáts, S., Takemura, G., Takigawa, N., Talbot, N. J., Tamagno, E., Tamburini, J., Tan, C.-P., Tan, L., Tan, M. L., Tan, M., Tan, Y.-J., Tanaka, K., Tanaka, M., Tang, D., Tang, D., Tang, G., Tanida, I., Tanji, K., Tannous, B. A., Tapia, J. A., Tasset-Cuevas, I., Tatar, M., Tavassoly, I., Tavernarakis, N., Taylor, A., Taylor, G. S., Taylor, G. A., Taylor, J. P., Taylor, M. J., Tchetina, E. V., Tee, A. R., Teixeira-Clerc, F., Telang, S., Tencomnao, T., Teng, B.-B., Teng, R.-J., Terro, F., Tettamanti, G., Theiss, A. L., Theron, A. E., Thomas, K. J., Thomé, M. P., Thomes, P. G., Thorburn, A., Thorner, J., Thum, T., Thumm, M., Thurston, T. L., Tian, L., Till, A., Ting, J. P.-Y., Titorenko, V. I., Toker, L., Toldo, S., Tooze, S. A., Topisirovic, I., Torgersen, M. L., Torosantucci, L., Torriglia, A., Torrisi, M. R., Tournier, C., Towns, R., Trajkovic, V., Travassos, L. H., Triola, G., Tripathi, D. N., Trisciuoglio, D., Troncoso, R., Trougakos, I. P., Truttmann, A. C., Tsai, K.-J., Tschan, M. P., Tseng, Y.-H., Tsukuba, T., Tsung, A., Tsvetkov, A. S., Tu, S., Tuan, H.-Y., Tucci, M., Tumbarello, D. A., Turk, B., Turk, V., Turner, R. F., Tveita, A. A., Tyagi, S. C., Ubukata, M., Uchiyama, Y., Udelnow, A., Ueno, T., Umekawa, M., Umemiya-Shirafuji, R., Underwood, B. R., Ungermann, C., Ureshino, R. P., Ushioda, R., Uversky, V. N., Uzcátegui, N. L., Vaccari, T., Vaccaro, M. I., Váchová, L., Vakifahmetoglu-Norberg, H., Valdor, R., Valente, E. M., Vallette, F., Valverde, A. M., Van den Berghe, G., Van Den Bosch, L., van den Brink, G. R., van der Goot, F. G., van der Klei, I. J., van der Laan, L. J., van Doorn, W. G., van Egmond, M., van Golen, K. L., Van Kaer, L., van Lookeren Campagne, M., Vandenabeele, P., Vandenberghe, W., Vanhorebeek, I., Varela-Nieto, I., Vasconcelos, M. H., Vasko, R., Vavvas, D. G., Vega-Naredo, I., Velasco, G., Velentzas, A. D., Velentzas, P. D., Vellai, T., Vellenga, E., Vendelbo, M. H., Venkatachalam, K., Ventura, N., Ventura, S., Veras, P. S., Verdier, M., Vertessy, B. G., Viale, A., Vidal, M., Vieira, H. L. A., Vierstra, R. D., Vigneswaran, N., Vij, N., Vila, M., Villar, M., Villar, V. H., Villarroya, J., Vindis, C., Viola, G., Viscomi, M. T., Vitale, G., Vogl, D. T., Voitsekhovskaja, O. V., von Haefen, C., von Schwarzenberg, K., Voth, D. E., Vouret-Craviari, V., Vuori, K., Vyas, J. M., Waeber, C., Walker, C. L., Walker, M. J., Walter, J., Wan, L., Wan, X., Wang, B., Wang, C., Wang, C.-Y., Wang, C., Wang, C., Wang, C., Wang, D., Wang, F., Wang, F., Wang, G., Wang, H.-J., Wang, H., Wang, H.-G., Wang, H., Wang, H.-D., Wang, J., Wang, J., Wang, M., Wang, M.-Q., Wang, P.-Y., Wang, P., Wang, R. C., Wang, S., Wang, T.-F., Wang, X., Wang, X.-J., Wang, X.-W., Wang, X., Wang, X., Wang, Y., Wang, Y., Wang, Y., Wang, Y.-J., Wang, Y., Wang, Y., Wang, Y. T., Wang, Y., Wang, Z.-N., Wappner, P., Ward, C., Ward, D. M., Warnes, G., Watada, H., Watanabe, Y., Watase, K., Weaver, T. E., Weekes, C. D., Wei, J., Weide, T., Weihl, C. C., Weindl, G., Weis, S. N., Wen, L., Wen, X., Wen, Y., Westermann, B., Weyand, C. M., White, A. R., White, E., Whitton, J. L., Whitworth, A. J., Wiels, J., Wild, F., Wildenberg, M. E., Wileman, T., Wilkinson, D. S., Wilkinson, S., Willbold, D., Williams, C., Williams, K., Williamson, P. R., Winklhofer, K. F., Witkin, S. S., Wohlgemuth, S. E., Wollert, T., Wolvetang, E. J., Wong, E., Wong, G. W., Wong, R. W., Wong, V. K. W., Woodcock, E. A., Wright, K. L., Wu, C., Wu, D., Wu, G. S., Wu, J., Wu, J., Wu, M., Wu, M., Wu, S., Wu, W. K., Wu, Y., Wu, Z., Xavier, C. P., Xavier, R. J., Xia, G.-X., Xia, T., Xia, W., Xia, Y., Xiao, H., Xiao, J., Xiao, S., Xiao, W., Xie, C.-M., Xie, Z., Xie, Z., Xilouri, M., Xiong, Y., Xu, C., Xu, C., Xu, F., Xu, H., Xu, H., Xu, J., Xu, J., Xu, J., Xu, L., Xu, X., Xu, Y., Xu, Y., Xu, Z.-X., Xu, Z., Xue, Y., Yamada, T., Yamamoto, A., Yamanaka, K., Yamashina, S., Yamashiro, S., Yan, B., Yan, B., Yan, X., Yan, Z., Yanagi, Y., Yang, D.-S., Yang, J.-M., Yang, L., Yang, M., Yang, P.-M., Yang, P., Yang, Q., Yang, W., Yang, W. Y., Yang, X., Yang, Y., Yang, Y., Yang, Z., Yang, Z., Yao, M.-C., Yao, P. J., Yao, X., Yao, Z., Yao, Z., Yasui, L. S., Ye, M., Yedvobnick, B., Yeganeh, B., Yeh, E. S., Yeyati, P. L., Yi, F., Yi, L., Yin, X.-M., Yip, C. K., Yoo, Y.-M., Yoo, Y. H., Yoon, S.-Y., Yoshida, K.-I., Yoshimori, T., Young, K. H., Yu, H., Yu, J. J., Yu, J.-T., Yu, J., Yu, L., Yu, W. H., Yu, X.-F., Yu, Z., Yuan, J., Yuan, Z.-M., Yue, B. Y., Yue, J., Yue, Z., Zacks, D. N., Zacksenhaus, E., Zaffaroni, N., Zaglia, T., Zakeri, Z., Zecchini, V., Zeng, J., Zeng, M., Zeng, Q., Zervos, A. S., Zhang, D. D., Zhang, F., Zhang, G., Zhang, G.-C., Zhang, H., Zhang, H., Zhang, H., Zhang, H., Zhang, J., Zhang, J., Zhang, J., Zhang, J., Zhang, J.-P., Zhang, L., Zhang, L., Zhang, L., Zhang, L., Zhang, M.-Y., Zhang, X., Zhang, X. D., Zhang, Y., Zhang, Y., Zhang, Y., Zhang, Y., Zhang, Y., Zhao, M., Zhao, W.-L., Zhao, X., Zhao, Y. G., Zhao, Y., Zhao, Y., Zhao, Y.-X., Zhao, Z., Zhao, Z. J., Zheng, D., Zheng, X.-L., Zheng, X., Zhivotovsky, B., Zhong, Q., Zhou, G.-Z., Zhou, G., Zhou, H., Zhou, S.-F., Zhou, X.-J., Zhu, H., Zhu, H., Zhu, W.-G., Zhu, W., Zhu, X.-F., Zhu, Y., Zhuang, S.-M., Zhuang, X., Ziparo, E., Zois, C. E., Zoladek, T., Zong, W.-X., Zorzano, A. and Zughaier, S. M. (2016) “Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)”, Autophagy. Taylor & Francis, pp. 1–222. doi: 10.1080/15548627.2015.1100356.   edoc
Spang, A. (2016) “Membrane Tethering Complexes in the Endosomal System”, Frontiers in Cell and Developmental Biology. Frontiers Media, 4(35), pp. 1–7. doi: 10.3389/fcell.2016.00035.   edoc | Open Access
Zhu, M., Wu, G., Li, Y. X., Stevens, J. K., Fan, C. X., Spang, A. and Dong, M. Q. (2015) “Serum- and Glucocorticoid-Inducible Kinase-1 (SGK-1) Plays a Role in Membrane Trafficking in Caenorhabditis elegans”, PLoS ONE. Public Library of Science, 10(6), p. e0130778. doi: 10.1371/journal.pone.0130778.   edoc | Open Access
Estrada, A. F., Muruganandam, G., Prescianotto-Baschong, C. and Spang, A. (2015) “The ArfGAP2/3 Glo3 and ergosterol collaborate in transport of a subset of cargoes”, Biology Open. Company of Biologists, 4(7), pp. 792–802. doi: 10.1242/bio.011528.   edoc | Open Access
Spang, A. (2015) “Anniversary of the discovery of sec mutants by Novick and Schekman”, Molecular Biology of the Cell. American Society for Cell Biology, 26(10), pp. 1783–1785. doi: 10.1091/mbc.E14-11-1511.   edoc | Open Access
Spang, A. (2015) “The road not taken: Less traveled roads from the TGN to the plasma membrane”, Membranes. MDPI, Vol. 5, H. 1, pp. 84–98. doi: 10.3390/membranes5010084.   edoc | Open Access
Herrmann, J. M. and Spang, A. (2015) “Intracellular parcel service : current issues in intracellular membrane trafficking”, Methods in Molecular Biology. Humana Press, 1270, pp. 1–12. doi: 10.1007/978-1-4939-2309-0_1.   edoc
Spang, A. (2015) “A small GTPase involved in mitochondrial morphology and function”, Biochemical Society Transactions. Portland Press, 43(1), pp. 108–110. doi: 10.1042/BST20140284.   edoc
Spang, A. (2014) “Die Biomedizin im Umbruch”. Switzerland: SRF 2. Available at:   
Solinger, J. A. and Spang, A. (2014) “Loss of the Sec1/Munc18 family proteins VPS-33.2 and VPS-33.1 bypass a block in endosome maturation in C. elegans”, Molecular Biology of the Cell. American Society for Cell Biology, 25(24), pp. 3909–3925. doi: 10.1091/mbc.E13-12-0710.   edoc | Open Access
Ackema, K. B., Hench, J., Böckler, S., Wang, S. C., Sauder, U., Mergentaler, H., Westermann, B., Bard, F., Frank, S. and Spang, A. (2014) “The small GTPase Arf1 modulates mitochondrial morphology and function”, The EMBO Journal. Nature Publishing Group, 33(22), pp. 2659–2675. doi: 10.15252/embj.201489039.   edoc
Solinger, J. A., Poteryaev, D. and Spang, A. (2014) “Application of RNAi Technology and Fluorescent Protein Markers to Study Membrane Traffic in C. elegans”, Methods in Molecular Biology. Humana Press, 1174, pp. 329–347. doi: 10.1007/978-1-4939-0944-5_23.   edoc
Ritz, A. M., Trautwein, M., Grassinger, F. and Spang, A. (2014) “The Prion-like domain in the exomer-dependent cargo Pin2 serves as a trans-Golgi retention motif”, Cell Reports. Elsevier, 7(1), pp. 249–260. doi: 10.1016/j.celrep.2014.02.026.   edoc | Open Access
Weidner, J., Wang, C., Prescianotto-Baschong, C., Estrada, A. F. and Spang, A. (2014) “The polysome-associated proteins Scp160 and Bfr1 prevent P body formation under normal growth conditions”, Journal of Cell Science. Company of Biologists, 127(5), pp. 1–35. doi: 10.1242/jcs.142083.   edoc | Open Access
Spang, A. (2013) “Das geheime Leben der Zelle - Anne Spang im Gespräch”. Switzerland: SRF 2.   
Spang, A. J. F. S. (2013) “Nobelpreis - Tages-Anzeiger”, Tages-Anzeiger, 14 October, p. x.   
Spang, A. interviewt von B., Katharina and Radiosprecher Biber, P. (2013) “Reaktionen der Nobelpreis-Gewinner”. Switzerland: SRF 2. Available at:   
Spang, A. (2013) “Der Tanz der Proteine”. Switzerland: SR 2. Available at:   
Sacristan, C., Manzano-Lopez, J., Reyes, A., Spang, A., Muniz, M. and Roncero, C. (2013) “Oligomerization of the chitin synthase Chs3 is monitored at the Golgi and affects its endocytic recycling”, Molecular Microbiology. Blackwell, 90(2), pp. 252–266. doi: 10.1111/mmi.12360.   edoc
Spang, A. (2013) “Retrograde traffic from the Golgi to the endoplasmic reticulum”, Cold Spring Harbor Perspectives in Biology. Cold Spring Harbor Laboratory Press, 5(6), pp. 313–322. doi: 10.1101/cshperspect.a013391.   edoc
Ackema, K. B., Sauder, U., Solinger, J. A. and Spang, A. (2013) “The ArfGEF GBF-1 Is Required for ER Structure, Secretion and Endocytic Transport in C. elegans”, PLoS ONE. Public Library of Science, Vol. 8, H. 6 , e67076. doi: 10.1371/journal.pone.0067076.   edoc | Open Access
Stevens, J. and Spang, A. (2013) “N-Glycosylation Is Required for Secretion and Mitosis in C. elegans”, PLoS ONE. Public Library of Science, 8(5), p. e63687. doi: 10.1371/journal.pone.0063687.   edoc | Open Access
Solinger, J. A. and Spang, A. (2013) “Tethering complexes in the endocytic pathway : CORVET and HOPS”, FEBS Journal. Wiley, 280(12), pp. 2743–2757. doi: 10.1111/febs.12151.   edoc
Hong, W. and Spang, A. (2013) “Precise and timely delivery of proteins within cells continues to be an exciting area of cell biology”, Molecular Biology of the Cell. American Society for Cell Biology, 24(6), p. 670. doi: 10.1091/mbc.E12-12-0871.   edoc | Open Access
Spang, A. (2013) “Traffic COPs: rules of detection”, The EMBO Journal. Nature Publishing Group, 32(7), pp. 915–916. doi: 10.1038/emboj.2013.57.   edoc
Rockenbauch, U., Ritz, A. M., Sacristan, C., Roncero, C. and Spang, A. (2012) “The complex interactions of Chs5p, the ChAPs and the cargo Chs3p”, Molecular Biology of the Cell. American Society for Cell Biology, 23(22), pp. 4402–4415. doi: 10.1091/mbc.E11-12-1015.   edoc | Open Access
Spang, A. (2012) “The DSL1 complex : the smallest but not the least CATCHR”, Traffic. Blackwell, 13(7), pp. 908–913. doi: 10.1111/j.1600-0854.2012.01362.x.   edoc
Spang, A. (2011) “Zellbiologie : über die Rolle der Endozytose bei Krankheiten”, BIOspektrum. Springer, 17(6), pp. 626–628. doi: 10.1007/s12268-011-0099-y.   edoc | Open Access
Johannessen, M., Walquist, M., Gerits, N., Dragset, M., Spang, A. and Moens, U. (2011) “BKV Agnoprotein Interacts with α-Soluble N-Ethylmaleimide-Sensitive Fusion Attachment Protein, and Negatively Influences Transport of VSVG-EGFP”, PLoS ONE. Public Library of Science, Vol. 6, H. 9 , e24489. doi: 10.1371/journal.pone.0024489.   edoc | Open Access
Zanolari, B., Rockenbauch, U., Trautwein, M., Clay, L., Barral, Y. and 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. Company of Biologists, 124(7), pp. 1055–1066. doi: 10.1242/jcs.072371.   edoc | Open Access
Diefenbacher, M., Thorsteinsdottir, H. and Spang, A. (2011) “The DSL1 tethering complex actively participates in SNARE complex assembly at the endoplasmic reticulum in S. cerevisiae”, Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology, 286(28), pp. 25027–25038. doi: 10.1074/jbc.M110.215657.   edoc | Open Access
Kilchert, C. and Spang, A. (2011) “Cotranslational transport of ABP140 mRNA to the distal pole of S. cerevisiae”, The EMBO journal. Nature Publishing Group, 30(17), pp. 3567–3580. doi: 10.1038/emboj.2011.247.   edoc | Open Access
Spang, A. (2011) “Signalling gets sorted by retromer”, The EMBO Journal. Nature Publishing Group, 30(15), pp. 2988–2989. doi: 10.1038/emboj.2011.232.   edoc
Rodriguez, F. and Spang, A. (2010) “Studying the ArfGAP-dependent conformational changes in SNAREs”, Methods in Molecular Biology. Humana Press, 619, pp. 377–387. doi: 10.1007/978-1-60327-412-8_22.   edoc
Spang, A., Shiba, Y. and Randazzo, P. A. (2010) “Arf GAPs: Gatekeepers of vesicle generation”, FEBS Letters. Elsevier, 584(12), pp. 2646–2651. doi: 10.1016/j.febslet.2010.04.005.   edoc
Kilchert, C., Weidner, J., Prescianotto-Baschong, C. and Spang, A. (2010) “Defects in the Secretory Pathway and High Ca2+ Induce Multiple P-bodies”, Molecular Biology of the Cell. American Society for Cell Biology, 21(15), pp. 2624–2638. doi: 10.1091/mbc.E10-02-0099.   edoc | Open Access
Poteryaev, D., Datta, S., Ackema, K., Zerial, M. and Spang, A. (2010) “Identification of the Switch in Early-to-Late Endosome Transition”, Cell. Cell Press, 141(3), pp. 497–508. doi: 10.1016/j.cell.2010.03.011.   edoc
Malone, J. G., Jaeger, T., Spangler, C., Ritz, D., Spang, A., Arrieumerlou, C., Kaever, V., Landmann, R. and Jenal, U. (2010) “YfiBNR Mediates Cyclic di-GMP Dependent Small Colony Variant Formation and Persistence in Pseudomonas aeruginosa”, PLoS Pathogens. Public Library of Science, 6(3), p. e1000804. doi: 10.1371/journal.ppat.1000804.   edoc | Open Access
Spang, A. (2009) “On the fate of early endosomes”, Biological Chemistry. de Gruyter, 390(8), pp. 753–759. doi: 10.1515/BC.2009.056.   edoc | Open Access
Schindler, C., Rodriguez, F., Poon, P. P., Singer, R. A., Johnston, G. C. and Spang, A. (2009) “The GAP Domain and the SNARE, Coatomer and Cargo Interaction Region of the ArfGAP2/3 Glo3 are Sufficient for Glo3 Function”, Traffic. Blackwell, 10(9), pp. 1362–1375. doi: 10.1111/j.1600-0854.2009.00952.x.   edoc
Spang, A. (2009) “On vesicle formation and tethering in the ER-Golgi shuttle”, Current Opinion in Cell Biology. Elsevier, 21(4), pp. 531–536. doi: 10.1016/   edoc
Poteryaev, D. and Spang, A. (2008) “Application of RNAi technology and fluorescent protein markers to study membrane traffic in Caenorhabditis elegans”, Methods in Molecular Biology. Humana Press, 440, pp. 331–347. doi: 10.1007/978-1-4939-0944-5_23.   edoc
Herrmann, J. M. and Spang, A. (2008) “Freight management in the cell : current aspects of intracellular membrane trafficking”, Methods in Molecular Biology. Humana Press, 457, pp. 3–12. doi: 10.1007/978-1-59745-261-8_1.   edoc
Spang, A. (2008) “Membrane traffic in the secretory pathway : the life cycle of a transport vesicle”, Cellular and Molecular Life Sciences. Birkhäuser, 65(18), pp. 2781–2789. doi: 10.1007/s00018-008-8349-y.   edoc
Kamena, F., Diefenbacher, M., Kilchert, C., Schwarz, H. and Spang, A. (2008) “Ypt1p is essential for retrograde Golgi-ER transport and for Golgi maintenance in S. cerevisiae”, Journal of Cell Science. Company of Biologists, 121(8), pp. 1293–1302. doi: 10.1242/jcs.016998.   edoc | Open Access
Mesecke, N., Spang, A., Deponte, M. and Herrmann, J. M. (2008) “A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance”, Molecular Biology of the Cell. American Society for Cell Biology, 19(6), pp. 2673–2680. doi: 10.1091/mbc.E07-09-0896.   edoc | Open Access
Poon, P. P. and Spang, A. (2008) “Vesicular Transport : EnSNAREd by GAPs”, Current Biology. Cell Press, 18(22), pp. R1053-R1054. doi: 10.1016/j.cub.2008.10.002.   edoc
Dhonukshe, P., Grigoriev, I., Fischer, R., Tominaga, M., Robinson, D. G., Hasek, J., Paciorek, T., Petrasek, J., Seifertova, D., Tejos, R., Meisel, L. A., Zazimalova, E., Gadella, T. W. J. J., Stierhof, Y. .-D., Ueda, T., Oiwa, K., Akhmanova, A., Brock, R., Spang, A. and Friml, J. (2008) “Auxin transport inhibitors impair vesicle motility and actin cytoskeleton dynamics in diverse eukaryotes”, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 105(11), pp. 4489–4494. doi: 10.1073/pnas.0711414105.   edoc
Aguilera-Romero, A., Kaminska, J., Spang, A., Riezman, H. and Muniz, M. (2008) “The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus”, The Journal of cell biology. Rockefeller University Press, Vol. 180, H. 4, pp. 713–720. doi: 10.1083/jcb.200710025.   edoc | Open Access
Schindler, C. and Spang, A. (2007) “Interaction of SNAREs with ArfGAPs precedes recruitment of Sec18p/NSF”, Molecular Biology of the Cell. American Society for Cell Biology, 18(8), pp. 2852–2863. doi: 10.1091/mbc.E06-08-0756.   edoc | Open Access
Poteryaev, D., Fares, H., Bowerman, B. and Spang, A. (2007) “Caenorhabditis elegans SAND-1 is essential for RAB-7 function in endosomal traffic”, The EMBO Journal. Nature Publishing Group, 26(2), pp. 301–312. doi: 10.1038/sj.emboj.7601498.   edoc
Bembenek, J. N., Richie, C. T., Squirrell, J. M., Campbell, J. M., Eliceiri, K. W., Poteryaev, D., Spang, A., Golden, A. and White, J. G. (2007) “Cortical granule exocytosis in C. elegans is regulated by cell cycle components including separase”, Development. Company of Biologists, 134(21), pp. 3837–3848. doi: 10.1242/dev.011361.   edoc | Open Access
Michelsen, K., Schmid, V., Metz, J., Heusser, K., Liebel, U., Schwede, T., Spang, A. and Schwappach, B. (2007) “Novel cargo-binding site in the beta and delta subunits of coatomer”, The Journal of cell biology. Rockefeller University Press, Vol. 179, H. 2, pp. 209–217. doi: 10.1083/jcb.200704142.   edoc | Open Access
Schmutz, C., Stevens, J. and Spang, A. (2007) “Functions of the novel RhoGAP proteins RGA-3 and RGA-4 in the germ line and in the early embryo of C. elegans”, Development. Company of Biologists, 134(19), pp. 3495–3505. doi: 10.1242/dev.000802.   edoc | Open Access
Trautwein, M., Schindler, C., Gauss, R., Dengjel, J., Hartmann, E. and Spang, A. (2006) “Arf1p, Chs5p and the ChAPs are required for export of specialized cargo from the Golgi”, The EMBO Journal. Nature Publishing Group, 25(5), pp. 943–954. doi: 10.1038/sj.emboj.7601007.   edoc
Stavru, F., Hulsmann, B. B., Spang, A., Hartmann, E., Cordes, V. C. and Gorlich, D. (2006) “NDC1 : a crucial membrane-integral nucleoporin of metazoan nuclear pore complexes”, The Journal of cell biology. Rockefeller University Press, Vol. 173, H. 4, pp. 509–519. doi: 10.1083/jcb.200601001.   edoc | Open Access
Robinson, M., Poon, P. P., Schindler, C., Murray, L. E., Kama, R., Gabriely, G., Singer, R. A., Spang, A., Johnston, G. C. and Gerst, J. E. (2006) “The Gcs1 Arf-GAP mediates Snc1,2 v-SNARE retrieval to the Golgi in yeast”, Molecular Biology of the Cell. American Society for Cell Biology, 17(4), pp. 1845–1858. doi: 10.1091/mbc.E05-09-0832.   edoc | Open Access
Macara, I. G. and Spang, A. (2006) “Closing the GAP between polarity and vesicle transport”, Cell. Cell Press, 125(3), pp. 419–421. doi: 10.1016/j.cell.2006.04.011.   edoc
Forde, A. (2005) “Germany: deciphering cellular processes : [interview with A. Spang]”, Science. American Association for the Advancement of Science |, Vol. 310, no. 5747, pp. 519–520.   edoc
Gauss, R., Trautwein, M., Sommer, T. and Spang, A. (2005) “New modules for the repeated internal and N-terminal epitope tagging of genes in Saccharomyces cerevisiae”, Yeast. Wiley, 22(1), pp. 1–12. doi: 10.1002/yea.1187.   edoc
Schmutz, C. and Spang, A. (2005) “Knockdown of the centrosomal component SAS-5 results in defects in nuclear morphology in Caenorhabditis elegans”, European Journal of Cell Biology. Elsevier, 84(1), pp. 75–82. doi: 10.1016/j.ejcb.2004.10.004.   edoc
Weinberger, A., Kamena, F., Kama, R., Spang, A. and Gerst, J. E. (2005) “Control of Golgi morphology and function by Sed5 t-SNARE phosphorylation”, Molecular Biology of the Cell. American Society for Cell Biology, 16(10), pp. 4918–4930. doi: 10.1091/mbc.E05-02-0101.   edoc | Open Access
Wang, H., Spang, A., Sullivan, M. A., Hryhorenko, J. and Hagen, F. K. (2005) “The terminal phase of cytokinesis in the Caenorhabditis elegans early embryo requires protein glycosylation”, Molecular Biology of the Cell. American Society for Cell Biology, 16(9), pp. 4202–4213. doi: 10.1091/mbc.E05-05-0472.   edoc | Open Access
Poteryaev, D., Squirrell, J. M., Campbell, J. M., White, J. G. and Spang, A. (2005) “Involvement of the actin cytoskeleton and homotypic membrane fusion in ER dynamics in Caenorhabditis elegans”, Molecular Biology of the Cell. American Society for Cell Biology, 16(5), pp. 2139–2153. doi: 10.1091/mbc.E04-08-0726.   edoc | Open Access
Poteryaev, D. and Spang, A. (2005) “A role of SAND-family proteins in endocytosis”, Biochemical Society Transactions. Portland Press, 33(4), pp. 606–608. doi: 10.1042/BST0330606.   edoc
Luedeke, C., Frei, S. B., Sbalzarini, I., Schwarz, H., Spang, A. and Barral, Y. (2005) “Septin-dependent compartmentalization of the endoplasmic reticulum during yeast polarized growth”, The Journal of cell biology. Rockefeller University Press, Vol. 169, H. 6, pp. 897–908. doi: 10.1083/jcb.200412143.   edoc | Open Access
Kamena, F. and Spang, A. (2004) “Tip20p prohibits back-fusion of COPII vesicles with the endoplasmic reticulum”, Science. American Association for the Advancement of Science, 304(5668), pp. 286–289. doi: 10.1126/science.1095049.   edoc
Spang, A. (2004) “Vesicle transport : a close collaboration of Rabs and effectors”, Current Biology. Cell Press, 14(1), pp. R33-R34. doi: 10.1016/j.cub.2003.12.021.   edoc
Lewis, S. M., Poon, P. P., Singer, R. A., Johnston, G. C. and Spang, A. (2004) “The ArfGAP Glo3 is required for the generation of COPI vesicles”, Molecular Biology of the Cell. American Society for Cell Biology, 15(9), pp. 4064–4072. doi: 10.1091/mbc.E04-04-0316.   edoc | Open Access
Trautwein, M., Dengjel, J., Schirle, M. and Spang, A. (2004) “Arf1p provides an unexpected link between COPI vesicles and mRNA in Saccharomyces cerevisiae”, Molecular Biology of the Cell. American Society for Cell Biology, 15(11), pp. 5021–5037. doi: 10.1091/mbc.E04-05-0411.   edoc | Open Access
Sandmann, T., Herrmann, J. M., Dengjel, J., Schwarz, H. and Spang, A. (2003) “Suppression of coatomer mutants by a new protein family with COPI and COPII binding motifs in Saccharomyces cerevisiae”, Molecular Biology of the Cell. American Society for Cell Biology, 14(8), pp. 3097–3113. doi: 10.1091/mbc.E02-11-0736.   edoc | Open Access
Spang, A. (2002) “ARF1 regulatory factors and COPI vesicle formation”, Current Opinion in Cell Biology. Elsevier, 14(4), pp. 423–427. doi: 10.1016/S0955-0674(02)00346-0.   edoc
Rein, U., Andag, U., Duden, R., Schmitt, H. D. and Spang, A. (2002) “ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat”, The Journal of cell biology. Rockefeller University Press, Vol. 157, H. 3, pp. 395–404. doi: 10.1083/jcb.200112092.   edoc | Open Access
Spang, A. (2001) “Hefe und Wurm : Ebenbilder des Menschen?”, BIOforum, 7/8, pp. 498–499.   edoc
Spang, A., Herrmann, J. M., Hamamoto, S. and Schekman, R. (2001) “The ADP ribosylation factor-nucleotide exchange factors Gea1p and Gea2p have overlapping, but not redundant functions in retrograde transport from the Golgi to the endoplasmic reticulum”, Molecular Biology of the Cell. American Society for Cell Biology, 12(4), pp. 1035–1045. doi: 10.1091/mbc.12.4.1035.   edoc | Open Access
Todorow, Z., Spang, A., Carmack, E., Yates, J. and Schekman, R. (2000) “Active recycling of yeast Golgi mannosyltransferase complexes through the endoplasmic reticulum”, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 97(25), pp. 13643–13648. doi: 10.1073/pnas.250472397.   edoc
Poon, P. P., Cassel, D., Spang, A., Rotman, M., Pick, E., Singer, R. A. and Johnston, G. C. (1999) “Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function”, The EMBO Journal. Nature Publishing Group, 18(3), pp. 555–564. doi: 10.1093/emboj/18.3.555.   edoc
Springer, S., Spang, A. and Schekman, R. (1999) “A primer on vesicle budding”, Cell. Cell Press, 97(2), pp. 145–148. doi: 10.1016/S0092-8674(00)80722-9.   edoc
Spang, A. and Schekman, R. (1998) “Reconstitution of retrograde transport from the Golgi to the ER in vitro”, Journal of Cell Biology. Rockefeller University Press, 143(3), pp. 589–599. doi: 10.1083/jcb.143.3.589.   edoc | Open Access
Spang, A., Matsuoka, K., Hamamoto, S., Schekman, R. and Orci, L. (1998) “Coatomer, Arf1p, and nucleotide are required to bud coat protein complex I-coated vesicles from large synthetic liposomes”, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 95(19), pp. 11199–11204. doi: 10.1073/pnas.95.19.11199.   edoc
Wiech, H., Geier, B. M., Paschke, T., Spang, A., Grein, K., Steinkotter, J., Melkonian, M. and Schiebel, E. (1996) “Characterization of green alga, yeast, and human centrins : Specific subdomain features determine functional diversity”, Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology, 271(37), pp. 22453–22461. doi: 10.1074/jbc.271.37.22453.   edoc | Open Access
Spang, A., Grein, K. and Schiebel, E. (1996) “The spacer protein Spc110p targets calmodulin to the central plaque of the yeast spindle pole body”, Journal of Cell Science. Company of Biologists, 109(9), pp. 2229–2237.   edoc | Open Access
Geissler, S., Pereira, G., Spang, A., Knop, M., Soues, S., Kilmartin, J. and Schiebel, E. (1996) “The spindle pole body component Spc98p interacts with the gamma-tubulin-like Tub4p of Saccharomyces cerevisiae at the sites of microtubule attachment”, The EMBO Journal. Nature Publishing Group, 15(15), pp. 3899–3911. Available at:   edoc
Spang, A., Geissler, S., Grein, K. and Schiebel, E. (1996) “gamma-Tubulin-like Tub4p of Saccharomyces cerevisiae is associated with the spindle pole body substructures that organize microtubules and is required for mitotic spindle formation”, Journal of Cell Biology. Rockefeller University Press, 134(2), pp. 429–441. doi: 10.1083/jcb.134.2.429.   edoc | Open Access
Spang, A., Courtney, I., Grein, K., Matzner, M. and Schiebel, E. (1995) “The Cdc31p-binding protein Kar1p is a component of the half bridge of the yeast spindle pole body”, Journal of Cell Biology. Rockefeller University Press, 128(5), pp. 863–877. doi: 10.1083/jcb.128.5.863.   edoc | Open Access
Spang, A., Courtney, I., Fackler, U., Matzner, M. and Schiebel, E. (1993) “The calcium-binding protein cell division cycle 31 of Saccharomyces cerevisiae is a component of the half bridge of the spindle pole body”, Journal of Cell Biology. Rockefeller University Press, 123(2), pp. 405–416. doi: 10.1083/jcb.123.2.405.   edoc | Open Access
Rouille, Y., Spang, A., Chauvet, J. and Acher, R. (1992) “A neurosecretory granule Lys-Arg Ca(2+)-dependent endopeptidase putatively involved in prooxytocin and provasopressin processing”, Neuropeptides. Churchill Livingstone, 22(4), pp. 223–228. doi: 10.1016/0143-4179(92)90050-7.   edoc
Rouille, Y., Spang, A., Chauvet, J. and Acher, R. (1992) “Evidence for distinct dibasic processing endopeptidases with Lys-Arg and Arg-Arg specificities in neurohypophysial secretory granules”, Biochemical and Biophysical Research Communications. Elsevier, 183(1), pp. 128–137. doi: 10.1016/0006-291X(92)91618-Z.   edoc
Chauvet, J., Rouille, Y., Spang, A., Cardine, A. M. and Acher, R. (1992) “Processing endopeptidase deficiency in neurohypophysial secretory granules of the diabetes insipidus (Brattleboro) rat”, Bioscience Reports. The Biochemical Society, 12(6), pp. 445–451. doi: 10.1007/BF01122032.   edoc | Open Access