Article
Structure-based humanization of a therapeutic antibody for multiple myeloma.
Marino, S.F. and Daumke, O.
Journal of Molecular Medicine 102
(9): 1151-1161.
September 2024
Structural characterization of Thogoto Virus nucleoprotein provides insights into viral RNA encapsidation and RNP assembly.
Dick, A., Mikirtumov, V., Fuchs, J., Krupp, F., Olal, D., Bendl, E., Sprink, T., Diebolder, C., Kudryashev, M., Kochs, G., Roske, Y. and Daumke, O.
Structure 32
(8): 1068-1078.
8 August 2024
Identification of drug-like molecules targeting the ATPase activity of dynamin-like EHD4.
Mohd, S., Oder, A., Specker, E., Neuenschwander, M., von Kries, J.P. and Daumke, O.
PLoS ONE 19
(7): e0302704.
29 July 2024
Pathogenic mutations of human phosphorylation sites affect protein–protein interactions.
Rrustemi, T., Meyer, K., Roske, Y., Uyar, B., Akalin, A., Imami, K., Ishihama, Y., Daumke, O. and Selbach, M.
Nature Communications 15
(1): 3146.
11 April 2024
Structural insights into the activation mechanism of antimicrobial GBP1.
Weismehl, M., Chu, X., Kutsch, M., Lauterjung, P., Herrmann, C., Kudryashev, M. and Daumke, O.
EMBO Journal 43
(4): 615-636.
15 February 2024
GIMAP5 deficiency reveals a mammalian ceramide-driven longevity assurance pathway.
Park, A.Y., Leney-Greene, M., Lynberg, M., Gabrielski, J.Q., Xu, X., Schwarz, B., Zheng, L., Balasubramaniyam, A., Ham, H., Chao, B., Zhang, Y., Matthews, H.F., Cui, J., Yao, Y., Kubo, S., Chanchu, J.M., Morawski, A.R., Cook, S.A., Jiang, P., Ravell, J.C., Cheng, Y.H., George, A., Faruqi, A., Pagalilauan, A.M., Bergerson, J.R.E., Ganesan, S., Chauvin, S.D., Aluri, J., Edwards-Hicks, J., Bohrnsen, E., Tippett, C., Omar, H., Xu, L., Butcher, G.W., Pascall, J., Karakoc-Aydiner, E., Kiykim, A., Maecker, H., Tezcan, İ., Esenboga, S., Heredia, R.J., Akata, D., Tekin, S., Kara, A., Kuloglu, Z., Unal, E., Kendirli, T., Dogu, F., Karabiber, E., Atkinson, T.P., Cochet, C., Filhol, O., Bosio, C.M., Davis, M.M., Lifton, R.P., Pearce, E.L., Daumke, O., Aytekin, C., Şahin, G.E., Aksu, A.Ü., Uzel, G., Koneti Rao, V., Sari, S., Boztug, K., Cagdas, D., Haskologlu, S., Ikinciogullari, A., Schwefel, D., Vilarinho, S., Baris, S., Ozen, A., Su, H.C. and Lenardo, M.J.
Nature Immunology 25
(2): 282-293.
February 2024
Structural analysis of PLD3 reveals insights into the mechanism of lysosomal 5' exonuclease-mediated nucleic acid degradation.
Roske, Y., Cappel, C., Cremer, N., Hoffmann, P., Koudelka, T., Tholey, A., Heinemann, U., Daumke, O. and Damme, M.
Nucleic Acids Research 52
(1): 370-384.
11 January 2024
Topological reaction coordinate captures the folding transition state ensemble in a pierced lasso protein.
Noel, J.K. and Haglund, E.
Journal of Physical Chemistry B 128
(1): 117-124.
11 January 2024
Transcriptional reprogramming by mutated IRF4 in lymphoma.
Schleussner, N., Cauchy, P., Franke, V., Giefing, M., Fornes, O., Vankadari, N., Assi, S.A., Costanza, M., Weniger, M.A., Akalin, A., Anagnostopoulos, I., Bukur, T., Casarotto, M.G., Damm, F., Daumke, O., Edginton-White, B., Gebhardt, J.C.M., Grau, M., Grunwald, S., Hansmann, M.L., Hartmann, S., Huber, L., Kärgel, E., Lusatis, S., Noerenberg, D., Obier, N., Pannicke, U., Fischer, A., Reisser, A., Rosenwald, A., Schwarz, K., Sundararaj, S., Weilemann, A., Winkler, W., Xu, W., Lenz, G., Rajewsky, K., Wasserman, W.W., Cockerill, P.N., Scheidereit, C., Siebert, R., Küppers, R., Grosschedl, R., Janz, M., Bonifer, C. and Mathas, S.
Nature Communications 14
(1): 6947.
7 November 2023
MHC-II dynamics are maintained in HLA-DR allotypes to ensure catalyzed peptide exchange.
Abualrous, E.T., Stolzenberg, S., Sticht, J., Wieczorek, M., Roske, Y., Günther, M., Dähn, S., Boesen, B.B., Calvo, M.M., Biese, C., Kuppler, F., Medina-García, Á., Álvaro-Benito, M., Höfer, T., Noé, F. and Freund, C.
Nature Chemical Biology 19
(10): 1196-1204.
October 2023
A multimorphic mutation in IRF4 causes human autosomal dominant combined immunodeficiency.
Fornes, O., Jia, A., Kuehn, H.S., Min, Q., Pannicke, U., Schleussner, N., Thouenon, R., Yu, Z., de Los Angeles Astbury, M., Biggs, C.M., Galicchio, M., Garcia-Campos, J.A., Gismondi, S., Gonzalez Villarreal, G., Hildebrand, K.J., Hönig, M., Hou, J., Moshous, D., Pittaluga, S., Qian, X., Rozmus, J., Schulz, A.S., Staines-Boone, A.T., Sun, B., Sun, J., Uwe, S., Venegas-Montoya, E., Wang, W., Wang, X., Ying, W., Zhai, X., Zhou, Q., Akalin, A., André, I., Barth, T.F.E., Baumann, B., Brüstle, A., Burgio, G., Bustamante, J.C., Casanova, J.L., Casarotto, M.G., Cavazzana, M., Chentout, L., Cockburn, I.A., Costanza, M., Cui, C., Daumke, O., Del Bel, K.L., Eibel, H., Feng, X., Franke, V., Gebhardt, J.C.M., Götz, A., Grunwald, S., Hoareau, B., Hughes, T.R., Jacobsen, E.M., Janz, M., Jolma, A., Lagresle-Peyrou, C., Lai, N., Li, Y., Lin, S., Lu, H.Y., Lugo-Reyes, S.O., Meng, X., Möller, P., Moreno-Corona, N., Niemela, J.E., Novakovsky, G., Perez-Caraballo, J.J., Picard, C., Poggi, L., Puig-Lombardi, M.E., Randall, K.L., Reisser, A., Schmitt, Y., Seneviratne, S., Sharma, M., Stoddard, J., Sundararaj, S., Sutton, H., Tran, L.Q., Wang, Y., Wasserman, W.W., Wen, Z., Winkler, W., Xiong, E., Yang, A.W.H., Yu, M., Zhang, L., Zhang, H., Zhao, Q., Zhen, X., Enders, A., Kracker, S., Martinez-Barricarte, R., Mathas, S., Rosenzweig, S.D., Schwarz, K., Turvey, S.E. and Wang, J.Y.
Science Immunology 8
(79): eade7953.
January 2023
Development of selective inhibitors of phosphatidylinositol 3-kinase C2α.
Lo, W.T., Belabed, H., Kücükdisli, M., Metag, J., Roske, Y., Prokofeva, P., Ohashi, Y., Horatscheck, A., Cirillo, D., Krauss, M., Schmied, C., Neuenschwander, M., von Kries, J.P., Médard, G., Kuster, Be., Perisic, O., Williams, R.L., Daumke, O., Payrastre, B., Severin, S., Nazaré, M. and Haucke, V.
Nature Chemical Biology 19
(1): 18-27.
January 2023
Cryo-electron tomography reveals structural insights into the membrane remodeling mode of dynamin-like EHD filaments.
Melo, A.A., Sprink, T., Noel, J.K., Vázquez-Sarandeses, E., van Hoorn, C., Mohd, S., Loerke, J., Spahn, C.M.T. and Daumke, O.
Nature Communications 13
(1): 7641.
10 December 2022
Structural insights into crista junction formation by the Mic60-Mic19 complex.
Bock-Bierbaum, T., Funck, K., Wollweber, F., Lisicki, E., von der Malsburg, K., von der Malsburg, A., Laborenz, J., Noel, J.K., Hessenberger, M., Jungbluth, S., Bernert, C., Kunz, S., Riedel, D., Lilie, H., Jakobs, S., van der Laan, M. and Daumke, O.
Science Advances 8
(35): eabo4946.
2 September 2022
GIMAP6 regulates autophagy, immune competence, and inflammation in mice and humans.
Yao, Y., Du Jiang, P., Chao, B.N., Cagdas, D., Kubo, S., Balasubramaniyam, A., Zhang, Y., Shadur, B., NaserEddin, A., Folio, L.R., Schwarz, B., Bohrnsen, E., Zheng, L., Lynberg, M., Gottlieb, S., Leney-Greene, M.A., Park, A.Y., Tezcan, I., Akdogan, A., Gocmen, R., Onder, S., Rosenberg, A., Soilleux, E.J., Johnson, E., Jackson, P.K., Demeter, J., Chauvin, S.D., Paul, F., Selbach, M., Bulut, H., Clatworthy, M.R., Tuong, Z.K., Zhang, H., Stewart, B.J., Bosio, C.M., Stepensky, P., Clare, S., Ganesan, S., Pascall, J.C., Daumke, O., Butcher, G.W., McMichael, A.J., Simon, A.K. and Lenardo, M.J.
Journal of Experimental Medicine 219
(6): e20201405.
6 June 2022
Competitively disrupting the neutrophil-specific receptor-autoantigen CD177:proteinase 3 membrane complex reduces anti-PR3 antibody-induced neutrophil activation.
Marino, S.F., Jerke, U., Rolle, S., Daumke, O. and Kettritz, R.
Journal of Biological Chemistry 298
(3): 101598.
March 2022
Structural basis of phosphatidylinositol 3-kinase C2α function.
Lo, W.T., Zhang, Y., Vadas, O., Roske, Y., Gulluni, F., De Santis, M.C., Zagar, A.V., Stephanowitz, H., Hirsch, E., Liu, F., Daumke, O., Kudryashev, M. and Haucke, V.
Nature Structural & Molecular Biology 29
(3): 218-228.
March 2022
SMOG 2 and OpenSMOG: extending the limits of structure-based models.
de Oliveira, A.B., Contessoto, V.G., Hassan, A., Byju, S., Wang, A., Wang, Y., Dodero-Rojas, E., Mohanty, U., Noel, J.K., Onuchic, J.N. and Whitford, P.C.
Protein Science 31
(1): 158-172.
January 2022
Lysine acetylation regulates the interaction between proteins and membranes.
Okada, A.K., Teranishi, K., Ambroso, M.R., Isas, J.M., Vazquez-Sarandeses, E., Lee, J.Y., Melo, A.A., Pandey, P., Merken, D., Berndt, L., Lammers, M., Daumke, O., Chang, K., Haworth, I.S. and Langen, R.
Nature Communications 12
(1): 6466.
9 November 2021
A simple pressure-assisted method for MicroED specimen preparation.
Zhao, J., Xu, H., Lebrette, H., Carroni, M., Taberman, H., Högbom, M. and Zou, X.
Nature Communications 12
(1): 5036.
19 August 2021
Quantification and demonstration of the collective constriction-by-ratchet mechanism in the dynamin molecular motor.
Ganichkin, O.M., Vancraenenbroeck, R., Rosenblum, G., Hofmann, H., Mikhailov, A.S., Daumke, O. and Noel, J.K.
Proceedings of the National Academy of Sciences of the United States of America 118
(28): e2101144118.
13 July 2021
Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily.
Liu, J., Tassinari, M., Souza, D.P., Naskar, S., Noel, J.K., Bohuszewicz, O., Buck, M., Williams, T.A., Baum, B. and Low, H.H.
Cell 184
(14): 3660-3673.
8 July 2021
The ARFRP1-dependent Golgi scaffolding protein GOPC is required for insulin secretion from pancreatic β-cells.
Wilhelmi, Ilka, Grunwald, S., Gimber, N., Popp, O., Dittmar, G., Arumughan, A., Wanker, E.E., Laeger, T., Schmoranzer, J., Daumke, O. and Schümann, A.
Molecular Metabolism 45
: 101151.
March 2021
Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates.
Grunwald, S., Hopf, L.V.M., Bock-Bierbaum, T., Lally, C.C.M., Spahn, C.M.T. and Daumke, O.
Nature Communications 11
(1): 5506.
2 November 2020
Monogenic variants in dystonia: an exome-wide sequencing study.
Zech, M., Jech, R., Boesch, S., Škorvánek, M., Weber, S., Wagner, M., Zhao, C., Jochim, A., Necpál, J., Dincer, Y., Vill, K., Distelmaier, F., Stoklosa, M., Krenn, M., Grunwald, S., Bock-Bierbaum, T., Fečíková, A., Havránková, P., Roth, J., Příhodová, I., Adamovičová, M., Ulmanová, O., Bechyně, K., Danhofer, P., Veselý, B., Haň, V., Pavelekova, P., Gdovinová, Z., Mantel, T., Meindl, T., Sitzberger, A., Schröder, S., Blaschek, A., Roser, T., Bonfert, M.V., Haberlandt, E., Plecko, B., Leineweber, B., Berweck, S., Herberhold, T., Langguth, B., Švantnerová, J., Minár, M., Ramos-Rivera, G.A., Wojcik, M.H., Pajusalu, S., Õunap, K., Schatz, U.A., Pölsler, L., Milenkovic, I., Laccone, F., Pilshofer, V., Colombo, R., Patzer, S., Iuso, A., Vera, J., Troncoso, M., Fang, F., Prokisch, H., Wilbert, F., Eckenweiler, M., Graf, E., Westphal, D.S., Riedhammer, K.M., Brunet, T., Alhaddad, B., Berutti, R., Strom, T.M., Hecht, M., Baumann, M., Wolf, M., Telegrafi, A., Person, R.E., Zamora, F.M., Henderson, L.B., Weise, D., Musacchio, T., Volkmann, J., Szuto, A., Becker, J., Cremer, K., Sycha, T., Zimprich, F., Kraus, V., Makowski, C., Gonzalez-Alegre, P., Bardakjian, T.M., Ozelius, L.J., Vetro, A., Guerrini, R., Maier, E., Borggraefe, I., Kuster, A., Wortmann, S.B., Hackenberg, A., Steinfeld, R., Assmann, B., Staufner, C., Opladen, T., Růžička, E., Cohn, R.D., Dyment, D., Chung, W.K., Engels, H., Ceballos-Baumann, A., Ploski, R., Daumke, O., Haslinger, B., Mall, V., Oexle, K. and Winkelmann, J.
Lancet Neurology 19
(11): 908-918.
November 2020
hGBP1 coordinates chlamydia restriction and inflammasome activation through sequential GTP hydrolysis.
Xavier, A., Al-Zeer, M.A., Meyer, T.F. and Daumke, O.
Cell Reports 31
(7): 107667.
19 May 2020
The pierced lasso topology leptin has a bolt on dynamic domain composed by the disordered loops I and III.
Danielsson, J., Noel, J.K., Simien, J.M., Duggan, B.M., Oliveberg, M., Onuchic, J.N., Jennings, P.A. and Haglund, E.
Journal of Molecular Biology 432
(9): 3050-3063.
17 April 2020
Age attenuates the T-type Ca(V) 3.2-RyR axis in vascular smooth muscle.
Fan, G., Kaßmann, M., Cui, Y., Matthaeus, C., Kunz, S., Zhong, C., Zhu, S., Xie, Yu, Tsvetkov, D., Daumke, O., Huang, Yu and Gollasch, M.
Aging Cell 19
(4): e13134.
April 2020
EHD2-mediated restriction of caveolar dynamics regulates cellular fatty acid uptake.
Matthaeus, C., Lahmann, I., Kunz, S., Jonas, W., Melo, A.A., Lehmann, M., Larsson, E., Lundmark, R., Kern, M., Blüher, M., Olschowski, H., Kompa, J., Brügger, B., Müller, D.N., Haucke, V., Schürmann, A., Birchmeier, C. and Daumke, O.
Proceedings of the National Academy of Sciences of the United States of America 117
(13): 7471-7481.
31 March 2020
Polymer-like model to study the dynamics of dynamin filaments on deformable membrane tubes.
Noel, J.K., Noé, F., Daumke, O. and Mikhailov, A.S.
Biophysical Journal 117
(10): 1870-1891.
19 November 2019
eNOS-NO-induced small blood vessel relaxation requires EHD2-dependent caveolae stabilization.
Matthaeus, C., Lian, X., Kunz, S., Lehmann, M., Zhong, C., Bernert, C., Lahmann, I., Müller, D.N., Gollasch, M. and Daumke, O.
PLoS ONE 14
(10): e0223620.
10 October 2019
53BP1 supports immunoglobulin class switch recombination independently of its DNA double-strand break end protection function.
Sundaravinayagam, D., Rahjouei, A., Andreani, M., Tupiņa, D., Balasubramanian, S., Saha, T., Delgado-Benito, V., Coralluzzo, V., Daumke, O. and Di Virgilio, M.
Cell Reports 28
(6): 1389-1399.
6 August 2019
Structure and assembly of the mitochondrial membrane remodelling GTPase Mgm1.
Faelber, K., Dietrich, L., Noel, J.K., Wollweber, F., Pfitzner, A.K., Mühleip, A., Sánchez, R., Kudryashev, M., Chiaruttini, N., Lilie, H., Schlegel, J., Rosenbaum, E., Hessenberger, M., Matthaeus, C., Kunz, S., von der Malsburg, A., Noé, F., Roux, A., van der Laan, M., Kühlbrandt, W. and Daumke, O.
Nature 571
(7765): 429-433.
18 July 2019
Studying ribosome dynamics with simplified models.
Levi, M., Noel, J.K. and Whitford, P.C.
Methods 162-163
: 128-140.
1 June 2019
FIP200 claw domain binding to p62 promotes autophagosome formation at ubiquitin condensates.
Turco, E., Witt, M., Abert, C., Bock-Bierbaum, T., Su, M.Y., Trapannone, R., Sztacho, M., Danieli, A., Shi, X., Zaffagnini, G., Gamper, A., Schuschnig, M., Fracchiolla, D., Bernklau, D., Romanov, J., Hartl, M., Hurley, J.H., Daumke, O. and Martens, S.
Molecular Cell 74
(2): 330-346.
18 April 2019
Autocrine LTA signaling drives NF-κB and JAK-STAT activity and myeloid gene expression in Hodgkin lymphoma.
von Hoff, L., Kärgel, E., Franke, V., McShane, E., Schulz-Beiss, K.W., Patone, G., Schleussner, N., Kolesnichenko, M., Hübner, N., Daumke, O., Selbach, M., Akalin, A., Mathas, S. and Scheidereit, C.
Blood 133
(13): 1489-1494.
28 March 2019
A SEPT1-based scaffold is required for Golgi integrity and function.
Song, K., Gras, C., Capin, G., Gimber, N., Lehmann, M., Mohd, S., Puchkov, D., Rödiger, M., Wilhelmi, I., Daumke, O., Schmoranzer, J., Schürmann, A. and Krauss, M.
Journal of Cell Science 132
(3): jcs225557.
1 February 2019
Using SMOG 2 to simulate complex biomolecular assemblies.
Levi, M., Bandarkar, P., Yang, H., Wang, A., Mohanty, U., Noel, J.K. and Whitford, P.C.
Methods in Molecular Biology 2022
: 129-151.
2019
Atomistic simulations indicate the functional loop-to-coiled-coil transition in influenza hemagglutinin is not downhill.
Lin, X., Noel, J.K., Wang, Q., Ma, J. and Onuchic, J.N.
Proceedings of the National Academy of Sciences of the United States of America 115
(34): E7905-E7913.
21 August 2018
Structural basis for membrane tethering by a bacterial dynamin-like pair.
Liu, J., Noel, J.K. and Low, H.H.
Nature Communications 9
(1): 3345.
21 August 2018
Effects of allelic variations in the human myxovirus resistance protein A on its antiviral activity.
Graf, L., Dick, A., Sendker, F., Barth, E., Marz, M., Daumke, O. and Kochs, G.
Journal of Biological Chemistry 293
(9): 3056-3072.
2 March 2018
An AKAP-Lbc-RhoA interaction inhibitor promotes the translocation of aquaporin-2 to the plasma membrane of renal collecting duct principal cells.
Schrade, K., Tröger, J., Eldahshan, A., Zühlke, K., Abdul Azeez, K.R., Elkins, J.M., Neuenschwander, M., Oder, A., Elkewedi, M.M.H., Jaksch, S., Andrae, K., Li, J., Fernandes, J., Müller, P.M., Grunwald, S., Marino, S.F., Vukićević, T., Eichhorst, J., Wiesner, B., Weber, M., Kapiloff, M., Rocks, O., Daumke, O., Wieland, T., Knapp, S., von Kries, J.P. and Klussmann, E.
PLoS ONE 13
(1): e0191423.
26 January 2018
Anisotropic fluctuations in the ribosome determine tRNA kinetics.
Yang, H., Noel, J.K. and Whitford, P.C.
Journal of Physical Chemistry B 121
(47): 10593-10601.
30 November 2017
Molecular simulations suggest a force-dependent mechanism of vinculin activation.
Sun, L., Noel, J.K., Levine, H. and Onuchic, J.N.
Biophysical Journal 113
(8): 1697-1710.
17 October 2017
Cryo-EM studies of Drp1 reveal cardiolipin interactions that activate the helical oligomer.
Francy, C.A., Clinton, R.W., Froehlich, C., Murphy, C. and Mears, J.A.
Scientific Reports 7
(1): 10744.
6 September 2017
Chlamydia trachomatis prevents apoptosis via activation of PDPK1-MYC and enhanced mitochondrial binding of hexokinase II.
Al-Zeer, M.A., Xavier, A., Abu Lubad, M., Sigulla, J., Kessler, M., Hurwitz, R. and Meyer, T.F.
EBioMedicine 23
: 100-110.
September 2017
Structural basis for aryl hydrocarbon receptor-mediated gene activation.
Schulte, K.W., Green, E., Wilz, A., Platten, M. and Daumke, O.
Structure 25
(7): 1025-1033.
5 July 2017
Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions.
Hessenberger, M., Zerbes, R.M., Rampelt, H., Kunz, S., Xavier, A.H., Purfürst, B., Lilie, H., Pfanner, N., van der Laan, M. and Daumke, O.
Nature Communications 8
: 15258.
31 May 2017
Structural insights into the activation mechanism of dynamin-like EHD ATPases.
Melo, A.A., Hegde, B.G., Shah, C., Larsson, E., Isas, J.M., Kunz, S., Lundmark, R., Langen, R. and Daumke, O.
Proceedings of the National Academy of Sciences of the United States of America 114
(22): 5629-5634.
30 May 2017
Characterization of the CD177 interaction with the ANCA antigen proteinase 3.
Jerke, U., Marino, S.F., Daumke, O. and Kettritz, R.
Scientific Reports 7
: 43328.
27 February 2017
Quantitative GTPase affinity purification identifies Rho family protein interaction partners.
Paul, F., Zauber, H., von Berg, L., Rocks, O., Daumke, O. and Selbach, M.
Molecular & Cellular Proteomics 16
(1): 73-85.
1 January 2017
How EF-Tu can contribute to efficient proofreading of aa-tRNA by the ribosome.
Noel, J.K. and Whitford, P.C.
Nature Communications 7
: 13314.
31 October 2016
Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers.
Arumughan, A., Roske, Y., Barth, C., Lleras Forero, L., Bravo-Rodriguez, K., Redel, Al., Kostova, S., McShane, E., Opitz, R., Faelber, K., Rau, K., Mielke, T., Daumke, O., Selbach, M., Sanchez-Garcia, E., Rocks, O., Panáková, D., Heinemann, U. and Wanker, E.E.
Nature Communications 7
: 13047.
20 October 2016
Bimodal antagonism of PKA signalling by ARHGAP36.
Eccles, R.L., Czajkowski, M.T., Barth, C., Müller, P.M., McShane, E., Grunwald, S., Beaudette, P., Mecklenburg, N., Volkmer, R., Zühlke, K., Dittmar, G., Selbach, M., Hammes, A., Daumke, O., Klussmann, E., Urbé, S. and Rocks, O.
Nature Communications 7
: 12963.
7 October 2016
Lowered pH leads to fusion peptide release and a highly dynamic intermediate of influenza hemagglutinin.
Lin, X.C., Noel, J.K., Wang, Q.H., Ma, J.P. and Onuchic, J.N.
Journal of Physical Chemistry B 120
(36): 9654-9660.
15 September 2016
AKAP18:PKA-RIIα structure reveals crucial anchor points for recognition of regulatory subunits of PKA.
Götz, F., Roske, Y., Schulz, M.S., Autenrieth, K., Bertinetti, D., Faelber, K., Zühlke, K., Kreuchwig, A., Kennedy, E., Krause, G., Daumke, O., Herberg, F.W., Heinemann, U. and Klussmann, E.
Biochemical Journal 473
(13): 1881-1894.
28 June 2016
SMOG 2: A versatile software package for generating structure-based models.
Noel, J.K., Levi, M., Raghunathan, M., Lammert, H., Hayes, R.L., Onuchic, J.N. and Whitford, P.C.
PLoS Computational Biology 12
(3): e1004794.
10 March 2016
Structure of the hantavirus nucleoprotein provides insights into the mechanism of RNA encapsidation.
Olal, D. and Daumke, O.
Cell Reports 14
(9): 2092-2099.
8 March 2016
The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashion.
Schulte, K., Pawlowski, N., Faelber, K., Fröhlich, C., Howard, J. and Daumke, O.
BMC Biology 14
(1): 14.
2 March 2016
A complex water network contributes to high-affinity binding in an antibody-antigen interface.
Marino, S.F., Olal, D. and Daumke, O.
Data in Brief 6
: 394-397.
March 2016
Dynamics of the ligand binding domain layer during AMPA receptor activation.
Baranovic, J., Chebli, M., Salazar, H., Carbone, A.L., Faelber, K., Lau, A.Y., Daumke, O. and Plested, A.J.R.
Biophysical Journal 110
(4): 896-911.
23 February 2016
Crystal structure of the dynamin tetramer.
Reubold, T.F., Faelber, K., Plattner, N., Posor, Y., Ketel, K., Curth, U., Schlegel, J., Anand, R., Manstein, D.J., Noé, F., Haucke, V., Daumke, O. and Eschenburg, S.
Nature 525
(7569): 404-408.
17 September 2015
Phosphorylation of PACSIN2 by protein kinase C triggers the removal of caveolae from the plasma membrane.
Senju, Y., Rosenbaum, E., Shah, C., Hamada-Nakahara, S., Itoh, Y., Yamamoto, K., Hanawa-Suetsugu, K., Daumke, O. and Suetsugu, S.
Journal of Cell Science 128
(15): 2766-2780.
1 August 2015
Potent anti-tumor response by targeting B cell maturation antigen (BCMA) in a mouse model of multiple myeloma.
Oden, F., Marino, S.F., Brand, J., Scheu, S., Kriegel, C., Olal, D., Takvorian, A., Westermann, J., Yilmaz, B., Hinz, M., Daumke, O., Höpken, U.E., Müller, G. and Lipp, M.
Molecular Oncology 9
(7): 1348-1358.
August 2015
New role for the (pro)renin receptor in T cell development.
Geisberger, S., Maschke, U., Gebhardt, M., Kleinewietfeld, M., Manzel, A., Linker, R.A., Chidgey, A., Dechend, R., Nguyen, G., Daumke, O., Muller, D.N., Wright, M.D. and Binger, K.J.
Blood 126
(4): 504-507.
23 July 2015
Role of nucleotide binding and GTPase domain dimerization in dynamin-like myxovirus resistance protein A for GTPase activation and antiviral activity.
Dick, A., Graf, L., Olal, D., von der Malsburg, A., Gao, S., Kochs, G. and Daumke, O.
Journal of Biological Chemistry 290
(20): 12779-12792.
15 May 2015
Roquin binding to target mRNAs involves a winged helix-turn-helix motif.
Schuetz, A., Murakawa, Y., Rosenbaum, E., Landthaler, M. and Heinemann, U.
Nature Communications 5
: 5701.
11 December 2014
Structural insights into RNA encapsidation and helical assembly of the Toscana virus nucleoprotein.
Olal, D., Dick, A., Woods, V.L., Liu, T., Li, S., Devignot, S., Weber, F., Saphire, E.O. and Daumke, O.
Nucleic Acids Research 42
(9): 6025-6037.
14 May 2014
Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2.
Shah, C., Hegde, B.G., Morén, B., Behrmann, E., Mielke, T., Moenke, G., Spahn, C.M., Lundmark, R., Daumke, O. and Langen, R.
Structure 22
(3): 409-420.
4 March 2014
Functional mapping of human dynamin-1-like GTPase domain based on X-ray structure analyses.
Wenger, J., Klinglmayr, E., Fröhlich, C., Eibl, C., Gimeno, A., Hessenberger, M., Puehringer, S., Daumke, O. and Goettig, P.
PLoS ONE 8
(8): e71835.
19 August 2013
Structural insights into oligomerization and mitochondrial remodelling of dynamin 1-like protein.
Fröhlich, C., Grabiger, S., Schwefel, D., Faelber, K., Rosenbaum, E., Mears, J., Rocks, O. and Daumke, O.
EMBO Journal 32
(9): 1280-1292.
2 May 2013
Structural insights into the mechanism of GTPase activation in the GIMAP family.
Schwefel, D., Arasu, B.S., Marino, S.F., Lamprecht, B., Köchert, K., Rosenbaum, E., Eichhorst, J., Wiesner, B., Behlke, J., Rocks, O., Mathas, S. and Daumke, O.
Structure 21
(4): 550-559.
2 April 2013
Sarcolemmal repair is a slow process and includes EHD2.
Marg, A., Schoewel, V., Timmel, T., Schulze, A., Shah, C., Daumke, O. and Spuler, S.
Traffic 13
(9): 1286-1294.
September 2012
A stomatin dimer modulates the activity of acid-sensing ion channels.
Brand, J., Smith, E.S.J., Schwefel, D., Lapatsina, L., Poole, K., Omerbasic, D., Kozlenkov, A., Behlke, J., Lewin, G.R. and Daumke, O.
EMBO Journal 31
(17): 3635-3646.
29 August 2012
EHD2 regulates caveolar dynamics via ATP-driven targeting and oligomerization.
Moren, B., Shah, C., Howes, M.T., Schieber, N.L., McMahon, H.T., Parton, R.G., Daumke, O. and Lundmark, R.
Molecular Biology of the Cell 23
(7): 1316-1329.
9 February 2012
Structure of myxovirus resistance protein A reveals intra- and intermolecular domain interactions required for the antiviral function.
Gao, S., von der Malsburg, A., Dick, A., Faelber, K., Schroeder, G.F., Haller, O., Kochs, G. and Daumke, O.
Immunity 35
(4): 514-525.
28 October 2011
Crystal structure of nucleotide-free dynamin.
Faelber, K., Posor, Y., Gao, S., Held, M., Roske, Y., Schulze, D., Haucke, V., Noe, F. and Daumke, O.
Nature 477
(7366): 556-560.
29 September 2011
Crystal structures of the bacterial solute receptor AcbH displaying an exclusive substrate preference for beta-D-galactopyranose.
Licht, A., Bulut, H., Scheffel, F.M., Daumke, O., Wehmeier, U.F., Saenger, W., Schneider, E. and Vahedi-Faridi, A.
Journal of Molecular Biology 406
(1): 92-105.
11 February 2011
GTP-dependent scaffold formation in the GTPase of Immunity Associated Protein family.
Schwefel, D. and Daumke, O.
Small GTPases 2
(1): 27-30.
January 2011
Structure of a classical MHC class I molecule that binds "non-classical" ligands.
Hee, C.S., Gao, S., Loll, B., Miller, M.M., Uchanska-Ziegler, B., Daumke, O. and Ziegler, A.
PLoS Biology 8
(12): e1000557.
7 December 2010
Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2).
Schwefel, D., Froehlich, C., Eichhorst, J., Wiesner, B., Behlke, J., Aravind, L. and Daumke, O.
Proceedings of the National Academy of Sciences of the United States of America 107
(47): 20299-20304.
23 November 2010
Structure of the MxA stalk elucidates the assembly of ring-like units of an antiviral module.
Daumke, O., Gao, S., von der Malsburg, A., Haller, O. and Kochs, G.
Small GTPases 1
(1): 62-64.
July 2010
Purification, crystallization and preliminary X-ray analysis of human GIMAP2.
Schwefel, D., Froehlich, C. and Daumke, O.
Acta Crystallographica Section F 66
(6): 725-729.
1 June 2010
Structural basis of oligomerization in the stalk region of dynamin-like MxA.
Gao, S., von der Malsburg, A., Paeschke, S., Behlke, J., Haller, O., Kochs, G. and Daumke, O.
Nature 465
(7297): 502-506.
27 May 2010
Host cell interactome of tyrosine-phosphorylated bacterial proteins.
Selbach, M., Paul, F.E., Brandt, S., Guye, P., Daumke, O., Backert, S., Dehio, C. and Mann, M.
Cell Host & Microbe 5
(4): 397-403.
23 April 2009
Expression, purification and preliminary X-ray crystallographic analysis of the chicken MHC class I molecule YF1*7.1.
Hee, C.S., Gao, S., Miller, M.M., Goto, R.M., Ziegler, A., Daumke, O. and Uchanska-Ziegler, B.
Acta Crystallographica Section F 65
(Pt 4): 422-425.
1 April 2009
Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling.
Daumke, O., Lundmark, R., Vallis, Y., Martens, S., Butler, P.J.G. and McMahon, H.T.
Nature 449
(7164): 923-927.
3 October 2007
Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature.
Henne, W.M., Kent, H.M., Ford, M.G.J., Hegde, B.G., Daumke, O., Butler, P.J.G., Mittal, R., Langen, R., Evans, P.R. and McMahon, H.T.
Structure 15
(7): 839-52.
July 2007
Insight into catalysis of a unique GTPase reaction by a combined biochemical and FTIR approach.
Chakrabarti, P.P., Daumke, O., Suveyzdis, Y., Koetting, C., Gerwert, K. and Wittinghofer, A.
Journal of Molecular Biology 367
(4): 983-95.
6 April 2007
GAP1 family members constitute bifunctional Ras and Rap GTPase-activating proteins.
Kupzig, S., Deaconescu, D., Bouyoucef, D., Walker, S.A., Liu, Q., Polte, C.L., Daumke, O., Ishizaki, T., Lockyer, P.J., Wittinghofer, A. and Cullen, P.J.
Journal of Biological Chemistry 281
(15): 9891-900.
14 April 2006
Crystal structure of THEP1 from the hyperthermophile Aquifex aeolicus: a variation of the RecA fold.
Rossbach, M., Daumke, O., Klinger, C., Wittinghofer, A. and Kaufmann, M.
BMC Structural Biology 5
: 7.
20 March 2005
Synthesis of GTP-derived Ras ligands.
Soulère, L., Aldrich, C., Daumke, O., Gail, R., Kissau, L., Wittinghofer, A. and Waldmann, H.
ChemBioChem 5
(10): 1448-53.
4 October 2004
The GTPase-activating protein Rap1GAP uses a catalytic asparagine.
Daumke, O., Weyand, M., Chakrabarti, P.P., Vetter, I.R. and Wittinghofer, A.
Nature 429
(6988): 197-201.
13 May 2004
Purification, crystallization and preliminary structural characterization of human Rap1GAP.
Daumke, O., Wittinghofer, A. and Weyand, M.
Acta Crystallographica Section D : Structural Biology 60
(Pt 4): 752-4.
April 2004
Rap-specific GTPase activating protein follows an alternative mechanism.
Brinkmann, T., Daumke, O., Herbrand, U., Kühlmann, D., Stege, P., Ahmadian, M.R. and Wittinghofer, A.
Journal of Biological Chemistry 277
(15): 12525-31.
12 April 2002
Functional asymmetry of the ATP-binding-cassettes of the ABC transporter TAP is determined by intrinsic properties of the nucleotide binding domains.
Daumke, O. and Knittler, M.R.
European Journal of Biochemistry 268
(17): 4776-86.
September 2001
Distinct functional properties of the TAP subunits coordinate the nucleotide-dependent transport cycle.
Alberts, P., Daumke, O., Deverson, E.V., Howard, J.C. and Knittler, M.R.
Current Biology 11
(4): 242-51.
20 February 2001
Review
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition).
Klionsky, D.J., Abdel-Aziz, A.K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M.H., Abudu, Y.P., Acevedo-Arozena, A., Adamopoulos, I.E., Adeli, K., Adolph, T.E., Adornetto, A., Aflaki, E., Agam, G., Agarwal, A., Aggarwal, B.B., Agnello, M., Agostinis, P., Agrewala, J.N., Agrotis, A., Aguilar, P.V., Ahmad, S.T., Ahmed, Z.M., Ahumada-Castro, U., Aits, S., Aizawa, S., Akkoc, Y., Akoumianaki, T., Akpinar, H.A., Al-Abd, A.M., Al-Akra, L., Al-Gharaibeh, A., Alaoui-Jamali, M.A., Alberti, S., Alcocer-Gómez, E., Alessandri, C., Ali, M., Alim Al-Bari, M.A., Aliwaini, S., Alizadeh, J., Almacellas, E., Almasan, A., Alonso, A., Alonso, G.D., Altan-Bonnet, N., Altieri, D.C., Álvarez, E.M.C., Alves, S., Alves da Costa, C., Alzaharna, M.M., Amadio, M., Amantini, C., Amaral, C., Ambrosio, S., Amer, A.O., Ammanathan, V., An, Z., Andersen, S.U., Andrabi, S.A., Andrade-Silva, M., Andres, A.M., Angelini, S., Ann, D., Anozie, U.C., Ansari, M.Y., Antas, P., Antebi, A., Antón, Z., Anwar, T., Apetoh, L., Apostolova, N., Araki, T., Araki, Y., Arasaki, K., Araújo, W.L., Araya, J., Arden, C., Arévalo, M.A., Arguelles, S., Arias, E., Arikkath, J., Arimoto, H., Ariosa, A.R., Armstrong-James, D., Arnauné-Pelloquin, L., Aroca, A., Arroyo, D.S., Arsov, I., Artero, R., Asaro, D.M.L., Aschner, M., Ashrafizadeh, M., Ashur-Fabian, O., Atanasov, A.G., Au, A.K., Auberger, P., Auner, H.W., Aurelian, L., Autelli, R., Avagliano, L., Ávalos, Y., Aveic, S., Aveleira, C.A., Avin-Wittenberg, T., Aydin, Y., Ayton, S., Ayyadevara, S., Azzopardi, M., Baba, M.u, Backer, J.M., Backues, S.K., Bae, D.H., Bae, O.N., Bae, S.H., Baehrecke, E.H., Baek, A., Baek, S.H., Baek, S.H., Bagetta, G., Bagniewska-Zadworna, A., Bai, H., Bai, J., Bai, X., Bai, Y., Bairagi, N., Baksi, S., Balbi, T., Baldari, C.T., Balduini, W., Ballabio, A., Ballester, M., Balazadeh, S., Balzan, R., Bandopadhyay, R., Banerjee, S., Banerjee, S., Bánréti, A., Bao, Y., Baptista, M.S., Baracca, A., Barbati, C., Bargiela, A., Barilà, D., Barlow, P.G., Barmada, S.J., Barreiro, E., Barreto, G.E., Bartek, J., Bartel, B., Bartolome, A., Barve, G.R., Basagoudanavar, S.H., Bassham, D.C., Bast, R.C., Basu, A., Batoko, H., Batten, I., Baulieu, E.E., Baumgarner, B.L., Bayry, J., Beale, R., Beau, I., Beaumatin, F., Bechara, L.R.G., Beck, G.R., Beers, M.F., Begun, J., Behrends, C., Behrens, G.M.N., Bei, R., Bejarano, E., Bel, S., Behl, C., Belaid, A., Belgareh-Touzé, N., Bellarosa, C., Belleudi, F., Belló Pérez, M., Bello-Morales, R., Beltran, J.S.O., Beltran, S., Benbrook, D.M., Bendorius, M., Benitez, B.A., Benito-Cuesta, I., Bensalem, J., Berchtold, M.W., Berezowska, S., Bergamaschi, D., Bergami, M., Bergmann, A., Berliocchi, L., Berlioz-Torrent, C., Bernard, A., Berthoux, L., Besirli, C.G., Besteiro, S., Betin, V.M., Beyaert, R., Bezbradica, J.S., Bhaskar, K., Bhatia-Kissova, I., Bhattacharya, R., Bhattacharya, S., Bhattacharyya, S., Bhuiyan, M.S., Bhutia, S.K., Bi, L., Bi, X., Biden, T.J., Bijian, K., Billes, V.A., Binart, N., Bincoletto, C., Birgisdottir, A.B., Bjorkoy, G., Blanco, G., Blas-Garcia, A., Blasiak, J., Blomgran, R., Blomgren, K., Blum, J.S., Boada-Romero, E., Boban, M., Boesze-Battaglia, K., Boeuf, P., Boland, B., Bomont, P., Bonaldo, P., Bonam, S.R., Bonfili, L., Bonifacino, J.S., Boone, B.A., Bootman, M.D., Bordi, M., Borner, C., Bornhauser, B.C., Borthakur, G., Bosch, J., Bose, S., Botana, L.M., Botas, J., Boulanger, C.M., Boulton, M.E., Bourdenx, M., Bourgeois, B., Bourke, N.M., Bousquet, G., Boya, P., Bozhkov, P.V., Bozi, L.H.M., Bozkurt, T.O., Brackney, D.E., Brandts, C.H., Braun, R.J., Braus, G.H., Bravo-Sagua, R., Bravo-San Pedro, J.M., Brest, P., Bringer, M.A., Briones-Herrera, A., Broaddus, V.C., Brodersen, P., Brodsky, J.L., Brody, S.L., Bronson, P.G., Bronstein, J.M., Brown, C.N., Brown, R.E., Brum, P.C., Brumell, J.H., Brunetti-Pierri, N., Bruno, D., Bryson-Richardson, R.J., Bucci, C., Buchrieser, C., Bueno, M., Buitrago-Molina, L.E., Buraschi, S., Buch, S., Buchan, J.R., Buckingham, E.M., Budak, H., Budini, M., Bultynck, G., Burada, F., Burgoyne, J.R., Burón, M.I., Bustos, V., Büttner, S., Butturini, E., Byrd, A., Cabas, I., Cabrera-Benitez, S., Cadwell, K., Cai, J., Cai, L., Cai, Q., Cairó, M., Calbet, J.A., Caldwell, G.A., Caldwell, K.A., Call, J.A., Calvani, R., Calvo, A.C., Calvo-Rubio Barrera, M., Camara, N.O., Camonis, J.H., Camougrand, N., Campanella, M., Campbell, E.M., Campbell-Valois, F.X., Campello, S., Campesi, I., Campos, J.C., Camuzard, O., Cancino, J., Candido de Almeida, D., Canesi, L., Caniggia, I., Canonico, B., Cantí, C., Cao, B., Caraglia, M., Caramés, B., Carchman, E.H., Cardenal-Muñoz, E., Cardenas, C., Cardenas, L., Cardoso, S.M., Carew, J.S., Carle, G.F., Carleton, G., Carloni, S., Carmona-Gutierrez, D., Carneiro, L.A., Carnevali, O., Carosi, J.M., Carra, S., Carrier, A., Carrier, L., Carroll, B., Carter, A.B., Carvalho, A.N., Casanova, M., Casas, C., Casas, J., Cassioli, C., Castillo, E.F., Castillo, K., Castillo-Lluva, S., Castoldi, F., Castori, M., Castro, A.F., Castro-Caldas, M., Castro-Hernandez, J., Castro-Obregon, S., Catz, S.D., Cavadas, C., Cavaliere, F., Cavallini, G., Cavinato, M., Cayuela, M.L., Cebollada Rica, P., Cecarini, V., Cecconi, F., Cechowska-Pasko, M., Cenci, S., Ceperuelo-Mallafré, V., Cerqueira, J.J., Cerutti, J.M., Cervia, D., Cetintas, V.B., Cetrullo, S., Chae, H.J., Chagin, A.S., Chai, C.Y., Chakrabarti, G., Chakrabarti, O., Chakraborty, T., Chakraborty, T., Chami, M., Chamilos, G., Chan, D.W., Chan, E.Y.W., Chan, E.D., Chan, H.Y.E., Chan, H.H., Chan, H., Chan, M.T.V., Chan, Y.S., Chandra, P.K., Chang, C.P., Chang, C., Chang, H.C., Chang, K., Chao, J., Chapman, T., Charlet-Berguerand, N., Chatterjee, S., Chaube, S.K., Chaudhary, A., Chauhan, S., Chaum, E., Checler, F., Cheetham, M.E., Chen, C.S., Chen, G.C., Chen, J.F., Chen, L.L., Chen, L., Chen, L., Chen, M., Chen, M.K., Chen, N., Chen, Q., Chen, R.H., Chen, S., Chen, W., Chen, W., Chen, X.M., Chen, X.W., Chen, X., Chen, Y., Chen, Y.G., Chen, Y., Chen, Y., Chen, Y.J., Chen, Y.Q., Chen, Z.S., Chen, Z., Chen, Z.H., Chen, Z.J., Chen, Z., Cheng, H., Cheng, J., Cheng, S.Y., Cheng, W., Cheng, X., Cheng, X.T., Cheng, Y., Cheng, Z., Chen, Z., Cheong, H., Cheong, J.K., Chernyak, B.V., Cherry, S., Cheung, C.F.R., Cheung, C.H.A., Cheung, K.H., Chevet, E., Chi, R.J., Chiang, A.K.S., Chiaradonna, F., Chiarelli, R., Chiariello, M., Chica, N., Chiocca, S., Chiong, M., Chiou, S.H., Chiramel, A.I., Chiurchiù, V., Cho, D.H., Choe, S.K., Choi, A.M.K., Choi, M.E., Choudhury, K.R., Chow, N.S., Chu, C.T., Chua, J.P., Chua, J.J.E., Chung, H., Chung, K.P., Chung, S., Chung, S.H., Chung, Y.L., Cianfanelli, V., Ciechomska, I.A., Cifuentes, M., Cinque, L., Cirak, S., Cirone, M., Clague, M.J., Clarke, R., Clementi, E., Coccia, E.M., Codogno, P., Cohen, E., Cohen, M.M, Colasanti, T., Colasuonno, F., Colbert, R.A., Colell, A., Čolić, M., Coll, N.S., Collins, M.O., Colombo, M.I., Colón-Ramos, D.A., Combaret, L., Comincini, S., Cominetti, M.R., Consiglio, A., Conte, A., Conti, F., Contu, V.R., Cookson, M.R., Coombs, K.M., Coppens, I., Corasaniti, M.T., Corkery, D.P., Cordes, N., Cortese, K., Costa, M.D.C., Costantino, S., Costelli, P., Coto-Montes, A., Crack, P.J., Crespo, J.L., Criollo, A., Crippa, V., Cristofani, R., Csizmadia, T., Cuadrado, A., Cui, B., Cui, J., Cui, Y., Cui, Y., Culetto, E., Cumino, A.C., Cybulsky, A.V., Czaja, M.J., Czuczwar, S.J., D'Adamo, S., D'Amelio, M., D'Arcangelo, D., D'Lugos, A.C., D'Orazi, G., da Silva, J.A., Dafsari, H.S., Dagda, R.K., Dagdas, Y., Daglia, M., Dai, X., Dai, Y., Dai, Y., Dal Col, J., Dalhaimer, P., Dalla Valle, L., Dallenga, T., Dalmasso, G., Damme, M., Dando, I., Dantuma, N.P., Darling, A.L., Das, H., Dasarathy, S., Dasari, S.K., Dash, S., Daumke, O., Dauphinee, A.N., Davies, J.S., Dávila, V.A., Davis, R.J., Davis, T., Dayalan Naidu, S., De Amicis, F., De Bosscher, K., De Felice, F., De Franceschi, L., De Leonibus, C., de Mattos Barbosa, M.G., De Meyer, G.R.Y., De Milito, A., De Nunzio, C., De Palma, C., De Santi, M., De Virgilio, C., De Zio, D., Debnath, J., DeBosch, B.J., Decuypere, J.P., Deehan, M.A., Deflorian, G., DeGregori, J., Dehay, B., Del Rio, G., Delaney, J.R., Delbridge, L.M.D., Delorme-Axford, E., Delpino, M.V., Demarchi, F., Dembitz, V., Demers, N.D., Deng, H., Deng, Z., Dengjel, J., Dent, P., Denton, D., DePamphilis, M.L., Der, C.J., Deretic, V., Descoteaux, A., Devis, L., Devkota, S., Devuyst, O., Dewson, G., Dharmasivam, M., Dhiman, R., di Bernardo, D., Di Cristina, M., Di Domenico, F., Di Fazio, P., Di Fonzo, A., Di Guardo, G., Di Guglielmo, G.M., Di Leo, L., Di Malta, C., Di Nardo, A., Di Rienzo, M., Di Sano, F., Diallinas, G., Diao, J., Diaz-Araya, G., Díaz-Laviada, I., Dickinson, J.M., Diederich, M., Dieudé, M., Dikic, I., Ding, S., Ding, W.X., Dini, L., Dinić, J., Dinic, M., Dinkova-Kostova, A.T., Dionne, M.S., Distler, J.H.W., Diwan, A., Dixon, I.M.C., Djavaheri-Mergny, M., Dobrinski, I., Dobrovinskaya, O., Dobrowolski, R., Dobson, R.C.J., Đokić, J., Dokmeci Emre, S., Donadelli, M., Dong, B., Dong, X., Dong, Z., Dorn Ii, G.W., Dotsch, V., Dou, H., Dou, J., Dowaidar, M., Dridi, S., Drucker, L., Du, A., Du, C., Du, G., Du, H.N., Du, L.L., du Toit, A., Duan, S.B., Duan, X., Duarte, S.P., Dubrovska, A., Dunlop, E.A., Dupont, N., Durán, R.V., Dwarakanath, B.S., Dyshlovoy, S.A., Ebrahimi-Fakhari, D., Eckhart, L., Edelstein, C.L., Efferth, T., Eftekharpour, E., Eichinger, L., Eid, N., Eisenberg, T., Eissa, N.T., Eissa, S., Ejarque, M., El Andaloussi, A., El-Hage, N., El-Naggar, S., Eleuteri, A.M., El-Shafey, E.S., Elgendy, M., Eliopoulos, A.G., Elizalde, M.M., Elks, P.M., Elsasser, H.P., Elsherbiny, E.S., Emerling, B.M., Emre, N.C.T., Eng, C.H., Engedal, N., Engelbrecht, A.M., Engelsen, A.S.T., Enserink, J.M., Escalante, R., Esclatine, A., Escobar-Henriques, M., Eskelinen, E.L., Espert, L., Eusebio, M.O., Fabrias, G., Fabrizi, C., Facchiano, A., Facchiano, F., Fadeel, B., Fader, C., Faesen, A.C., Fairlie, W.D., Falcó, A., Falkenburger, B.H., Fan, D., Fan, J., Fan, Y., Fang, E.F., Fang, Y., Fang, Y., Fanto, M., Farfel-Becker, T., Faure, M., Fazeli, G., Fedele, A.O., Feldman, A.M., Feng, D., Feng, J., Feng, L., Feng, Y., Feng, Y., Feng, W., Fenz Araujo, T., Ferguson, T.A., Fernández, A.F., Fernandez-Checa, J.C., Fernández-Veledo, S., Fernie, A.R., Ferrante, A.W., Ferraresi, A., Ferrari, M.F., Ferreira, J.C.B., Ferro-Novick, S., Figueras, A., Filadi, R., Filigheddu, N., Filippi-Chiela, E., Filomeni, G., Fimia, G.M., Fineschi, V., Finetti, F., Finkbeiner, S., Fisher, E.A., Fisher, P.B., Flamigni, F., Fliesler, S.J., Flo, T.H., Florance, I., Florey, O., Florio, T., Fodor, E., Follo, C., Fon, E.A., Forlino, A., Fornai, F., Fortini, P., Fracassi, A., Fraldi, A., Franco, B., Franco, R., Franconi, F., Frankel, L.B., Friedman, S.L., Fröhlich, L.F., Frühbeck, G., Fuentes, J.M., Fujiki, Y., Fujita, N., Fujiwara, Y., Fukuda, M., Fulda, S., Furic, L., Furuya, N., Fusco, C., Gack, M.U., Gaffke, L., Galadari, S., Galasso, A., Galindo, M.F., Gallolu Kankanamalage, S., Galluzzi, L., Galy, V., Gammoh, N., Gan, B., Ganley, I.G., Gao, F., Gao, H., Gao, M., Gao, P., Gao, S.J., Gao, W., Gao, X., Garcera, A., Garcia, M.N., Garcia, V.E., García-Del Portillo, F., Garcia-Escudero, V., Garcia-Garcia, A., Garcia-Macia, M., García-Moreno, D., Garcia-Ruiz, C., García-Sanz, P., Garg, A.D., Gargini, R., Garofalo, T., Garry, R.F., Gassen, N.C., Gatica, D., Ge, L., Ge, W., Geiss-Friedlander, R., Gelfi, C., Genschik, P., Gentle, I.E., Gerbino, V., Gerhardt, C., Germain, K., Germain, M., Gewirtz, D.A., Ghasemipour Afshar, E., Ghavami, S., Ghigo, A., Ghosh, M., Giamas, G., Giampietri, C., Giatromanolaki, A., Gibson, G.E., Gibson, S.B., Ginet, V., Giniger, E., Giorgi, C., Girao, H., Girardin, S.E., Giridharan, M., Giuliano, S., Giulivi, C., Giuriato, S., Giustiniani, J., Gluschko, A., Goder, V., Goginashvili, A., Golab, J., Goldstone, D.C., Golebiewska, A., Gomes, L.R., Gomez, R., Gómez-Sánchez, R., Gomez-Puerto, M.C., Gomez-Sintes, R., Gong, Q., Goni, F.M., González-Gallego, J., Gonzalez-Hernandez, T., Gonzalez-Polo, R.A., Gonzalez-Reyes, J.A., González-Rodríguez, P., Goping, I.S., Gorbatyuk, M.S., Gorbunov, N.V., Görgülü, K., Gorojod, R.M., Gorski, S.M., Goruppi, S., Gotor, C., Gottlieb, R.A., Gozes, I., Gozuacik, D., Graef, M., Gräler, M.H., Granatiero, V., Grasso, D., Gray, J.P., Green, D.R., Greenhough, A., Gregory, S.L., Griffin, E.F., Grinstaff, M.W., Gros, F., Grose, C., Gross, A.S., Gruber, F., Grumati, P., Grune, T., Gu, X., Guan, J.L., Guardia, C.M., Guda, K., Guerra, F., Guerri, C., Guha, P., Guillén, C., Gujar, S., Gukovskaya, A., Gukovsky, I., Gunst, J., Günther, A., Guntur, A.R., Guo, C., Guo, C., Guo, H., Guo, L.W., Guo, M., Gupta, P., Gupta, S.K., Gupta, S., Gupta, V.B., Gupta, V., Gustafsson, A.B., Gutterman, D.D., H B, R., Haapasalo, A., Haber, J.E., Hać, A., Hadano, S., Hafrén, A.J., Haidar, M., Hall, B.S., Halldén, G., Hamacher-Brady, A., Hamann, A., Hamasaki, M., Han, W., Hansen, M., Hanson, P.I., Hao, Z., Harada, M., Harhaji-Trajkovic, L., Hariharan, N., Haroon, N., Harris, J., Hasegawa, T., Hasima Nagoor, N., Haspel, J.A., Haucke, V., Hawkins, W.D., Hay, B.A., Haynes, C.M., Hayrabedyan, S.B., Hays, T.S., He, C., He, Q., He, R.R., He, Y.W., He, Y.Y., Heakal, Y., Heberle, A.M., Hejtmancik, J.F., Helgason, G.V., Henkel, V., Herb, M., Hergovich, A., Herman-Antosiewicz, A., Hernández, A., Hernandez, C., Hernandez-Diaz, S., Hernandez-Gea, V., Herpin, A., Herreros, J., Hervás, J.H., Hesselson, D., Hetz, C., Heussler, V.T., Higuchi, Y., Hilfiker, S., Hill, J.A., Hlavacek, W.S., Ho, E.A., Ho, I.H.T., Ho, P.W.L., Ho, S.L., Ho, W.Y., Hobbs, G.A., Hochstrasser, M., Hoet, P.H.M., Hofius, D., Hofman, P., Höhn, A., Holmberg, C.I., Hombrebueno, J.R., Yi-Ren Hong, C.W.H., Hooper, L.V., Hoppe, T., Horos, R., Hoshida, Y., Hsin, I.L., Hsu, H.Y., Hu, B., Hu, D., Hu, L.F., Hu, M.C., Hu, R., Hu, W., Hu, Y.C., Hu, Z.W., Hua, F., Hua, J., Hua, Y., Huan, C., Huang, C., Huang, C., Huang, C., Huang, C., Huang, H., Huang, K., Huang, M.L.H., Huang, R., Huang, S., Huang, T., Huang, X., Huang, Y.J., Huber, T.B., Hubert, V., Hubner, C.A., Hughes, S.M., Hughes, W.E., Humbert, M., Hummer, G., Hurley, J.H., Hussain, S., Hussain, S., Hussey, P.J., Hutabarat, M., Hwang, H.Y., Hwang, S., Ieni, A., Ikeda, F., Imagawa, Y., Imai, Y., Imbriano, C., Imoto, M., Inman, D.M., Inoki, K., Iovanna, J., Iozzo, R.V., Ippolito, G., Irazoqui, J.E., Iribarren, P., Ishaq, M., Ishikawa, M., Ishimwe, N., Isidoro, C., Ismail, N., Issazadeh-Navikas, S., Itakura, E., Ito, D., Ivankovic, D., Ivanova, S., Iyer, A.K.V., Izquierdo, J.M., Izumi, M., Jäättelä, M., Jabir, M.S., Jackson, W.T., Jacobo-Herrera, N., Jacomin, A.C., Jacquin, E., Jadiya, P., Jaeschke, H., Jagannath, C., Jakobi, A.J., Jakobsson, J., Janji, B., Jansen-Dürr, P., Jansson, P.J., Jantsch, J., Januszewski, S., Jassey, A., Jean, S., Jeltsch-David, H., Jendelova, P., Jenny, A., Jensen, T.E., Jessen, N., Jewell, J.L., Ji, J., Jia, L., Jia, R., Jiang, L., Jiang, Q., Jiang, R., Jiang, T., Jiang, X., Jiang, Y., Jimenez-Sanchez, M., Jin, E.J., Jin, F., Jin, H., Jin, L., Jin, L., Jin, M., Jin, S., Jo, E.K., Joffre, C., Johansen, T., Johnson, G.V.W., Johnston, S.A., Jokitalo, E., Jolly, M.K., Joosten, L.A.B., Jordan, J., Joseph, B., Ju, D., Ju, J.S., Ju, J., Juárez, E., Judith, D., Juhász, G., Jun, Y., Jung, C.H., Jung, S.C., Jung, Y.K., Jungbluth, H., Jungverdorben, J., Just, S., Kaarniranta, K., Kaasik, A., Kabuta, T., Kaganovich, D., Kahana, A., Kain, R., Kajimura, S., Kalamvoki, M., Kalia, M., Kalinowski, D.S., Kaludercic, N., Kalvari, I., Kaminska, J., Kaminskyy, V.O., Kanamori, H., Kanasaki, K., Kang, C., Kang, R., Kang, S.S., Kaniyappan, S., Kanki, T., Kanneganti, T.D., Kanthasamy, A.G., Kanthasamy, A., Kantorow, M., Kapuy, O., Karamouzis, M.V., Karim, M.D.R., Karmakar, P., Katare, R.G., Kato, M., Kaufmann, S.H.E., Kauppinen, A., Kaushal, G.P., Kaushik, S., Kawasaki, K., Kazan, K., Ke, P.Y., Keating, D.J., Keber, U., Kehrl, J.H., Keller, K.E., Keller, C.W., Kemper, J.K., Kenific, C.M., Kepp, O., Kermorgant, S., Kern, A., Ketteler, R., Keulers, T.G., Khalfin, B., Khalil, H., Khambu, B., Khan, S.Y., Khandelwal, V.K.M., Khandia, R., Kho, W., Khobrekar, N.V., Khuansuwan, S., Khundadze, M., Killackey, S.A., Kim, D., Kim, D.R., Kim, D.H., Kim, D.E., Kim, E.Y., Kim, E.K., Kim, H.R., Kim, H.S., Kim, H.R., Kim, J.H., Kim, J.K., Kim, J.H., Kim, J., Kim, J.H., Kim, K.I.I., Kim, P.K., Kim, S.J., Kimball, S.R., Kimchi, A., Kimmelman, A.C., Kimura, T., King, M.A., Kinghorn, K.J., Kinsey, C.G., Kirkin, V., Kirshenbaum, L.A., Kiselev, S.L., Kishi, S., Kitamoto, K., Kitaoka, Y., Kitazato, K., Kitsis, R.N., Kittler, J.T., Kjaerulff, O., Klein, P.S., Klopstock, T., Klucken, J., Knævelsrud, H., Knorr, R.L., Ko, B.C.B., Ko, F., Ko, J.L., Kobayashi, H., Kobayashi, S., Koch, I., Koch, J.C., Koenig, U., Kögel, D., Koh, Y.H., Koike, M., Kohlwein, S.D., Kocaturk, N.M., Komatsu, M., König, J., Kono, T., Kopp, B.T., Korcsmaros, T., Korkmaz, G., Korolchuk, V.I., Korsnes, M.S., Koskela, A., Kota, J., Kotake, Y., Kotler, M.L., Kou, Y., Koukourakis, M.I., Koustas, E., Kovacs, A.L., Kovács, T., Koya, D., Kozako, T., Kraft, C., Krainc, D., Krämer, H., Krasnodembskaya, A.D., Kretz-Remy, C., Kroemer, G., Ktistakis, N.T., Kuchitsu, K., Kuenen, S., Kuerschner, L., Kukar, T., Kumar, A., Kumar, A., Kumar, D., Kumar, D., Kumar, S., Kume, S., Kumsta, C., Kundu, C.N., Kundu, M., Kunnumakkara, A.B., Kurgan, L., Kutateladze, T.G., Kutlu, O., Kwak, S.A., Kwon, H.J., Kwon, T.K., Kwon, Y.T., Kyrmizi, I., La Spada, A., Labonté, P., Ladoire, S., Laface, I., Lafont, F., Lagace, D.C., Lahiri, V., Lai, Z., Laird, A.S., Lakkaraju, A., Lamark, T., Lan, S.H., Landajuela, A., Lane, D.J.R., Lane, J.D., Lang, C.H., Lange, C., Langel, Ü., Langer, R., Lapaquette, P., Laporte, J., LaRusso, N.F., Lastres-Becker, I., Lau, W.C.Y., Laurie, G.W., Lavandero, S., Law, B.Y.K., Law, H.K.W., Layfield, R., Le, W., Le Stunff, H., Leary, A.Y., Lebrun, J.J., Leck, L.Y.W., Leduc-Gaudet, J.P., Lee, C., Lee, C.P., Lee, D.H., Lee, E.B., Lee, E.F., Lee, G.M., Lee, H.J., Lee, H.K., Lee, J.M., Lee, J.S., Lee, J.A., Lee, J.Y., Lee, J.H., Lee, M., Lee, M.G., Lee, M.J., Lee, M.S., Lee, S.Y., Lee, S.J., Lee, S.Y., Lee, S.B., Lee, W.H., Lee, Y.R., Lee, Y.H., Lee, Y., Lefebvre, C., Legouis, R., Lei, Y.L., Lei, Y., Leikin, S., Leitinger, G., Lemus, L., Leng, S., Lenoir, O., Lenz, G., Lenz, H.J., Lenzi, P., León, Y., Leopoldino, A.M., Leschczyk, C., Leskelä, S., Letellier, E., Leung, C.T., Leung, P.S., Leventhal, J.S., Levine, B., Lewis, P.A., Ley, K., Li, B., Li, D.Q., Li, J., Li, J., Li, J., Li, K., Li, L., Li, M., Li, M., Li, M., Li, M., Li, M., Li, P.L., Li, M.Q., Li, Q., Li, S., Li, T., Li, W., Li, W., Li, X., Li, Y.P., Li, Y., Li, Z., Li, Z., Li, Z., Lian, J., Liang, C., Liang, Q., Liang, W., Liang, Y., Liang, Y.T., Liao, G., Liao, L., Liao, M., Liao, Y.F., Librizzi, M., Lie, P.P.Y., Lilly, M.A., Lim, H.J., Lima, T.R.R., Limana, F., Lin, C., Lin, C.W., Lin, D.S., Lin, F.C., Lin, J.D., Lin, K.M., Lin, K.H., Lin, L.T., Lin, P.H., Lin, Q., Lin, S., Lin, S.J., Lin, W., Lin, X., Lin, Y.X., Lin, Y.S., Linden, R., Lindner, P., Ling, S.C., Lingor, P., Linnemann, A.K., Liou, Y.C., Lipinski, M.M., Lipovšek, S., Lira, V.A., Lisiak, N., Liton, P.B., Liu, C., Liu, C.H., Liu, C.F., Liu, C.H., Liu, F., Liu, H., Liu, H.S., Liu, H.F., Liu, H., Liu, J., Liu, J., Liu, J., Liu, L., Liu, L., Liu, M., Liu, Q., Liu, W., Liu, W., Liu, X.H., Liu, X., Liu, X., Liu, X., Liu, X., Liu, Y., Liu, Y., Liu, Y., Liu, Y., Liu, Y., Livingston, J.A., Lizard, G., Lizcano, J.M., Ljubojevic-Holzer, S., LLeonart, M.E., Llobet-Navàs, D., Llorente, A., Lo, C.H., Lobato-Márquez, D., Long, Q., Long, Y.C., Loos, B., Loos, J.A., López, M.G., López-Doménech, G., López-Guerrero, J.A., López-Jiménez, A.T., López-Pérez, O., López-Valero, I., Lorenowicz, M.J., Lorente, M., Lorincz, P., Lossi, L., Lotersztajn, S., Lovat, P.E., Lovell, J.F., Lovy, A., Lőw, P., Lu, G., Lu, H., Lu, J.H., Lu, J.J., Lu, M., Lu, S., Luciani, A., Lucocq, J.M., Ludovico, P., Luftig, M.A., Luhr, M., Luis-Ravelo, D., Lum, J.J., Luna-Dulcey, L., Lund, A.H., Lund, V.K., Lünemann, J.D., Lüningschrör, P., Luo, H., Luo, R., Luo, S., Luo, Z., Luparello, C., Lüscher, B., Luu, L., Lyakhovich, A., Lyamzaev, K.G., Lystad, A.H., Lytvynchuk, L., Ma, A.C., Ma, C., Ma, M., Ma, N.F., Ma, Q.H., Ma, X., Ma, Y., Ma, Z., MacDougald, O.A., Macian, F., MacIntosh, G.C., MacKeigan, J.P., Macleod, K.F., Maday, S., Madeo, F., Madesh, M., Madl, T., Madrigal-Matute, J., Maeda, A., Maejima, Y., Magarinos, M., Mahavadi, P., Maiani, E., Maiese, K., Maiti, P., Maiuri, M.C., Majello, B., Major, M.B., Makareeva, E., Malik, F., Mallilankaraman, K., Malorni, W., Maloyan, A., Mammadova, N., Man, G.C.W., Manai, F., Mancias, J.D., Mandelkow, E.M., Mandell, M.A., Manfredi, A.A., Manjili, M.H., Manjithaya, R., Manque, P., Manshian, B.B., Manzano, R., Manzoni, C., Mao, K., Marchese, C., Marchetti, S., Marconi, A.M., Marcucci, F., Mardente, S., Mareninova, O.A., Margeta, M., Mari, M., Marinelli, S., Marinelli, O., Mariño, G., Mariotto, S., Marshall, R.S., Marten, M.R., Martens, S., Martin, A.P.J., Martin, K.R., Martin, S., Martin, S., Martín-Segura, A., Martín-Acebes, M.A., Martin-Burriel, I., Martin-Rincon, M., Martin-Sanz, P., Martina, J.A., Martinet, W., Martinez, A., Martinez, A., Martinez, J., Martinez Velazquez, M., Martinez-Lopez, N., Martinez-Vicente, M., Martins, D.O., Martins, J.O., Martins, W.K., Martins-Marques, T., Marzetti, E., Masaldan, S., Masclaux-Daubresse, C., Mashek, D.G., Massa, V., Massieu, L., Masson, G.R., Masuelli, L., Masyuk, A.I., Masyuk, T.V., Matarrese, P., Matheu, A., Matoba, S., Matsuzaki, S., Mattar, P., Matte, A., Mattoscio, D., Mauriz, J.L., Mauthe, M., Mauvezin, C., Maverakis, E., Maycotte, P., Mayer, J., Mazzoccoli, G., Mazzoni, C., Mazzulli, J.R., McCarty, N., McDonald, C., McGill, M.R., McKenna, S.L., McLaughlin, B.A., McLoughlin, F., McNiven, M.A., McWilliams, T.G., Mechta-Grigoriou, F., Medeiros, T.C., Medina, D.L., Megeney, L.Y., Megyeri, K., Mehrpour, M., Mehta, J.L., Meijer, A.J., Meijer, A.H., Mejlvang, J., Meléndez, A., Melk, A., Memisoglu, G., Mendes, A.F., Meng, D., Meng, F., Meng, T., Menna-Barreto, R., Menon, M.B., Mercer, C., Mercier, A.E., Mergny, J.L., Merighi, A., Merkley, S.D., Merla, G., Meske, V., Mestre, A.C., Metur, S.P., Meyer, C., Meyer, H., Mi, W., Mialet-Perez, J., Miao, J., Micale, L., Miki, Y., Milan, E., Milczarek, M., Miller, D.L., Miller, S.I., Miller, S., Millward, S.W., Milosevic, I., Minina, E.A., Mirzaei, H., Mirzaei, H.R., Mirzaei, M., Mishra, A., Mishra, N., Mishra, P.K., Misirkic Marjanovic, M., Misasi, R., Misra, A., Misso, G., Mitchell, C., Mitou, G., Miura, T., Miyamoto, S., Miyazaki, M., Miyazaki, M., Miyazaki, T., Miyazawa, K., Mizushima, N., Mogensen, T.H., Mograbi, B., Mohammadinejad, R., Mohamud, Y., Mohanty, A., Mohapatra, S., Möhlmann, T., Mohmmed, A., Moles, A., Moley, K.H., Molinari, M., Mollace, V., Møller, A.B., Mollereau, B., Mollinedo, F., Montagna, C., Monteiro, M.J., Montella, A., Montes, L.R., Montico, B., Mony, V.K., Monzio Compagnoni, G., Moore, M.N., Moosavi, M.A., Mora, A.L., Mora, M., Morales-Alamo, D., Moratalla, R., Moreira, P.I., Morelli, E., Moreno, S., Moreno-Blas, D., Moresi, V., Morga, B., Morgan, A.H., Morin, F., Morishita, H., Moritz, O.L., Moriyama, M., Moriyasu, Y., Morleo, M., Morselli, E., Moruno-Manchon, J.F., Moscat, J., Mostowy, S., Motori, E., Moura, A.F., Moustaid-Moussa, N., Mrakovcic, M., Muciño-Hernández, G., Mukherjee, A., Mukhopadhyay, S., Mulcahy Levy, J.M., Mulero, V., Muller, S., Münch, C., Munjal, A., Munoz-Canoves, P., Muñoz-Galdeano, T., Münz, C., Murakawa, T., Muratori, C., Murphy, B.M., Murphy, J.P., Murthy, A., Myöhänen, T.T., Mysorekar, I.U., Mytych, J., Nabavi, S.M., Nabissi, M., Nagy, P., Nah, J., Nahimana, A., Nakagawa, I., Nakamura, K., Nakatogawa, H., Nandi, S.S., Nanjundan, M., Nanni, M., Napolitano, G., Nardacci, R., Narita, M., Nassif, M., Nathan, I., Natsumeda, M., Naude, R.J., Naumann, C., Naveiras, O., Navid, F., Nawrocki, S.T., Nazarko, T.Y., Nazio, F., Negoita, F., Neill, T., Neisch, A.L., Neri, L.M., Netea, M.G., Neubert, P., Neufeld, T.P., Neumann, D., Neutzner, A., Newton, P.T., Ney, P.A., Nezis, I.P., Ng, C.C.W., Ng, T.B., Nguyen, H.T.T., Nguyen, L.T., Ni, H.M., Ní Cheallaigh, C., Ni, Z., Nicolao, M.C., Nicoli, F., Nieto-Diaz, M., Nilsson, P., Ning, S., Niranjan, R., Nishimune, H., Niso-Santano, M., Nixon, R.A., Nobili, A., Nobrega, C., Noda, T., Nogueira-Recalde, U., Nolan, T.M., Nombela, I., Novak, I., Novoa, B., Nozawa, T., Nukina, N., Nussbaum-Krammer, C., Nylandsted, J., O'Donovan, T.R., O'Leary, S.M., O'Rourke, E.J., O'Sullivan, M.P., O'Sullivan, T.E., Oddo, S., Oehme, I., Ogawa, M., Ogier-Denis, E., Ogmundsdottir, M.H., Ogretmen, B., Oh, G.T., Oh, S.H., Oh, Y.J., Ohama, T., Ohashi, Y., Ohmuraya, M., Oikonomou, V., Ojha, R., Okamoto, K., Okazawa, H., Oku, M., Oliván, S., Oliveira, J.M.A., Ollmann, M., Olzmann, J.A., Omari, S., Omary, M.B., Önal, G., Ondrej, M., Ong, S.B., Ong, S.G., Onnis, A., Orellana, J.A., Orellana-Muñoz, S., Ortega-Villaizan, M.D.M., Ortiz-Gonzalez, X.R., Ortona, E., Osiewacz, H.D., Osman, A.H.K., Osta, R., Otegui, M.S., Otsu, K., Ott, C., Ottobrini, L., Ou, J.H.J., Outeiro, T.F., Oynebraten, I., Ozturk, M., Pagès, G., Pahari, S., Pajares, M., Pajvani, U.B., Pal, R., Paladino, S., Pallet, N., Palmieri, M., Palmisano, G., Palumbo, C., Pampaloni, F., Pan, L., Pan, Q., Pan, W:, Pan, X., Panasyuk, G., Pandey, R., Pandey, U.B., Pandya, V., Paneni, F., Pang, S.Y., Panzarini, E., Papademetrio, D.L., Papaleo, E., Papinski, D., Papp, D., Park, E.C., Park, H.T., Park, J.M., Park, J.I., Park, J.T., Park, J., Park, S.C., Park, S.Y., Parola, A.H., Parys, J.B., Pasquier, A., Pasquier, B., Passos, J.F., Pastore, N., Patel, H.H., Patschan, D., Pattingre, S., Pedraza-Alva, G., Pedraza-Chaverri, J., Pedrozo, Z., Pei, G., Pei, J., Peled-Zehavi, H., Pellegrini, J.M., Pelletier, J., Peñalva, M.A., Peng, D., Peng, Y., Penna, F., Pennuto, M., Pentimalli, F., Pereira, C.M.F., Pereira, G.J.S., Pereira, L.C., Pereira de Almeida, L., Perera, N.D., Pérez-Lara, A., Perez-Oliva, A.B., Pérez-Pérez, M.E., Periyasamy, P., Perl, A., Perrotta, C., Perrotta, I., Pestell, R.G., Petersen, M., Petrache, I., Petrovski, G., Pfirrmann, T., Pfister, A.S., Philips, J.A., Pi, H., Picca, A., Pickrell, A.M., Picot, S., Pierantoni, G.M., Pierdominici, M., Pierre, P., Pierrefite-Carle, V., Pierzynowska, K., Pietrocola, F., Pietruczuk, M., Pignata, C., Pimentel-Muiños, F.X., Pinar, M., Pinheiro, R.O., Pinkas-Kramarski, R., Pinton, P., Pircs, K., Piya, S., Pizzo, P., Plantinga, T.S., Platta, H.W., Plaza-Zabala, A., Plomann, M., Plotnikov, E.Y., Plun-Favreau, H., Pluta, R., Pocock, R., Pöggeler, S., Pohl, C., Poirot, M., Poletti, A., Ponpuak, M., Popelka, H., Popova, B., Porta, H., Porte Alcon, S., Portilla-Fernandez, E., Post, M., Potts, M.B., Poulton, J., Powers, T., Prahlad, V., Prajsnar, T.K., Praticò, D., Prencipe, R., Priault, M., Proikas-Cezanne, T., Promponas, V.J., Proud, C.G., Puertollano, R., Puglielli, L., Pulinilkunnil, T., Puri, D., Puri, R., Puyal, J., Qi, X., Qi, Y., Qian, W., Qiang, L., Qiu, Y., Quadrilatero, J., Quarleri, J., Raben, N., Rabinowich, H., Ragona, D., Ragusa, M.J., Rahimi, N., Rahmati, M., Raia, V., Raimundo, N., Rajasekaran, N.S., Ramachandra Rao, S., Rami, A., Ramírez-Pardo, I., Ramsden, D.B., Randow, F., Rangarajan, P.N., Ranieri, D., Rao, H., Rao, L., Rao, R., Rathore, S., Ratnayaka, J.A., Ratovitski, E.A., Ravanan, P., Ravegnini, G., Ray, S.K., Razani, B., Rebecca, V., Reggiori, F., Régnier-Vigouroux, A., Reichert, A.S., Reigada, D., Reiling, J.H., Rein, T., Reipert, S., Rekha, R.S., Ren, H., Ren, J., Ren, W., Renault, T., Renga, G., Reue, K., Rewitz, K., Ribeiro de Andrade Ramos, B., Riazuddin, S.A., Ribeiro-Rodrigues, T.M., Ricci, J.E., Ricci, R., Riccio, V., Richardson, D.R., Rikihisa, Y., Risbud, M.V., Risueño, R.M., Ritis, K., Rizza, S., Rizzuto, R., Roberts, H.C., Roberts, L.D., Robinson, K.J., Roccheri, M.C., Rocchi, S., Rodney, G.G., Rodrigues, T., Rodrigues Silva, V.R., Rodriguez, A., Rodriguez-Barrueco, R., Rodriguez-Henche, N., Rodriguez-Rocha, H., Roelofs, J., Rogers, R.S., Rogov, V.V., Rojo, A.I., Rolka, K., Romanello, V., Romani, L., Romano, A., Romano, P.S., Romeo-Guitart, D., Romero, L.C., Romero, M., Roney, J.C., Rongo, C., Roperto, S., Rosenfeldt, M.T., Rosenstiel, P., Rosenwald, A.G., Roth, K.A., Roth, L., Roth, S., Rouschop, K.M.A., Roussel, B.D., Roux, S., Rovere-Querini, P., Roy, A., Rozieres, A., Ruano, D., Rubinsztein, D.C., Rubtsova, M.P., Ruckdeschel, K., Ruckenstuhl, C., Rudolf, E., Rudolf, R., Ruggieri, A., Ruparelia, A.A., Rusmini, P., Russell, R.R., Russo, G.L., Russo, M., Russo, R., Ryabaya, O.O., Ryan, K.M., Ryu, K.Y., Sabater-Arcis, M., Sachdev, U., Sacher, M., Sachse, C., Sadhu, A., Sadoshima, J., Safren, N., Saftig, P., Sagona, A.P., Sahay, G., Sahebkar, A., Sahin, M., Sahin, O., Sahni, S., Saito, N., Saito, S., Saito, T., Sakai, R., Sakai, Y., Sakamaki, J.I., Saksela, K., Salazar, G., Salazar-Degracia, A., Salekdeh, G.H., Saluja, A.K., Sampaio-Marques, B., Sanchez, M.C., Sanchez-Alcazar, J.A., Sanchez-Vera, V., Sancho-Shimizu, V., Sanderson, J.T., Sandri, M., Santaguida, S., Santambrogio, L., Santana, M.M., Santoni, G., Sanz, A., Sanz, P., Saran, S., Sardiello, M., Sargeant, T.J., Sarin, A., Sarkar, C., Sarkar, S., Sarrias, M.R., Sarkar, S., Sarmah, D.T., Sarparanta, J., Sathyanarayan, A., Sathyanarayanan, R., Scaglione, K.M., Scatozza, F., Schaefer, L., Schafer, Z.T., Schaible, U.E., Schapira, A.H.V., Scharl, M., Schatzl, H.M., Schein, C.H., Scheper, W., Scheuring, D., Schiaffino, M.V., Schiappacassi, M., Schindl, R., Schlattner, U., Schmidt, O., Schmitt, R., Schmidt, S.D., Schmitz, I., Schmukler, E., Schneider, A., Schneider, B.E., Schober, R., Schoijet, A.C., Schott, M.B., Schramm, M., Schröder, B., Schuh, K., Schüller, C., Schulze, R.L., Schürmanns, L., Schwamborn, J.C., Schwarten, M., Scialo, F., Sciarretta, S., Scott, M.J., Scotto, K.W., Scovassi, A.I., Scrima, A., Scrivo, A., Sebastian, D., Sebti, S., Sedej, S., Segatori, L., Segev, N., Seglen, P.O., Seiliez, I., Seki, E., Selleck, S.B., Sellke, F.W., Selsby, J.T., Sendtner, M., Senturk, S., Seranova, E., Sergi, C., Serra-Moreno, R., Sesaki, H., Settembre, C., Setty, S.R.G., Sgarbi, G., Sha, O., Shacka, J.J., Shah, J.A., Shang, D., Shao, C., Shao, F., Sharbati, S., Sharkey, L.M., Sharma, D., Sharma, G., Sharma, K., Sharma, P., Sharma, S., Shen, H.M., Shen, H., Shen, J., Shen, M., Shen, W., Shen, Z., Sheng, R., Sheng, Z., Sheng, Z.H., Shi, J., Shi, X., Shi, Y.H., Shiba-Fukushima, K., Shieh, J.J., Shimada, Y., Shimizu, S., Shimozawa, M., Shintani, T., Shoemaker, C.J., Shojaei, S., Shoji, I., Shravage, B.V., Shridhar, V., Shu, C.W., Shu, H.B., Shui, K., Shukla, A.K., Shutt, T.E., Sica, V., Siddiqui, A., Sierra, A., Sierra-Torre, V., Signorelli, S., Sil, P., Silva, B.J.A., Silva, J.D., Silva-Pavez, E., Silvente-Poirot, S., Simmonds, R.E., Simon, A.K., Simon, H.U., Simons, M., Singh, A., Singh, L.P., Singh, R., Singh, S.V., Singh, S.K., Singh, S.B., Singh, S., Singh, S.P., Sinha, D., Sinha, R.A., Sinha, S., Sirko, A., Sirohi, K., Sivridis, E.L., Skendros, P., Skirycz, A., Slaninová, I., Smaili, S.S., Smertenko, A., Smith, M.D., Soenen, S.J., Sohn, E.J., Sok, S.P.M., Solaini, G., Soldati, T., Soleimanpour, S.A., Soler, R.M., Solovchenko, A., Somarelli, J.A., Sonawane, A., Song, F., Song, H.K., Song, J.X., Song, K., Song, Z., Soria, L.R., Sorice, M., Soukas, A.A., Soukup, S.F., Sousa, D., Sousa, N., Spagnuolo, P.A., Spector, S.A., Srinivas Bharath, M.M., St Clair, D., Stagni, V., Staiano, L., Stalnecker, C.A., Stankov, M.V., Stathopulos, P.B., Stefan, K., Stefan, S.M., Stefanis, L., Steffan, J.S., Steinkasserer, A., Stenmark, H., Sterneckert, J., Stevens, C., Stoka, V., Storch, S., Stork, B., Strappazzon, F., Strohecker, A.M., Stupack, D.G., Su, H., Su, L.Yy, Su, L., Suarez-Fontes, A.M., Subauste, C.S., Subbian, S., Subirada, P.V., Sudhandiran, G., Sue, C.M., Sui, X., Summers, C., Sun, G., Sun, J., Sun, K., Sun, M.X., Sun, Q., Sun, Y., Sun, Z., Sunahara, K.K.S., Sundberg, E., Susztak, K., Sutovsky, P., Suzuki, H., Sweeney, G., Symons, J.D., Sze, S.C.W., Szewczyk, N.J., Tabęcka-Łonczynska, A., Tabolacci, C., Tacke, F., Taegtmeyer, H., Tafani, M., Tagaya, M., Tai, H., Tait, S.W.G., Takahashi, Y., Takats, S., Talwar, P., Tam, C., Tam, S.Y., Tampellini, D., Tamura, A., Tan, C.T., Tan, E.K., Tan, Y.Q., Tanaka, M., Tanaka, M., Tang, D., Tang, J., Tang, T.S., Tanida, I., Tao, Z., Taouis, M., Tatenhorst, L., Tavernarakis, N., Taylor, A., Taylor, G.A., Taylor, J.M., Tchetina, E., Tee, A.R., Tegeder, I., Teis, D., Teixeira, N., Teixeira-Clerc, F., Tekirdag, K.A., Tencomnao, T., Tenreiro, S., Tepikin, A.V., Testillano, P.S., Tettamanti, G., Tharaux, P.L., Thedieck, K., Thekkinghat, A.A., Thellung, S., Thinwa, J.W., Thirumalaikumar, V.P., Thomas, S.M., Thomes, P.G., Thorburn, A., Thukral, L., Thum, T., Thumm, M., Tian, L., Tichy, A., Till, A., Timmerman, V., Titorenko, V.I., Todi, S.V., Todorova, K., Toivonen, J.M., Tomaipitinca, L., Tomar, D., Tomas-Zapico, C., Tomić, S., Tong, B.C.K., Tong, C., Tong, X., Tooze, S.A., Torgersen, M.L., Torii, S., Torres-López, L., Torriglia, A., Towers, C.G., Towns, R., Toyokuni, S., Trajkovic, V., Tramontano, D., Tran, Q.G., Travassos, L.H., Trelford, C.B., Tremel, S., Trougakos, I.P., Tsao, B.P., Tschan, M.P., Tse, H.F., Tse, T.F., Tsugawa, H., Tsvetkov, A.S., Tumbarello, D.A., Tumtas, Y., Tuñón, M.J., Turcotte, S., Turk, B., Turk, V., Turner, B.J., Tuxworth, R.I., Tyler, J.K., Tyutereva, E.V., Uchiyama, Y., Ugun-Klusek, A., Uhlig, H.H., Ułamek-Kozioł, M., Ulasov, I.V., Umekawa, M., Ungermann, C., Unno, R., Urbe, S., Uribe-Carretero, E., Üstün, S., Uversky, V.N., Vaccari, T., Vaccaro, M.I., Vahsen, B.F., Vakifahmetoglu-Norberg, H., Valdor, R., Valente, M.J., Valko, A., Vallee, R.B., Valverde, A.M., Van den Berghe, G., van der Veen, S., Van Kaer, L., van Loosdregt, J., van Wijk, S.J.L., Vandenberghe, W., Vanhorebeek, I., Vannier-Santos, M.A., Vannini, N., Vanrell, M.C., Vantaggiato, C., Varano, G., Varela-Nieto, I., Varga, M., Vasconcelos, M.H., Vats, S., Vavvas, D.G., Vega-Naredo, I., Vega-Rubin-de-Celis, S., Velasco, G., Velázquez, A.P., Vellai, T., Vellenga, E., Velotti, F., Verdier, M., Verginis, P., Vergne, I., Verkade, P., Verma, M., Verstreken, P., Vervliet, T., Vervoorts, J., Vessoni, A.T., Victor, V.M., Vidal, M., Vidoni, C., Vieira, O.V., Vierstra, R.D., Viganó, S., Vihinen, H., Vijayan, V., Vila, M., Vilar, M., Villalba, J.M., Villalobo, A., Villarejo-Zori, B., Villarroya, F., Villarroya, J., Vincent, O., Vindis, C., Viret, C., Viscomi, M.T., Visnjic, D., Vitale, I., Vocadlo, D.J., Voitsekhovskaja, O.V., Volonté, C., Volta, M., Vomero, M., Von Haefen, C., Vooijs, M.A., Voos, W., Vucicevic, L., Wade-Martins, R., Waguri, S., Waite, K.A., Wakatsuki, S., Walker, D.W., Walker, M.J., Walker, S.A., Walter, J., Wandosell, F.G., Wang, B., Wang, C.Y., Wang, C., Wang, C., Wang, C., Wang, C.Y., Wang, D., Wang, F., Wang, F., Wang, F., Wang, G., Wang, H., Wang, H., Wang, H., Wang, H.G., Wang, J., Wang, J., Wang, J., Wang, J., Wang, K., Wang, L., Wang, L., Wang, M.H., Wang, M., Wang, N., Wang, P., Wang, P., Wang, P., Wang, P., Wang, Q.J., Wang, Q., Wang, Q.K., Wang, Q.A., Wang, W.T., Wang, W., Wang, X., Wang, X., Wang, Y., Wang, Y., Wang, Y., Wang, Y.Y., Wang, Y., Wang, Y., Wang, Y., Wang, Y., Wang, Z., Wang, Z., Wang, Z., Warnes, G., Warnsmann, V., Watada, H., Watanabe, E., Watchon, M., Wawrzyńska, A., Weaver, T.E., Wegrzyn, G., Wehman, A.M., Wei, H., Wei, L., Wei, T., Wei, Y., Weiergräber, O.H., Weihl, C.C., Weindl, G., Weiskirchen, R., Wells, A., Wen, R.H., Wen, X., Werner, A., Weykopf, B., Wheatley, S.P., Whitton, J.L., Whitworth, A.J., Wiktorska, K., Wildenberg, M.E., Wileman, T., Wilkinson, S., Willbold, D., Williams, B., Williams, R.S.B., Williams, R.L., Williamson, P.R., Wilson, R.A., Winner, B., Winsor, N.J., Witkin, S.S., Wodrich, H., Woehlbier, U., Wollert, T., Wong, E., Wong, J.H., Wong, R.W., Wong, V.K.W., Wong, W.L., Wu, A.G., Wu, C., Wu, J., Wu, J., Wu, K.K., Wu, M., Wu, S.Y., Wu, S., Wu, S.Y., Wu, S., Wu, W.K.K., Wu, X., Wu, X., Wu, Y.W., Wu, Y., Xavier, R.J., Xia, H., Xia, L., Xia, Z., Xiang, G., Xiang, J., Xiang, M., Xiang, W., Xiao, B., Xiao, G., Xiao, H., Xiao, H.T., Xiao, J., Xiao, L., Xiao, S., Xiao, Y., Xie, B., Xie, C.M., Xie, M., Xie, Y., Xie, Z., Xie, Z., Xilouri, M., Xu, C., Xu, E., Xu, H., Xu, J., Xu, J.R., Xu, L., Xu, W.W., Xu, X., Xue, Y., Yakhine-Diop, S.M.S., Yamaguchi, M., Yamaguchi, O., Yamamoto, A., Yamashina, S., Yan, S., Yan, S.J., Yan, Z., Yanagi, Y., Yang, C., Yang, D.S., Yang, H., Yang, H.T., Yang, H., Yang, J.M., Yang, J., Yang, J., Yang, L., Yang, L., Yang, M., Yang, P.M., Yang, Q., Yang, S., Yang, S., Yang, S.F., Yang, W., Yang, W.Y., Yang, X., Yang, X., Yang, Y., Yang, Y., Yao, H., Yao, S., Yao, X., Yao, Y.G., Yao, Y.M., Yasui, T., Yazdankhah, M., Yen, P.M., Yi, C., Yin, X.M., Yin, Y., Yin, Z., Yin, Z., Ying, M., Ying, Z., Yip, C.K., Yiu, S.P.T., Yoo, Y.H., Yoshida, K., Yoshii, S.R., Yoshimori, T., Yousefi, B., Yu, B., Yu, H., Yu, J., Yu, J., Yu, L., Yu, M.L., Yu, S.W., Yu, V.C., Yu, W.H., Yu, Z., Yu, Z., Yuan, J., Yuan, L.Q., Yuan, S., Yuan, S.S.F., Yuan, Y., Yuan, Z., Yue, J., Yue, Z., Yun, J., Yung, R.L., Zacks, D.N., Zaffagnini, G., Zambelli, V.O., Zanella, I., Zang, Q.S., Zanivan, S., Zappavigna, S., Zaragoza, P., Zarbalis, K.S., Zarebkohan, A., Zarrouk, A., Zeitlin, S.O., Zeng, J., Zeng, J.D., Žerovnik, E., Zhan, L., Zhang, B., Zhang, D.D., Zhang, H., Zhang, H., Zhang, H., Zhang, H., Zhang, H., Zhang, H., Zhang, H., Zhang, H.L., Zhang, J., Zhang, J., Zhang, J.P., Zhang, K.Y.B., Zhang, L.W., Zhang, L., Zhang, L., Zhang, L., Zhang, L., Zhang, M., Zhang, P., Zhang, S., Zhang, W., Zhang, X., Zhang, X.W., Zhang, X., Zhang, X., Zhang, X., Zhang, X., Zhang, X.D., Zhang, Y., Zhang, Y., Zhang, Y., Zhang, Y.D., Zhang, Y., Zhang, Y.Y., Zhang, Y., Zhang, Z., Zhang, Z., Zhang, Z., Zhang, Z., Zhang, Z., Zhang, Z., Zhao, H., Zhao, L., Zhao, S., Zhao, T., Zhao, X.F., Zhao, Y., Zhao, Y., Zhao, Y., Zhao, Y., Zheng, G., Zheng, K., Zheng, L., Zheng, S., Zheng, X.L., Zheng, Y., Zheng, Z.G., Zhivotovsky, B., Zhong, Q., Zhou, A., Zhou, B., Zhou, C., Zhou, G., Zhou, H., Zhou, H., Zhou, H., Zhou, J., Zhou, J., Zhou, J., Zhou, J., Zhou, K., Zhou, R., Zhou, X.J., Zhou, Y., Zhou, Y., Zhou, Y., Zhou, Z.Y., Zhou, Z., Zhu, B., Zhu, C., Zhu, G.Q., Zhu, H., Zhu, H., Zhu, H., Zhu, W.G., Zhu, Y., Zhu, Y., Zhuang, H., Zhuang, X., Zientara-Rytter, K., Zimmermann, C.M., Ziviani, E., Zoladek, T., Zong, W.X., Zorov, D.B., Zorzano, A., Zou, W., Zou, Z., Zou, Z., Zuryn, S., Zwerschke, W., Brand-Saberi, B., Dong, X.C., Kenchappa, C.S., Li, Z., Lin, Y., Oshima, S., Rong, Y., Sluimer, J.C., Stallings, C.L. and Tong, C.K.
Autophagy 17
(1): 1-382.
8 February 2021
Pathophysiological role of caveolae in hypertension.
Lian, X., Matthaeus, C., Kaßmann, M., Daumke, O. and Gollasch, M.
Frontiers in Medicine 6
: 153.
July 2019
Struktur und Funktion des mechanochemischen Motorproteins Dynamin.
Faelber, K. and Daumke, O.
BIOspektrum 24
(5): 481-483.
September 2018
Membrane fission by dynamin: what we know and what we need to know.
Antonny, B., Burd, C., De Camilli, P., Chen, E., Daumke, O., Faelber, K., Ford, M., Frolov, V.A., Frost, A., Hinshaw, J.E., Kirchhausen, T., Kozlov, M.M., Lenz, M., Low, H.H., McMahon, H., Merrifield, C., Pollard, T.D., Robinson, P.J., Roux, A. and Schmid, S.
EMBO Journal 35
(21): 2270-2284.
2 November 2016
Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.
Daumke, O. and Praefcke, G.J.
Biopolymers 105
(8): 580-593.
August 2016
Sequence co-evolutionary information is a natural partner to minimally-frustrated models of biomolecular dynamics.
Noel, J.K., Morcos, F. and Onuchic, J.N.
F1000 Research 5
(F1000 Faculty Rev): 106.
26 January 2016
BAR domain scaffolds in dynamin-mediated membrane fission.
Daumke, O., Roux, A. and Haucke, V.
Cell 156
(5): 882-892.
27 February 2014
Oligomerization of dynamin superfamily proteins in health and disease.
Faelber, K., Gao, S., Held, M., Posor, Y., Haucke, V., Noé, F. and Daumke, O.
Progress in Molecular Biology and Translational Science 117
: 411-443.
2013
Structural insights into dynamin-mediated membrane fission.
Faelber, K., Held, M., Gao, S., Posor, Y., Haucke, V., Noe, F. and Daumke, O.
Structure 20
(10): 1621-1628.
10 October 2012
Stomatin-domain proteins.
Lapatsina, L., Brand, J., Poole, K., Daumke, O. and Lewin, G.R.
European Journal of Cell Biology 91
(4): 240-245.
April 2012
Dynamin-like MxA GTPase: Structural insights into oligomerization and implications for antiviral activity.
Haller, O., Gao, S., von der Malsburg, A., Daumke, O. and Kochs, G.
Journal of Biological Chemistry 285
(37): 28419-28424.
10 September 2010
Editorial
Fraternal twins at work: Structures of PLD3/4 reveal mechanism for lysosomal nucleic acid breakdown.
Daumke, O. and Damme, M.
Structure 32
(6): 645-647.
6 June 2024
SPFH protein cage - one ring to rule them all.
Daumke, O. and Lewin, G.R.
Cell Research 32
(2): 117-118.
February 2022
How RB1CC1/FIP200 claws its way to autophagic engulfment of SQSTM1/p62-ubiquitin condensates.
Turco, E., Witt, M., Abert, C., Bock-Bierbaum, T., Su, M.Y., Trapannone, R., Sztacho, M., Danieli, A., Shi, X., Zaffagnini, G., Gamper, A., Schuschnig, M., Fracchiolla, D., Bernklau, D., Romanov, J., Hartl, M., Hurley, J.H., Daumke, O. and Martens, S.
Autophagy 15
(8): 1475-1477.
August 2019
Mitochondrial homeostasis: How do dimers of mitofusins mediate mitochondrial fusion?
Daumke, O. and Roux, A.
Current Biology 27
(9): R353-R356.
8 May 2017
Protein-mediated membrane remodeling.
Daumke, O. and Unger, V.M.
Journal of Structural Biology 196
(1): 1-2.
October 2016
Structural insights into membrane fusion at the endoplasmic reticulum.
Daumke, O. and Praefcke, G.J.
Proceedings of the National Academy of Sciences of the United States of America 108
(6): 2175-2176.
8 February 2011
Preprint
Mechanistic basis for motor-driven membrane constriction by dynamin.
Ganichkin, O., Vancraenenbroeck, R., Rosenblum, G., Hofmann, H., Mikhailov, A.S., Daumke, O. and Noel, J.K.
bioRxiv
: 2020.09.10.289546.
11 September 2020
This list was generated on Mon Nov 11 17:27:13 2024 UTC.
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