Publications of the Geyer Lab

Hochheiser, I.V. and Geyer, M. (2022). An assay for the seeding of homotypic Pyrin domain filament transitions. Methods Mol. Biol. 2523, 197–207.

Moecking, J. and Geyer, M. (2022). A surface plasmon resonance-based strategy to characterize interactions of NLR proteins with associated factors. Methods Mol. Biol. 2523, 161–177.

Hochheiser, I.V., Behrmann, H., Hagelueken, G., Rodríguez-Alcázar, J.F., Kopp, A., Latz, E., Behrmann, E., and Geyer, M. (2022). Directionality of PYD filament growth determined by the transition of NLRP3 nucleation seeds to ASC elongation. Sci. Adv. 8, eabn7583.

Steiner, A., Hrovat-Schaale, K., Prigione, I., Yu, C.H., Laohamonthonkul, P., Harapas, C.R., Low, R.R.J., De Nardo, D., Dagley, L.F., Mlodzianoski, M.J., Rogers, K.L., Zillinger, T., Hartmann, G., Gantier, M.P., Gattorno, M., Geyer, M., Volpi, S., Davidson, S., and Masters, S.L. (2022). Deficiency in coatomer complex I causes aberrant activation of STING signalling. Nat. Commun. 13:2321.

Hassoun, R., Erdmann, C., Schmitt, S., Fujita-Becker, S., Mügge, A., Schröder, R.R., Geyer, M., Borbor, M., Jaquet, K., Hamdani, N., and Mannherz, H.G. (2022). Functional characterization of cardiac actin mutants causing hypertrophic (p.A295S) and dilated cardiomyopathy (p.R312H and p.E361G). Int. J. Mol. Sci. 23:4465.

Hochheiser, I.V., Pilsl, M., Hagelueken, G., Moecking, J., Marleaux, M., Brinkschulte, R., Latz, E., Engel, C., and Geyer, M. (2022). Structure of the NLRP3 decamer bound to the cytokine release inhibitor CRID3. Nature 604, 184–189.

Funke, K., Düster, R., De-Graft Wilson, P., Arévalo, L., Geyer, M., and Schorle, H. (2022). Transcriptional CDK inhibitors as potential treatment option for testicular germ cell tumors. Cancers 14:1690.

Düster, R., Ji, Y., Pan, K.T., Urlaub, H., and Geyer, M. (2022). Functional characterization of the human Cdk10/Cyclin Q complex. Open Biol. 12:210381.

Keuler, T., Ferber, D., Marleaux, M., Geyer, M., and Gütschow, M. (2022). Structure-stability relationship of NLRP3 inflammasome-inhibiting sulfonylureas. ACS Omega 7, 8158–8162.

Steiner, A., Reygaerts, T., Pontillo, A., Ceccherini, I., Moecking, J., Moghaddas, F., Davidson, S., Caroli, F., Grossi, A., Castro, F.F.M., Kalil, J., Gohr, F.N., Schmidt, F.I., Bartok, E., Zillinger, T., Hartmann, G., Geyer, M., Gattorno, M., Mendonça, L.O., and Masters, S.L. (2022). Recessive NLRC4-autoinflammatory disease reveals an Ulcerative Colitis locus. J. Clin. Immunol. 42, 325–335.

Ludwig, K.U., Schmithausen, R.M., Li, D., Jacobs, M.L., Hollstein, R., Blumenstock, K., Liebing, J., Słabicki, M., Ben-Shmuel, A., Israeli, O., Weiss, S., Ebert, T.S., Paran, N., Rüdiger, W., Wilbring, G., Feldman, D., Lippke, B., Ishorst, N., Hochfeld, L.M., Beins, E.C., Kaltheuner, I.H., Schmitz, M., Wöhler, A., Döhla, M., Sib, E., Jentzsch, M., Borrajo, J.D., Strecker, J., Reinhardt, J., Cleary, B., Geyer, M., Hölzel, M., Macrae, R., Nöthen, M.M., Hoffmann, P., Exner, M., Regev, A., Zhang, F., and Schmid-Burgk, J.L. (2021). LAMP-Seq enables sensitive, multiplexed COVID-19 diagnostics using molecular barcoding. Nat. Biotechnol. 39, 1556–1562.

Kaltheuner, I.H., Anand, K., Moecking, J., Düster, R., Wang, J., Gray, N.S., and Geyer, M. (2021). Abemaciclib is a potent inhibitor of DYRK1A and HIP kinases involved in transcriptional regulation. Nat. Commun. 12:6607.

Cesarato, N., Wehner, M., Ghughunishvili, M., Schmidt, A., Axt, D., Thiele, H., Lentze, M.J., Has, C., Geyer, M., Basmanav, F.B., and Betz, R.C (2021). Four hypotrichosis families with mutations in the gene LSS presenting with and without neurodevelopmental phenotypes. Am. J. Med. Genet. A 185, 3900–3904.

Jiang, B., Jiang, J., Kaltheuner, I.H., Iniguez, A.B., Anand, K., Ferguson, F.M., Ficarro, S.B., Seong, B.K.A., Greifenberg, A.K., Dust, S., Kwiatkowski, N.P., Marto, J.A., Stegmaier, K., Zhang, T., Geyer, M., and Gray, N.S. (2021). Structure-activity relationship study of THZ531 derivatives enables the discovery of BSJ-01-175 as a dual CDK12/13 covalent inhibitor with efficacy in Ewing sarcoma. Eur. J. Med. Chem. 221:113481.

Walch, P., Selkrig, J., Knodler, L.A., Rettel, M., Stein, F., Fernandez, K., Viéitez, C., Potel, C.M., Scholzen, K., Geyer, M., Rottner, K., Steele-Mortimer, O., Savitski, M.M., Holden, D.W., and Typas, A. (2021). Global mapping of Salmonella enterica-host protein-protein interactions during infection. Cell Host Microbe 29, 1316–1332.

Erdmann, C., Hassoun, R., Schmitt, S., Kikuti, C., Houdusse, A., Mazur, A.J., Mügge, A., Hamdani, N., Geyer, M., Jaquet, K., and Mannherz, H.G. (2021). Integration of cardiac actin mutants causing hypertrophic (p.A295S) and dilated cardiomyopathy (p.R312H and p.E361G) into cellular structures. Antioxidants 10:1082.

Jiang, B., Gao, Y., Che, J., Lu, W., Kaltheuner, I.H., Dries, R., Kalocsay, M., Berberich, M.J., Jiang, J., You, I., Kwiatkowski, N.P., Riching, K.M., Daniels, D.L., Sorger, P.K., Geyer, M., Zhang, T., and Gray, N.S. (2021). Discovery and resistance mechanism of a selective CDK12 degrader. Nat. Chem. Biol. 17, 675–683.

Moecking, J., Laohamonthonkul, P., Chalker, K., White, M.J., Harapas, C.R., Yu, C.H., Davidson, S., Hrovat-Schaale, K., Hu, D., Eng, C., Huntsman, S., Calleja, D.J., Horvat, J.C., Hansbro, P.M., O'Donoghue, R.J.J., Ting, J.P., Burchard, E.G., Geyer, M., Gerlic, M., and Masters, S.L. (2021). NLRP1 variant M1184V decreases inflammasome activation in the context of DPP9 inhibition and asthma severity. J. Allergy Clin. Immunol. 147, 2134–2145.

Keuler, T., Gatterdam, K., Akbal, A., Lovotti, M., Marleaux, M., Geyer, M., Latz, E., and Gütschow, M. (2021). Development of fluorescent and biotin probes targeting NLRP3. Front. Chem. 9:642273.

Koenig, P.A., Das, H., Liu, H., Kümmerer, B.M., Gohr, F.N., Jenster, L.M., Schiffelers, L.D.J., Tesfamariam, Y.M., Uchima, M., Wuerth, J.D., Gatterdam, K., Ruetalo, N., Christensen, M.H., Fandrey, C.I., Normann, S., Tödtmann, J.M.P., Pritzl, S., Hanke, L., Boos, J., Yuan, M., Zhu, X., Schmid-Burgk, J.L., Kato, H., Schindler, M., Wilson, I.A., Geyer, M., Ludwig, K.U., Hällberg, B.M., Wu, N.C., and Schmidt, F.I. (2021). Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape. Science 371:eabe6230.

Düster, R., Kaltheuner, I.H., Schmitz, M., and Geyer, M. (2021). 1,6-Hexanediol, commonly used to dissolve liquid-liquid phase separated condensates, directly impairs kinase and phosphatase activities. J. Biol. Chem. 296:100260.

Rimel, J.K., Poss, Z.C., Erickson, B., Maas, Z.L., Ebmeier, C.C., Johnson, J.L., Decker, T.M., Yaron, T.M., Bradley, M.J., Hamman, K.B., Hu, S., Malojcic, G., Marineau, J.J., White, P.W., Breault, M., Tao, L., DeRoy, P., Clavette, C., Nayak, S., Damon, L.J., Kaltheuner, I.H., Bunch, H., Cantley, L.C., Geyer, M., Iwasa, J., Dowell, R.D., Bentley, D.L.,, Old, W.M., and Taatjes, D.J. (2020). Selective inhibition of CDK7 reveals high-confidence targets and new models for TFIIH function in transcription. Genes Dev. 34, doi: 10.1101/gad.341545.120. Online ahead of print.

Mayor-Ruiz, C., Bauer, S., Brand, M., Kozicka, Z., Siklos, M., Imrichova, H., Kaltheuner, I.H., Hahn, E., Seiler, K., Koren, A., Petzold, G., Fellner, M., Bock, C., Müller, A.C., Zuber, J., Geyer, M., Thomä, N.H., Kubicek, S., and Winter, G.E. (2020). Rational discovery of molecular glue degraders via scalable chemical profiling. Nat. Chem. Biol. 16, 1199–1207.

Braun, M., Aguilera, A.R., Sundarrajan, A., Corvino, D., Stannard, K., Krumeich, S., Das, I., Lima, L.G., Meza Guzman, L.G., Li, K., Li, R., Salim, N., Jorge, M.V., Ham, S., Kelly, G., Vari, F., Lepletier, A., Raghavendra, A., Pearson, S., Madore, J., Jacquelin, S., Effern, M., Quine, B., Koufariotis, L.T., Casey, M., Nakamura, K., Seo, E.Y., Hölzel, M., Geyer, M., Kristiansen, G., Taheri, T., Ahern, E., Hughes, B.G.M., Wilmott, J.S., Long, G.V., Scolyer, R.A., Batstone, M.D., Landsberg, J., Dietrich, D., Pop, O.T., Flatz, L., Dougall, W.C., Veillette, A., Nicholson, S.E., Möller, A., Johnston, R.J., Martinet, L., Smyth, M.J., and Bald, T. (2020). CD155 on Tumor Cells Drives Resistance to Immunotherapy by Inducing the Degradation of the Activating Receptor CD226 in CD8+ T Cells. Immunity 53, 805–823.

Marleaux, M., Anand, K., Latz, E., and Geyer, M. (2020). Crystal structure of the human NLRP9 Pyrin domain suggests a distinct mode of inflammasome assembly. FEBS Lett. 594, 2383–2395.

Fan, Z., Devlin, J.R., Hogg, S.J., Doyle, M.A., Harrison, P.F., Todorovski, I., Cluse, L.A., Knight, D.A., Sandow, J.J., Gregory, G., Fox, A., Beilharz, T.H., Kwiatkowski, N., Scott, N.E., Vidakovic, A.T., Kelly, G.P., Svejstrup, J.Q., Geyer, M., Gray, N.S., Vervoort, S.J., and Johnstone, R.W. (2020). CDK13 cooperates with CDK12 to control global RNA polymerase II processivity. Sci. Adv. 6:eaaz5041.

Friker, L.L., Scheiblich, H., Hochheiser, I.V., Brinkschulte, R., Riedel, D., Latz, E., Geyer, M., and Heneka, M.T. (2020). β-Amyloid clustering around ASC fibrils boosts its toxicity in microglia. Cell Rep. 30, 3743–3754.

Torres-Fernández, L.A., Jux, B., Bille, M., Port, Y., Schneider, K., Geyer, M., Mayer, G., and Kolanus, W. (2019). The mRNA repressor TRIM71 cooperates with nonsense-mediated decay factors to destabilize the mRNA of CDKN1A/p21. Nucleic Acids Res. 47, 11861–11879.

Hoss, F., Mueller, J.L., Rojas Ringeling, F., Rodriguez-Alcazar, J.F., Brinkschulte, R., Seifert, G., Stahl, R., Broderick, L., Putnam, C.D., Kolodner, R.D., Canzar, S., Geyer, M., Hoffman, H.M., and Latz, E. (2019). Alternative splicing regulates stochastic NLRP3 activity. Nat. Commun. 10:3238.

Olson, C.M., Liang, Y., Leggett, A., Park, W.D., Li, L., Mills, C.E., Elsarrag, S.Z., Ficarro, S.B., Zhang, T., Düster, R., Geyer, M., Sim, T., Marto, J.A., Sorger, P.K., Westover, K.D., Lin, C.Y., Kwiatkowski, N., and Gray, N.S. (2019). Development of a selective CDK7 covalent inhibitor reveals predominant cell-cycle phenotype. Cell Chem. Biol. 26, 792–803.

Baluapuri, A., Hofstetter, J., Dudvarski Stankovic, N., Endres, T., Bhandare, P., Vos, S.M., Adhikari, B., Schwarz, J.D., Narain, A., Vogt, M., Wang, S.Y., Düster, R., Jung, L.A., Vanselow, J.T., Wiegering, A., Geyer, M., Maric, H.M., Gallant, P., Walz, S., Schlosser, A., Cramer, P., Eilers, M., and Wolf, E. (2019). MYC recruits SPT5 to RNA polymerase II to promote processive transcription elongation. Mol. Cell 74, 674 – 687.

Bugai, A., Quaresma, A.J.C., Friedel, C.C., Lenasi, T., Düster, R., Sibley, C.R., Fujinaga, K., Kukanja, P., Hennig, T., Blasius, M., Geyer, M., Ule, J., Dölken, L., and Barborič, M. (2019). P-TEFb activation by RBM7 shapes a pro-survival transcriptional response to genotoxic stress. Mol. Cell 74, 254–267.

Krajewska, M., Dries, R., Grassetti, A.V., Dust, S., Gao, Y., Huang, H., Sharma, B., Day, D.S., Kwiatkowski, N., Pomaville, M., Dodd, O., Chipumuro, E., Zhang, T., Greenleaf, A.L., Yuan, G.C., Gray, N.S., Young, R.A., Geyer, M., Gerber, S.A., and George, R.E. (2019). CDK12 loss in cancer cells affects DNA damage response genes through premature cleavage and polyadenylation. Nat. Commun. 10:1757.

Grueb, S.S., Muhs, S., Popp, Y., Schmitt, S., Geyer, M., Lin, Y.N., and Windhorst, S. (2019). The formin Drosophila homologue of Diaphanous2 (Diaph2) controls microtubule dynamics in colorectal cancer cells independent of its FH2-domain. Sci. Rep. 9:5352.

Woeste, M.A., Stern, S., Raju, D.N., Grahn, E., Dittmann, D., Gutbrod, K., Dörmann, P., Hansen, J.N., Schonauer, S., Marx, C.E., Hamzeh, H., Körschen, H.G., Aerts, J.M.F.G., Bōnigk, W., Endepols, H., Sandhoff, R., Geyer, M., Berger, T.K., Bradke, F., and Wachten, D. (2019). Species-specific differences in non-lysosomal glucosylceramidase GBA2 function underlie locomotor dysfunction arising from loss-of-function mutations. J. Biol. Chem. 294, 3853–3871.

Rohrmoser, M., Kluge, M., Yahia, Y., Gruber-Eber, A., Maqbool, M.A., Forné, I., Krebs, S., Blum, H., Greifenberg, A.K., Geyer, M., Descostes, N., Imhof, A., Andrau, J.C., Friedel, C.C., and Eick, D. (2019). MIR sequences recruit zinc finger protein ZNF768 to expressed genes. Nucleic Acids Res. 47, 700–715.

Romano, M.T., Tafazzoli, A., Mattern, M., Sivalingam, S., Wolf, S., Rupp, A., Thiele, H., Altmüller, J., Nürnberg, P., Ellwanger, J., Gambon, R., Baumer, A., Kohlschmidt, N., Metze, D., Holdenrieder, S., Paus, R., Lütjohann, D., Frank, J., Geyer, M., Bertolini, M., Kokordelis, P., and Betz, R.C. (2018). Bi-allelic mutations in LSS, encoding lanosterol synthase, cause autosomal-recessive hypotrichosis simplex. Am. J. Hum. Genet. 103, 777–785.

Müller, J.A., Glöckle, A., Gawanbacht, A., Geyer, M., Münch, J., and Kirchhoff, F. (2018). Reduced susceptibility to VIRIP-based HIV-1 entry inhibitors has a high genetic barrier and severe fitness costs. J. Virol. 92, e00733-18.

Yu, C.F., Peng, W.M., Schlee, M., Barchet, W., Eis-Hübinger, A.M., Kolanus, W., Geyer, M., Schmitt, S., Steinhagen, F., Oldenburg, J., and Novak, N. (2018). SOCS1 and SOCS3 target IRF7 degradation to suppress TLR7-mediated type I IFN production of human plasmacytoid dendritic cells. J. Immunol. 200, 4024–4035.

Yu, C.H., Moecking, J., Geyer, M., and Masters, S.L. (2018). Mechanisms of NLRP1-mediated autoinflammatory disease in humans and mice. J. Mol. Biol. 430, 142–152.

Venegas, C., Kumar, S., Franklin, B.S., Dierkes, T., Brinkschulte, R., Tejera, D., Vieira-Saecker, A., Schwartz, S., Santarelli, F., Kummer, M.P., Griep, A., Gelpi, E., Beilharz, M., Riedel, D., Golenbock, D.T., Geyer, M., Walter, J., Latz, E., and Heneka, M.T. (2017). Microglia-derived ASC specks cross-seed amyloid-β in Alzheimer’s disease. Nature 552, 355–361.

Lim, E., Johnson, S.F., Geyer, M., Serra, V., and Shapiro, G.I. (2017). Sensitizing HR-proficient cancers to PARP inhibitors. Mol. Cell. Oncol. 4, e1299272.

Manrique, S., Sauter, D., Horenkamp, F.A., Lülf, S., Yu, H., Hotter, D., Anand, K., Kirchhoff, F., and Geyer, M. (2017). Endocytic sorting motif interactions involved in Nef-mediated downmodulation of CD4 and CD3. Nat. Commun. 8:442.

Jostes, S., Nettersheim, D., Fellermeyer, M., Schneider, S., Hafezi, F., Honecker, F., Schumacher, V., Geyer, M., Kristiansen, G., and Schorle, H. (2017). The bromodomain inhibitor JQ1 triggers growth arrest and apoptosis in testicular germ cell tumours in vitro and in vivo. J. Cell. Mol. Med. 21, 1300–1314.

Stutz, A., Kolbe, C.C., Stahl, R., Horvath, G.L., Franklin, B.S., van Ray, O., Brinkschulte, R., Geyer, M., Meissner, F., and Latz, E. (2017). NLRP3 inflammasome assembly is regulated by phosphorylation of the pyrin domain. J. Exp. Med. 214, 1725–1736.

Kim, E.S., Ackermann, C., Tóth, I., Dierks, P., Eberhard, J.M., Wroblewski, R., Scherg, F., Geyer, M., Schmidt, R.E., Beisel, C., Bockhorn, M., Haag, F., van Lunzen, J., and Schulze zur Wiesch, J. (2017). Down-regulation of CD73 on B cells of patients with viremic HIV correlates with B cell activation and disease progression. J. Leukoc. Biol. 101, 1263–1271.

Kage, F., Winterhoff, M., Dimchev, V., Mueller, J., Thalheim, T., Freise, A., Brühmann, S., Kollasser, J., Block, J., Dimchev, G., Geyer, M., Schnittler, H.J., Brakebusch, C., Stradal, T.E.B., Carlier, M.F., Sixt, M., Käs, J., Faix, J., and Rottner, K. (2017). FMNL formins boost lamellipodial force generation. Nat. Commun. 8:14832.

Mack, K., Starz, K., Sauter, D., Langer, S., Bibollet-Ruche, F., Learn, G.H., Stürzel, C.M., Leoz, M., Plantier, J.C., Geyer, M., Hahn, B.H., and Kirchhoff, F. (2017). Efficient Vpu-mediated tetherin antagonism by an HIV-1 group O strain. J. Virol. 91, e02177-16.

Johnson, S.F., Cruz, C., Greifenberg, A.K., Dust, S., Stover, D.G., Chi, D., Primack, B., Cao, S., Bernhardy, A.J., Coulson, R., Lazaro, J.B., Kochupurakkal, B., Sun, H., Unitt, C., Moreau, L.A., Sarosiek, K.A., Scaltriti, M., Juric, D., Baselga, J., Richardson, A.L., Rodig, S.J., D’Andrea, A.D., Balmaña, J., Johnson, N., Geyer, M., Serra, V., Lim, E., and Shapiro, G.I. (2016). CDK12 inhibition reverses de novo and acquired PARP inhibitor resistance in BRCA wild-type and mutated models of triple-negative breast cancer. Cell Rep. 17, 2367–2381.

Imle, A., Stolp, B., Böhmer, V., Geyer, M., Raz, E., and Fackler, O.T. (2016). D186/D190 is an allele-dependent determinant of HIV-1 Nef function. Virology 498, 44–56.

Zhang, T., Kwiatkowski, N., Olson, C.M., Dixon-Clarke, S.E., Abraham, B.J., Greifenberg, A.K., Ficarro, S.B., Elkins, J.M., Liang, Y., Hannett, N.M., Manz, T., Hao, M., Bartkowiak, B., Greenleaf, A.L., Marto, J.A., Geyer, M., Bullock, A.N., Young, R.A., and Gray, N.S. (2016). Covalent targeting of remote cysteine residues to develop CDK12 and CDK13 inhibitors. Nat. Chem. Biol. 12, 876–884.

Greifenberg, A.K., Hönig, D., Pilarova, K., Düster, R., Bartholomeeusen, K., Bösken, C.A., Anand, K., Blazek, D., and Geyer, M. (2016). Structural and functional analysis of the Cdk13/Cyclin K complex. Cell Rep. 14, 320–331.

Jaenicke, L.A., von Eyss, B., Carstensen, A., Wolf, E., Xu, W., Greifenberg, A.K., Geyer, M., Eilers, M., and Popov, N. (2016). Ubiquitin-dependent turnover of MYC antagonizes MYC/Paf1C complex accumulation to drive transcriptional elongation. Mol. Cell 61, 54–67.

Sansó, M., Levin, R.S., Lipp, J.J., Wang, V.Y., Greifenberg, A.K., Quezada, E.M., Ali, A., Ghosh, A., Larochelle, S., Rana, T.M., Geyer, M., Tong, L., Shokat, K.M., and Fisher, R.P. (2016). P-TEFb regulation of transcription termination factor Xrn2 revealed by a chemical genetic screen for Cdk9 substrates. Genes Dev. 30, 117–131.

Mangino, G., Famiglietti, M., Capone, C., Veroni, C., Percario, Z.A., Leone, S., Fiorucci, G., Lülf, S., Romeo, G., Agresti, C., Persichini, T., Geyer, M. and Affabris, E. (2015). HIV-1 myristoylated Nef treatment of murine microglial cells activates inducible nitric oxide synthase, NO2 production and neurotoxic activity. PLoS One 10, e0130189.

Kühn, S., Erdmann, C., Kage, F., Block, J., Schwenkmezger, L., Steffen, A., Rottner, K. and Geyer, M. (2015). The structure of FMNL2–Cdc42 yields insights into the mechanism of lamellipodia and filopodia formation. Nat. Commun. 6:7088.

Ekumi, K.M., Paculova, H., Lenasi, T., Pospichalova, V., Bösken, C.A., Rybarikova, J., Bryja, V., Geyer, M., Blazek, D. and Barboric, M. (2015). Ovarian carcinoma CDK12 mutations misregulate expression of DNA repair genes via deficient formation and function of the Cdk12/CycK complex. Nucleic Acids Res. 43, 2575–2589.

Geyer, M., Pelka, K. and Latz, E. (2015). Synergistic activation of Toll-like receptor 8 by two RNA degradation products. Nat. Struct. Mol. Biol. 22, 99–101.

Al Haj, A., Mazur, A.J., Radaszkiewicz, K., Radaszkiewicz, T., Makowiecka, A., Stopschinski, B.E., Schönichen, A., Geyer, M. and Mannherz, H.G. (2015). Distribution of formins in cardiac muscle: FHOD1 is a component of intercalated discs and costameres. Eur. J. Cell Biol. 94, 101–113.

Kluge, S.F., Mack, K., Iyer, S.S., Pujol, F.M., Heigele, A., Learn, G.H., Usmani, S.M., Sauter, D., Joas, S., Hotter, D., Bibollet-Ruche, F., Plenderleith, L.J., Peeters, M., Geyer, M., Sharp, P.M., Fackler, O.T., Hahn, B.H. and Kirchhoff, F. (2014). Nef proteins of epidemic HIV-1 group O strains antagonize human tetherin. Cell Host Microbe 16, 639–650.

Kühn, S. and Geyer, M. (2014). Formins as effector proteins of Rho GTPases. Small GTPases 5, e29513.

Itzen, F., Greifenberg, A.K., Bösken, C.A. and Geyer, M. (2014). Brd4 activates P-TEFb for RNA polymerase II CTD phosphorylation. Nucleic Acids Res. 42, 7577-7590.

Cui, H.L., Ditiatkovski, M., Kesani, R., Bobryshev, Y.V., Liu, Y., Geyer, M., Mukhamedova, N., Bukrinsky, M. and Sviridov, D. (2014). HIV protein Nef causes dyslipidemia and formation of foam cells in mouse models of atherosclerosis. FASEB J. 28, 2828-2839.

Schulze, N., Graessl, M., Blancke Soares, A., Geyer, M., Dehmelt, L. and Nalbant, P. (2014). FHOD1 regulates stress fiber organization by controlling the dynamics of transverse arcs and dorsal fibers. J. Cell Sci. 127, 1379–1393.

Bösken, C.A., Farnung, L., Hintermair, C., Merzel Schachter, M., Vogel-Bachmayr, K., Blazek, D., Anand, K., Fisher, R.P., Eick, D. and Geyer, M. (2014). The structure and substrate specificity of human Cdk12/Cyclin K. Nat. Commun. 5:3505.

Lülf, S., Matz, J., Rouyez, M.C., Järviluoma, A., Saksela, K., Benichou, S. and Geyer, M. (2014). Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody. Retrovirology 11:24.

Schmökel, J., Li, H., Shabir, A., Yu, H., Geyer, M., Silvestri, G., Sodora, D.L., Hahn, B.H. and Kirchhoff, F. (2013). Link between primate lentiviral coreceptor usage and Nef function. Cell Rep. 5, 997–1009.

Schröder, S., Herker, E., Itzen, F., He, D., Thomas, S., Gilchrist, D.A., Kaehlcke, K., Cho, S., Pollard, K.S., Capra, J.A., Schnölzer, M., Cole, P.A., Geyer, M., Bruneau, B.G., Adelman, K. and Ott, M. (2013). Acetylation of RNA Polymerase II regulates growth factor-induced gene transcription in mammalian cells. Mol. Cell 52, 314–324.

Eick, D. and Geyer, M. (2013). The RNA polymerase II carboxy-terminal domain (CTD) code. Chem. Rev. 113, 8456–8490.

Schönichen, A., Mannherz, H.G., Behrmann, E., Mazur, A.J., Kühn, S., Silván, U., Schoenenberger, C.A., Fackler, O.T., Raunser, S., Dehmelt, L. and Geyer, M. (2013). FHOD1 is a combined actin filament capping and bundling factor that selectively associates with actin arcs and stress fibers. J. Cell Sci. 126, 1891–1901.

Götz, N., Sauter, D., Usmani, S.M., Fritz, J.V., Goffinet, C., Heigele, A., Geyer, M., Bibollet-Ruche, F., Learn, G.H., Fackler, O.T., Hahn, B.H. and Kirchhoff, F. (2012). Reacquisition of Nef-mediated Tetherin antagonism in a single in vivo passage of HIV-1 through its original chimpanzee host. Cell Host Microbe 12, 373–380.

Meuwissen, P.J., Stolp, B., Iannucci, V., Vermeire, J., Naessens, E., Saksela, K., Geyer, M., Vanham, G., Arien, K.K., Fackler, O.T. and Verhasselt, B. (2012). Identification of a highly conserved valine-glycine-phenylalanine amino acid triplet required for HIV-1 Nef function. Retrovirology 9:34.

Järviluoma, A., Strandin, T., Lülf, S., Bouchet, J., Mäkelä, A.R., Geyer, M., Benichou, S. and Saksela, K. (2012). High-affinity target binding engineered via fusion of a single-domain antibody fragment with a ligand-tailored SH3 domain. PLoS One 7, e40331.

St. Amour, C.V., Sansó, M., Bösken, C.A., Lee, K.M., Larochelle, S., Zhang, C., Shokat, K.M., Geyer, M. and Fisher, R.P. (2012). Separate domains of fission yeast Cdk9 (P-TEFb) are required for capping enzyme recruitment and primed (Ser7-phosphorylated) CTD substrate recognition. Mol. Cell. Biol. 32, 2372–2383.

Block, J., Breitsprecher, D., Kühn, S., Winterhoff, M., Kage, F., Geffers, R., Duwe, P., Rohn, J.L., Baum, B., Brakebusch, C., Geyer, M., Stradal, T.E., Faix, J. and Rottner, K. (2012). FMNL2 drives actin-based protrusion and migration downstream of Cdc42. Curr. Biol. 22, 1005–1012.

Czudnochowski, N., Bösken, C.A. and Geyer, M. (2012). Serine-7 but not serine-5 phosphorylation primes RNA polymerase II CTD for P-TEFb recognition. Nat. Commun. 3:842.

Khalid, M., Yu, H., Sauter, D., Usmani, S.M., Schmökel, J., Feldman, J., Gruters, R.A., van der Ende, M.E., Geyer, M., Rowland-Jones, S., Osterhaus, A.D. and Kirchhoff, F. (2012). Efficient Nef-mediated down-modulation of TCR-CD3 and CD28 is associated with high CD4+ T cell counts in viremic HIV-2 infection. J. Virol. 86, 4906–4920.

Mangino, G., Serra, V., Borghi, P., Percario, Z.A., Horenkamp, F.A., Geyer, M. and Affabris, E. (2012). Exogenous Nef induces proinflammatory signaling events in murine macrophages. Viral Immunol. 25, 117–130.

Vaz, E., Dames, S.A., Geyer, M. and Brunsveld, L. (2012). Positional screening and NMR structure determination of side-chain-to-side-chain cyclized b(3)-peptides. Org. Biomol. Chem. 10, 1365–1373.

Lülf, S., Horenkamp, F.A., Breuer, S. and Geyer, M. (2011). Nef surfaces: Where to interfere with function. Curr. HIV Res. 9, 543–551.

Bigalke, J.M., Dames, S.A., Blankenfeldt, W., Grzesiek, S. and Geyer, M. (2011). Structure and dynamics of a stabilized coiled-coil domain in the P-TEFb regulator Hexim1. J. Mol. Biol. 414, 639–653.

Ott, M., Geyer, M. and Zhou, Q. (2011). The control of HIV transcription: Keeping RNA polymerase II on track. Cell Host Microbe 10, 426–435.

Boll, A., Jatho, A., Czudnochowski, N., Geyer, M., and Steinem, C. (2011). Mechanistic insights into the translocation of full length HIV-1 Tat across lipid membranes. Biochim. Biophys. Acta 1808, 2685–2693.

Dames, S.A., Junemann, A., Sass, H.J., Schönichen, A., Stopschinski, B.E., Grzesiek, S., Faix, J. and Geyer, M. (2011). Structure, dynamics, lipid binding, and physiological relevance of the putative GTPase-binding domain of Dictyostelium Formin C. J. Biol. Chem. 286, 36907–36920.

Mangino, G., Percario, Z.A., Fiorucci, G., Vaccari, G., Acconcia, F., Chiarabelli, C., Leone, S., Noto, A., Horenkamp, F.A., Manrique, S., Romeo, G., Polticelli, F., Geyer, M. and Affabris, E. (2011). HIV-1 Nef induces proinflammatory state in macrophages through its acidic cluster domain: Involvement of TNFa receptor associated factor 2. PLoS One 6, e22982.

Horenkamp, F.A., Breuer, S., Schulte, A., Lülf, S., Weyand, M., Saksela, K. and Geyer, M. (2011). Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly. Traffic 12, 867–877.

Breuer, S., Schievink, S.I., Schulte, A., Blankenfeldt, W., Fackler, O.T. and Geyer, M. (2011). Molecular design, functional characterization and structural basis of a protein inhibitor against the HIV-1 pathogenicity factor Nef. PLoS One 6, e20033.

Dames, S.A., Schönichen, A. and Geyer, M. (2011). 1H, 15N, and 13C assignments of the N-terminal activation domain of Dictyostelium discoideum Formin C. Biomol. NMR Assign. 5, 47–49.

Bigalke, J.M., Czudnochowski, N., Vollmuth, F., Vogel-Bachmayr, K., Anand, K. and Geyer, M. (2011). Formation of Tat–TAR containing ribonucleoprotein complexes for biochemical and structural analyses. Methods 53, 78–84.

Spoerner, M., Hozsa, C., Poetzl, J.A., Reiss, K., Ganser, P., Geyer, M., Kalbitzer, H.R. (2010). Conformational states of human rat sarcoma (Ras) protein complexed with its natural ligand GTP and their role for effector interaction and GTP hydrolysis. J. Biol. Chem. 285, 39768–39778.

Vollmuth, F. and Geyer, M. (2010). Interaction of propionylated and butyrylated histone H3 lysine marks with Brd4 bromodomains. Angew. Chem. Int. Ed. Engl. 49, 6768–6772.

Asztalos, B.F., Mujawar, Z., Morrow, M.P., Grant, A., Pushkarsky, T., Wanke, C., Shannon, R., Geyer, M., Kirchhoff, F., Sviridov, D., Fitzgerald, M.L., Bukrinsky, M., and Mansfield, K.G. (2010). Circulating Nef induces dyslipidemia in simian immunodeficiency virus–infected macaques by suppressing cholesterol efflux. J. Infect. Dis. 202, 614–623.

Schönichen, A., Bigalke, J.M., Urbanke, C., Grzesiek, S., Dames, S.A. and Geyer, M. (2010). A flexible bipartite coiled coil structure is required for the interaction of Hexim1 with the P-TEFb subunit Cyclin T1. Biochemistry 49, 3083–3091.

Etzkorn, M., Seidel, K., Li, L., Martell, S., Geyer, M., Engelhard, M. and Baldus, M. (2010). Complex formation and light activation in membrane-embedded sensory rhodopsin II as seen by solid-state NMR spectroscopy. Structure 18, 293–300.

Schönichen, A. and Geyer, M. (2010). Fifteen formins for an actin filament: a molecular view on the regulation of human formins. Biochim. Biophys. Acta 1803, 152–163.

Czudnochowski, N., Vollmuth, F., Baumann, S., Vogel-Bachmayr, K. and Geyer, M. (2010). Specificity of Hexim1 and Hexim2 complex formation with Cyclin T1/T2, Importin α and 7SK snRNA. J. Mol. Biol. 395, 28–41.

Gerlach, H., Laumann, V., Martens, A., Becker, C.F., Goody, R.S. and Geyer, M. (2010). HIV-1 Nef membrane association depends on charge, curvature, composition and sequence. Nat. Chem. Biol. 6, 46–53.

Vollmuth, F., Blankenfeldt, W. and Geyer, M. (2009). Structures of the dual bromodomains of the P-TEFb-activating protein Brd4 at atomic resolution. J. Biol. Chem. 284, 36547–36556.

Erlmann, P., Schmid, S., Horenkamp, F.A., Geyer, M., Pomorski, T.G. and Olayioye, M.A. (2009). DLC1 activation requires lipid interaction through a polybasic region preceding the RhoGAP domain. Mol. Biol. Cell 20, 4400–4411.

Mishra, R., Geyer, M. and Winter, R. (2009). NMR spectroscopic investigation of early events in IAPP amyloid fibril formation. ChemBioChem 10, 1769–1772.

Szilluweit, R., Boll, A., Lukowski, S., Gerlach, H., Fackler, O.T., Geyer, M. and Steinem, C. (2009). HIV-1 Nef perturbs artificial membranes: investigation of the contribution of the myristoyl anchor. Biophys. J. 96, 3242–3250.

Bergbrede, T., Chuky, N., Schoebel, S., Blankenfeldt, W., Geyer, M., Fuchs, E., Goody, R.S., Barr, F. and Alexandrov, K. (2009). Biophysical analysis of the interaction of Rab6a GTPase with its effector domains. J. Biol. Chem. 284, 2628–2635.

Anand, K., Schulte, A., Vogel-Bachmayr, K., Scheffzek, K. and Geyer, M. (2008). Structural insights into the Cyclin T1–Tat–TAR RNA transcription activation complex from EIAV. Nat. Struct. Mol. Biol. 15, 1287–1292.

Hannemann, S., Madrid, R., Stastna, J., Kitzing, T., Gasteier, J., Schönichen, A., Bouchet, J., Jimenez, A., Geyer, M., Grosse, R., Benichou, S. and Fackler, O.T. (2008). The Diaphanous-related formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing. J. Biol. Chem. 283, 27891–27903.

Vaz, E., Pomerantz, W.C., Geyer, M., Gellman, S.H. and Brunsveld, L. (2008). Comparison of design strategies for promotion of -peptide 14-helix stability in water. ChemBioChem 9, 2254–2259.

Schulte, A., Stolp, B., Schönichen, A., Pylypenko, O., Rak, A., Fackler, O.T. and Geyer, M. (2008). The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation. Structure 16, 1313–1323.

Jadlowsky, J.K., Nojima, M., Schulte, A., Geyer, M., Okamoto, T. and Fujinaga, K. (2008). Dominant negative mutant Cyclin T1 proteins inhibit HIV transcription by specifically degrading Tat. Retrovirology 5:63.

Pylypenko, O., Schönichen, A., Ludwig, D., Ungermann, C., Goody, R.S., Rak, A. and Geyer, M. (2008). Farnesylation of the SNARE protein Ykt6 increases its stability and helical folding. J. Mol. Biol. 377, 1334–1345.

Brügger, B., Krautkrämer, E., Tibroni, N., Munte, C.E., Rauch, S., Leibrecht, I., Glass, B., Breuer, S., Geyer, M., Kräusslich, H.G., Kalbitzer, H.R., Wieland, F.T. and Fackler, O.T. (2007). Human immunodeficiency virus type 1 Nef protein modulates the lipid composition of virions and host cell membrane microdomains. Retrovirology 4:70.

Schulte, A., Rak, A., Pylypenko, O., Ludwig, D. and Geyer, M. (2007). Purification, crystallization and preliminary structural characterization of the N-terminal region of the human formin-homology protein FHOD1. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63, 878–881.

Dames, S.A., Schönichen, A., Schulte, A., Barboric, M., Peterlin, B.M., Grzesiek, S., and Geyer, M. (2007). Structure of the Cyclin T binding domain of Hexim1 and molecular basis for its recognition of P-TEFb. Proc. Natl Acad. Sci. USA 104, 14312–14317.

Anand, K., Schulte, A., Fujinaga, K., Scheffzek, K. and Geyer, M. (2007). Cyclin box structure of the P-TEFb subunit Cyclin T1 derived from a fusion complex with EIAV Tat. J. Mol. Biol. 370, 826–836.

Barboric, M., Yik, J.H., Czudnochowski, N., Yang, Z., Chen, R., Contreras, X., Geyer, M., Peterlin, B.M. and Zhou, Q. (2007). Tat competes with HEXIM1 to increase the active pool of P-TEFb for HIV-1 transcription. Nucleic Acids Res. 35, 2003–2012.

Mangino, G., Percario, Z.A., Fiorucci, G., Vaccari, G., Manrique, S., Romeo, G., Federico, M., Geyer, M. and Affabris, E. (2007). In vitro treatment of human monocyte/macrophages with myristoylated recombinant Nef of human immunodeficiency virus type 1 leads to the activation of mitogen-activated protein kinases, IkappaB kinases, and interferon regulatory factor 3 and to the release of beta-Interferon. J. Virol. 81, 2777–2791.

Dames, S.A., Schönichen, A., Grzesiek, S. and Geyer, M. (2006) NMR assignment of the Cyclin T-binding domain of human Hexim1. J. Biomol. NMR 36, 39.

Giese, S.I., Woerz, I., Homann, S., Tibroni, N., Geyer, M. and Fackler, O.T. (2006). Specific and distinct determinants mediate membrane binding and lipid raft incorporation of HIV-1SF2 Nef. Virology 355, 175–191.

Lehmann, M.H., Walter, S., Ylisastigui, L., Striebel, F., Ovod, V., Geyer, M., Gluckman, J.C. and Erfle, V. (2006). Extracellular HIV-1 Nef increases migration of monocytes. Exp. Cell Res. 312, 3659–3668.

Schönichen, A., Alexander, M., Gasteier, J.E., Cuesta, F.E., Fackler, O.T. and Geyer, M. (2006). Biochemical characterization of the Diaphanous autoregulatory interaction in the Formin-homology protein FHOD1. J. Biol. Chem. 281, 5084–5093.

Breuer, S., Gerlach, H., Kolaric, B., Urbanke, C., Opitz, N. and Geyer, M. (2006). Biochemical indication for myristoylation-dependent conformational changes in HIV-1 Nef. Biochemistry 45, 2339–2349.

Mandic, R., Schamberger, C.J., Müller, J.F., Geyer, M., Zhu, L., Carey, T.E., Grénman, R., Dünne, A.A. and Werner, J.A. (2005). Reduced cisplatin sensitivity of head and neck squamous cell carcinoma cell lines correlates with mutations affecting the COOH-terminal nuclear localization signal of p53. Clin. Cancer Res. 11, 6845–6852.

Schulte, A., Czudnochowski, N., Barboric, M., Schönichen, A., Blazek, D., Peterlin, B.M. and Geyer, M. (2005). Identification of a Cyclin T-binding domain in Hexim1 and biochemical analysis of its binding competition with HIV-1 Tat. J. Biol. Chem. 280, 24968–24977.

Madrid, R., Gasteier, J.E., Bouchet, J., Schröder, S., Geyer, M., Benichou, S. and Fackler, O.T. (2005). Oligomerization of the Diaphanous-related formin FHOD1 requires a coiled-coil motif critical for its cytoskeletal and transcriptional activities. FEBS Lett. 579, 441–448.

Geyer, M., Wilde, C., Selzer, J., Aktories, K. and Kalbitzer, H.R. (2003). Glucosylation of Ras by Clostridium sordellii lethal toxin: Consequences for effector loop conformations observed by NMR spectroscopy. Biochemistry 42, 11951–11959.

Nekrep, N., Fontes, J.D., Geyer, M. and Peterlin, B.M. (2003). When the lymphocyte loses its clothes. Immunity 18, 453–457.

Fujinaga, K., Irwin, D., Taube, R., Zhang, F., Geyer, M. and Peterlin, B.M. (2002). A minimal chimera of human Cyclin T1 and Tat binds TAR and activates human immunodeficiency virus transcription in murine cells. J. Virol. 76, 12934–12939.

Stumber, M., Geyer, M., Graf, R., Kalbitzer, H.R., Scheffzek, K. and Haeberlen, U. (2002). Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid state NMR spectroscopy. J. Mol. Biol. 323, 899–907.

Fujinaga, K., Irwin, D., Geyer, M. and Peterlin, B.M. (2002). Optimized chimeras between kinase-inactive mutant Cdk9 and truncated Cyclin T1 proteins efficiently inhibit Tat transactivation and human immunodeficiency virus gene expression. J. Virol. 76, 10873–10881.

Nekrep, N., Jabrane-Ferrat, N., Wolf, H.M., Eibl, M.M., Geyer, M. and Peterlin B.M. (2002). Mutation in a winged-helix DNA-binding motif causes atypical bare lymphocyte syndrome. Nature Immunology 3, 1075–1081.

Geyer, M., Yu, H., Mandic, R. , Linnemann, T., Zheng, Y.H., Fackler, O.T. and Peterlin, B.M. (2002). Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery. J. Biol. Chem. 277, 28521–28529.

Stumber, M., Herrmann, C., Wohlgemuth, S., Kalbitzer, H.R., Jahn, W. and Geyer, M. (2002). Synthesis, Characterization and Application of two Nucleoside Triphosphate Analogues, GTPNH2 and GTPF. Eur. J. Biochem. 269, 3270–3278.

Geyer, M., Fackler, O.T. and Peterlin, B.M. (2002). Subunit H of the V-ATPase involved in endocytosis shows homology to -adaptins. Mol. Biol. Cell 13, 2045–2056.

Fackler, O.T., Wolf, D., Weber, H.O., Laffert, B., D’Aloja, P., Schuler-Thurner, B., Geffin, R., Saksela, K., Geyer, M., Peterlin, B.M., Schuler, G. and Baur, A.S. (2001). A natural variability in the proline-rich motif of Nef modulates HIV-1 replication in primary T cells. Curr. Biol. 11, 1294–1299.

Nekrep, N., Geyer, M., Jabrane-Ferrat, N. and Peterlin, B.M. (2001). Analysis of ankyrin repeats reveals how a single point mutation in RFXANK results in bare lymphocyte syndrome. Mol. Cell. Biol. 21, 5566–5576.

Geyer, M., Fackler, O.T. and Peterlin, B.M. (2001). Structure–function relationships in HIV-1 Nef. EMBO Rep. 2, 580–585.

Geyer, M. and Peterlin, B.M. (2001). Domain assembly, surface accessibility and sequence conservation in full length HIV-1 Nef. FEBS Lett. 496, 91–95.

Kremer, W., Schuler, B., Harrieder, S., Geyer, M., Gronwald, W., Welker, C., Jaenicke, R. and Kalbitzer, H.R. (2001). Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima. Eur. J. Biochem. 268, 2527–2539.

Boese, A., Galli, U., Geyer, M., Sauter, M. and Mueller-Lantzsch, N. (2001). The Rev/Rex homolog HERV-K cORF multimerizes via a C-terminal domain. FEBS Lett. 493, 117–121.

Mandic, R., Fackler, O.T., Geyer, M., Linnemann, T., Zheng, Y.H. and Peterlin, B.M. (2001). Negative factor from SIV binds to the catalytic subunit of the V-ATPase to internalize CD4 and to increase viral infectivity. Mol. Biol. Cell 12, 463–473.

Steiner, G., Kremer, W., Linnemann, T., Herrmann, C., Geyer, M. and Kalbitzer, H.R. (2000). Letter to the Editor: Sequence-specific resonance assignment of the Ras-binding domain of AF6. J. Biomol. NMR 18, 73–74.

Huber, F., Gronwald, W., Wohlgemuth, S., Herrmann, C., Geyer, M., Wittinghofer, A. and Kalbitzer, H.R. (2000). Letter to the Editor: Sequential NMR assignment of the Ras-binding domain of Byr2. J. Biomol. NMR 16, 355–356.

Fackler, O.T., Lu, X., Frost, J.A., Geyer, M., Jiang, B., Luo, W., Abo, A., Alberts, A.S. and Peterlin, B.M. (2000). p21-activated kinase 1 plays a critical role in cellular activation by Nef. Mol. Cell. Biol. 20, 2619–2627.

Taube, R., Fujinaga, K., Irwin, D., Wimmer, J., Geyer, M. and Peterlin, B.M. (2000). Interactions between equine cyclin T1, Tat and TAR are disrupted by a leucine to valine substitution found in human Cyclin T1. J. Virol. 74, 892–898.

before 2000
Praefcke, G.J., Geyer, M., Schwemmle, M., Kalbitzer, H.R. and Herrmann, C. (1999) Nucleotide-binding characteristics of human guanylate-binding protein 1 (hGBP1) and identification of the third GTP-binding motif. J. Mol. Biol. 292, 321–332.

Geyer, M., Assheuer, R., Klebe, C., Kuhlmann, J., Becker, J., Wittinghofer, A. and Kalbitzer, H.R. (1999). Conformational states of the nuclear GTP-binding protein Ran and its complexes with the exchange factor RCC1 and the effector protein RanBP1. Biochemistry 38, 11250–11260.

Fackler, O.T., Luo, W., Geyer, M., Alberts, A.S. and Peterlin, B.M. (1999). Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions. Mol. Cell 3, 729–739.

Plemenitas, A., Lu, X., Geyer, M., Veranic, P., Simon, M.N. and Peterlin, B.M. (1999). Activation of Ste20 by Nef from human immunodeficiency virus induces cytoskeletal rearrangements and downstream effector functions in Saccharomyces cerevisiae. Virology 258, 271–281.

Geyer, M., Munte, C.E., Schorr, J., Kellner, R. and Kalbitzer, H.R. (1999). Structure of the anchor domain of myristoylated and non-myristoylated HIV-1 Nef protein. J. Mol. Biol. 289, 123–138.

Vetter, I.R., Linnemann, T., Wohlgemuth, S., Geyer, M., Kalbitzer, H.R., Herrmann, C. and Wittinghofer, A. (1999). Structural and biochemical analysis on Ras-effector signaling via RalGDS. FEBS Lett. 451, 175–180.

Linnemann, T., Geyer, M., Jaitner, B.K., Block, C., Kalbitzer, H.R., Wittinghofer, A. and Herrmann, C. (1998). Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily. J. Biol. Chem. 274, 13556–13562.

Geyer, M. and Wittinghofer, A. (1997). GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins, Curr. Op. Struct. Biol. 7, 786–792.

Geyer, M., Herrmann, C., Wohlgemuth, S., Wittinghofer, A. and Kalbitzer, H.R. (1997). Structure of the Ras-binding domain of RalGEF and implications for Ras-binding and signalling. Nat. Struct. Biol. 4, 694–699.

Antz, C., Geyer, M., Fakler, B., Schott, M.K., Guy, H.R., Frank, R., Ruppersberg, J.P. and Kalbitzer, H.R. (1997). NMR structure of inactivation gates from mammalian voltage-dependent potassium channels. Nature 385, 272–275.

Schweins, T., Geyer, M., Kalbitzer, H.R., Wittinghofer, A. and Warshel, A. (1996). Linear free energy relationships in the intrinsic and GTPase activating protein-stimulated guanosine 5′-triphosphate hydrolysis of p21ras. Biochemistry 35, 14225–14231.

Raditsch, M., Geyer, M., Kalbitzer, H.R., Jahn, W., Ruppersberg, J.P. and Witzemann, V. (1996). Polyamine spider toxins and mammalian N-methyl-D-aspartate receptors: Structural basis for channel block and binding of argiotoxin636. Eur. J. Biochem. 240, 416–426.

Geyer, M., Schweins, T., Herrmann, C., Prisner, T., Wittinghofer, A. and Kalbitzer, H.R. (1996). Conformational transitions in p21ras and in its complexes with the effector protein Raf-RBD and the GTPase activating protein GAP. Biochemistry 35, 10308–10320.

Neidig, K.P., Geyer, M., Görler, A., Antz, C., Saffrich, R., Beneicke, W. and Kalbitzer, H.R. (1995) AURELIA, a program for computer-aided analysis of multidimensional NMR spectra. J. Biomol. NMR 6, 255–270.

Geyer, M., Neidig, K.P. and Kalbitzer, H.R. (1995). Automated peak integration in multidimensional NMR spectra by an optimized iterative segmentation procedure. J. Magn. Reson. Series B 109, 31–38.

Schweins, T., Geyer, M., Scheffzek, K., Warshel, A., Kalbitzer, H.R. and Wittinghofer, A. (1995). Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteins. Nat. Struct. Biol. 2, 36–44.

Franken, S.M., Scheidig, A.J., Krengel, U., Rensland, H., Lautwein, A., Geyer, M., Scheffzek, K., Goody, R.S., Kalbitzer, H.R., Pai, E.F. and Wittinghofer, A. (1993). Three-dimensional structures and properties of a transforming and a non-transforming glycine-12 mutant of p21H-ras. Biochemistry 32, 8411–8420.