Kögel A, Keidel A, Loukeri MJ, Kuhn CC, Langer LM, Schäfer IB, Conti E. Structural basis of mRNA decay by the human exosome–ribosome supercomplex. Nature. 2024; 635(8037):237-242. doi: 10.1038/s41586-024-08015-6

Keidel A, Kögel A , Reichelt P, Kowalinski E , Schäfer IB , Conti E. Concerted structural rearrangements enable RNA channeling into the cytoplasmic Ski238-Ski7-exosome assembly. Mol Cell. 2023;83(22):4093-4105.e7. doi: 10.1016/j.molcel.2023.09.037

Bonneau F, Basquin J, Steigenberger B, Schäfer T, Schäfer IB, Conti E. Nuclear mRNPs are compact particles packaged with a network of proteins promoting RNA-RNA interactions. Genes Dev. 2023;37(11-12):505-517. doi: 10.1101/gad.350630.123

Mauxion F, Basquin J, Ozgur S, Rame M, Albrecht J, Schäfer I, Seraphin B, Conti E. The human CNOT1-CNOT10-CNOT11 complex forms a structural platform for protein-protein interactions. Cell Rep. 2023;42(1):111902. doi: 10.1016/j.celrep.2022.111902

Xiong X, Blakely A, Kim JH, Menting JG, Schäfer IB, Schubert HL, Agrawal R, Gutmann T, Delaine C, Zhang YW, Artik GO, Merriman A, Eckert D, Lawrence MC, Coskun Ü, Fisher SJ, Forbes BE, Safavi-Hemami H, Hill CP, Hung-Chieh Chou D. Symmetric and asymmetric receptor conformation continuum induced by a new insulin. Nat Chem Biol. 2022;18(5):511-519. doi: 10.1038/s41589-022-00981-0

Kögel A, Keidel A, Bonneau F, Schäfer IB, Conti E. The human SKI complex regulates channeling of ribosome-bound RNA to the exosome via an intrinsic gatekeeping mechanism. Mol Cell. 2022;82(4):756-769.e8. doi: 10.1016/j.molcel.2022.01.009

Taschner M, Basquin J, Steigenberger B, Schäfer IB, Soh YM, Basquin C, Lorentzen E, Räschle M, Scheltema RA, Gruber S. Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding. EMBO J. 2021;40(15):e107807. doi: 10.15252/embj.2021107807

Finogenova K, Bonnet J, Poepsel, S, Schäfer IB, Finkl K, Schmid K, Litz C, Strauss M, Benda C, Müller J. Structural basis for PRC2 decoding of active histone methylation marks H3K36me2/3. Elife. 2020:9:e61964. doi: 10.7554/eLife.61964

Gutmann T, Schäfer IB, Poojari C, Brankatschk B, Vattulainen I, Strauss M, Coskun Ü. Cryo-EM structure of the complete and ligand-saturated insulin receptor ectodomain. J Cell Biol. 2020;219(1):e201907210. doi: 10.1083/jcb.201907210

Ali‐Ahmad A, Bilokapić S, Schäfer IB, Halić M, Sekulić N. CENP-C unwraps the human CENP-A nucleosome through the H2A C-terminal tail. EMBO Rep. 2019;20(10):e48913. doi: 10.15252/embr.201948913

Schäfer IB, Yamashita M, Schuller JM, Schüssler S, Reichelt P, Strauss M, Conti E. Molecular Basis for poly(A) RNP Architecture and Recognition by the Pan2-Pan3 Deadenylase. Cell. 2019;177(6):1619-1631.e21. doi: 10.1016/j.cell.2019.04.013

Schäfer IB, Rode M, Bonneau F, Schüssler S, Conti E. The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase. Nat Struct Mol Biol. 2014;21(7):591-8. doi: 10.1038/nsmb.2834

Hesketh GG, Pérez-Dorado I, Jackson LP, Wartosch L, Schäfer IB, Gray SR, McCoy AJ, Zeldin OB, Garman EF, Harbour ME, Evans PR, Seaman MNJ, Luzio JP, Owen DJ. VARP Is Recruited on to Endosomes by Direct Interaction with Retromer, Where Together They Function in Export to the Cell Surface. Dev Cell. 2014;29(5):591-606.
doi: 10.1016/j.devcel.2014.04.010

Schäfer IB, Hesketh GG, Bright NA , Gray SR, Pryor PR, Evans PR, Luzio JP, Owen DJ. The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically inactive conformation. Nat Struct Mol Biol. 2012;19(12):1300-9. doi: 10.1038/nsmb.2414

Kent HM, Evans PR, Schäfer IB, Gray SR, Sanderson CM, Luzio JP, Peden AA, Owen DJ. Structural basis of the intracellular sorting of the SNARE VAMP7 by the AP3 adaptor complex. Dev Cell. 2012;22(5):979-88. doi: 10.1016/j.devcel.2012.01.01

Riento K, Frick M, Schafer I, Nichols BJ. Endocytosis of flotillin-1 and flotillin-2 is regulated by Fyn kinase. J Cell Sci. 2009;122(Pt 7):912-8. doi: 10.1242/jcs.039024

Schäfer IB, Bailer SM, Düser MG, Börsch M, Bernal RA, Stock D, Grüber G. Crystal structure of the archaeal A1Ao ATP synthase subunit B from Methanosarcina mazei Gö1: Implications of nucleotide-binding differences in the major A1Ao subunits A and B. J Mol Biol. 2006;358(3):725-40. doi: 10.1016/j.jmb.2006.02.057

Schäfer I, Rössle M, Biuković G, Müller V, Grüber G. Structural and functional analysis of the coupling subunit F in solution and topological arrangement of the stalk domains of the methanogenic A1AO ATP synthase. J Bioenerg Biomembr. 2006;38(2):83-92.
doi: 10.1007/s10863-006-9015-4