Prof. Dr. Stefan Raunser

Stefan Raunser

Director, Structural Biochemistry


Publications

PubMed List>

> Publication list 10/2024 as PDF 

2024

Boiero Sanders M, Oosterheert W, Hofnagel O, Bieling P, Raunser S (2024). Phalloidin and DNase I-bound F-actin pointed end structures reveal principles of filament stabilization and disassembly.  Nat Commun
Source

Oosterheert W, Boiero Sanders M, Funk J, Prumbaum D, Raunser S, Bieling P (2024). Molecular mechanism of actin filament elongation by formins.  Science
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Redhardt M, Raunser S, Raisch T (2024). Cryo-EM structure of the Slo1 potassium channel with the auxiliary γ1 subunit suggests a mechanism for depolarization-independent activation.  FEBS Lett.
Source

Polley S, Raisch T, Ghetti S, Körner M, Terbeck M, Gräter F, Raunser S, Aponte-Santamaria Camilo, Vetter IR, Musacchio A (2024). Structure of the human KMN complex and implications for regulation of its assembly. NSMB
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Sitsel O, Wang Z, Janning P, Kroczek L, Wagner T, Raunser S (2024). Yersinia entomophaga Tc toxin is released by T10SS-dependent lysis of specialized cell subpopulations. Nature Microbiology
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2023

Belyy A, Heilen P, Hagel P, Hofnagel O, Raunser S (2023). Structure and activation mechanism of the Makes caterpillars floppy 1 toxin. Nat Commun
Source

Tamborrini D, Wang Z, Wagner T, Tacke S, Stabrin S, Grange M, Kho AL, Rees M, Bennet P, Gautel M, Raunser S (2023). Structure of the native myosin filament in the relaxed cardiac sarcomere. Nature
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Raisch T, Raunser S (2023). The modes of action of ion-channel-targeting neurotoxic insecticides: lessons from structural biology. Nat Struct Mol Biol.
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Oosterheert W, Blanc FEC, Roy A, Belyy A, Sanders MB, Hofnagel O, Hummer G, Bieling P, Raunser (2023). Molecular mechanisms of inorganic-phosphate release from the core and barbed end of actin filaments. Nat Struct Mol Biol.
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Quentin D, Schuhmacher JS, Klink BU, Lauer J, Shaikh TR, Huis In ’t Veld PJ, Welp LM, Urlaub H, Zerial M, Raunser S (2023). Structural basis of mRNA binding by the human FERRY Rab5 effector complex. Mol Cell
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Rice G, Wagner T, Stabrin M, Sitsel O, Prumbaum D, Raunser S (2023). TomoTwin: generalized 3D localization of macromolecules in cryo-electron tomograms with structural data mining. Nature Methods
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Wang Z, Raunser S (2023). Structural Biochemistry of Muscle Contraction. Annu Rev Biochem
Source

Bürgi J, Lill P, Giannopoulou EA, Jeffries CM, Chojnowski G, Raunser S, Gatsogiannis C, Wilmanns M (2022). Asymmetric horseshoe-like assembly of peroxisomal yeast oxalyl-CoA synthetase. Biol Chem
Source

2022

Boltje DB, Hoogenboom JP, Jakobi AJ, Jensen GJ, Jonker CTH, Kaag MJ, Koster AJ, Last MGF, de Agrela Pinto C, Plitzko JM, Raunser S, Tacke S, Wang Z, van der Wee EB, Wepf R, den Hoedt S (2022). A cryogenic, coincident fluorescence, electron and ion beam microscope. eLife
Source

Oosterheert W, Klink B. U, Belyy A, Pospich S, Raunser S (2022). Structural Basis of actin filament assembly and aging. Nature
Source

Xu Y, Viswanatha R, Sitsel O, Roderer D, Zhao H, Ashwood C, Voelcker C, Tian S, Raunser S, Perrimon N, Dong M (2022). CRISPR screens in Drosophila cells identify Vsg as a Tc toxin receptor. Nature
Source

Schöenfeld F, Stabrin M, Shaikh TR, Wagner T, Raunser S (2022). Accelerated 2D Classification With ISAC Using GPUs. Front Mol Biosci.
Source

Belyy A, Lindemann F, Roderer D, Funk J, Bardiaux B, Protze J, Bieling P, Oschkinat H, Raunser S (2022). Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin. Nat Commun
Source

Pesenti ME, Raisch T, Conti D, Walstein K, Hoffmann I, Vogt D, Prumbaum D, Vetter IR, Raunser S, Musacchio A (2022). Structure of the human inner kinetochore CCAN complex and its significance for human centromere organization. Mol Cell
Source

Raisch T, Ciossani G, d'Amico E, Cmentowski V, Carmignani S, Maffini S, Merino F, Wohlgemuth S, Vetter IR, Raunser S, Musacchio A (2022). Structure of the RZZ complex and molecular basis of Spindly-driven corona assembly at human kinetochores. EMBO J
Source

Urlaub D, Wolfsdorff N, Hoffmann JE, Dorok S, Hoffmann M, Anft M, Pieris N, Günther P, Schaaf B, Cassens U, Bröde P, Claus M, Picard LK, Wingert S, Backes S, Durak D, Babel N, Pöhlmann S, Renken F, Raunser S, Watzl C (2022). Neutralizing antibody responses 300 days after SARS-CoV-2 infection and induction of high antibody titers after vaccination. Eur J Immunol.
Source

Wang Z, Grange M, Pospich S, Wagner T, Kho A.L, Gautel M, Raunser S (2022). Structures from intact myofibrils reveal mechanism of thin filament regulation through nebulin. Science
Source

Link to freely available Paper!

Klink BU, Herrmann E, Antoni C, Langemeyer L, Kiontke S, Gatsogiannis C, Ungermann C, Kümmel D, Raunser S (2022). Structure of the Mon1-Ccz1 complex reveals molecular basis of membrane binding for Rab7 activation. Proc Natl Acad Sci U S A
Source

Günther P, Quentin D, Ahmad S, Sachar K, Gatsogiannis C, Whitney JC, Raunser S (2022). Structure of a bacterial Rhs effector exported by the type VI secretion system. PLoS Pathog 
Source


2021

Raisch T, Brockmann A, Ebbinghaus-Kintscher U, Freigang J, Gutbrod O, Kubicek J, Maertens B, Hofnagel O, Raunser S (2021). Small molecule modulation of the Drosophila Slo channel elucidated by cryo-EM. Nat Commun 
Source

Chen M, Blum D, Engelhard L, Raunser S , Wagner R & Gatsogiannis C (2021). Molecular architecture of black widow spider neurotoxins. Nat Commun 
Source

Pospich S, Sweeney HL, Houdusse A, Raunser S (2021). High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. eLife 
Source

Belyy A, Merino F, Mechold U, Raunser S (2021). Mechanism of actin-dependent activation of nucleotidyl cyclase toxins from bacterial human pathogens. Nat Commun. 
Source

Schoppe J, Schubert E, Apelbaum A, Yavavli E, Birkholz O, Stephanowitz H, Han Y, Perz A, Hofnagel O, Liu F, Piehler J, Raunser S, Ungermann C (2021). Flexible open conformation of the AP-3 complex explains its role in cargo recruitment at the Golgi. J Biol Chem. 
Source

Funk J, Merino F, Schaks M, Rottner K, Raunser S, Bieling P (2021). A barbed end interference mechanism reveals how capping protein promotes nucleation in branched actin networks. Nature Communications 
Source

Yu J, Raia P, Ghent CM, Raisch T, Sadian Y, Cavadini S, Sabale PM, Barford D, Raunser S, Morgan DO, Boland A (2021). Structural basis of human separase regulation by securin and CDK1-cyclin B1 Nature  
Source

Oliva R, Mukherjee SK, Ostermeier L, Pazurek LA, Kriegler S, Bader V, Prumbaum D, Raunser S, Winklhofer KF, Tatzelt J, Winter RHA (2021). Remodeling of the Fibrillation Pathway of α-Synuclein by Interaction with Antimicrobial Peptide LL-III Chemistry  
Source

Fitzian K, Brückner A, Brohée L, Zech R, Antoni C, Kiontke S, Gasper R, Linard Matos AL, Beel S, Wilhelm S, Gerke V, Ungermann C, Nellist M, Raunser S, Demetriades C, Oeckinghaus A, Kümmel D (2021). TSC1 binding to lysosomal PIPs is required for TSC complex translocation and mTORC1 regulation  Mol Cell  
Source

Klika Skopic M, Gramse C, Oliva R, Pospich S, Neukirch L, Manisegaran M, Raunser S, Winter R, Weberskirch R, Brunschweiger A (2021). Towards DNA-encoded Micellar Chemistry: DNA-micelle Association and Environment-sensitivity of Catalysis.  Chemistry  
Source

Tacke S, Erdmann P, Wang Z, Klumpe S, Grange M, Plitzko J, Raunser S (2021). A streamlined workflow for automated cryo focused ion beam milling  J Struct Biol  
Source

Wang Z, Grange M, Wagner T, Kho AL, Gautel M, Raunser S (2021). The molecular basis for sarcomere organization in vertebrate skeletal muscle  Cell  
Source

Pospich S, Küllmer F, Nasufovic V, Funk J, Belyy A, Bieling P, Arndt HD, Raunser S (2021). Cryo-EM resolves molecular recognition of an optojasp photoswitch bound to actin filaments in both switch states.  Angew Chem Int Ed Engl.  
Source


2020

Ahmad S, Tsang KL, Sachar K, Quentin D, Tashin TM, Bullen NP, Raunser S, McArthur AG, Prehna G, Whitney JC. (2020). Structural basis for effector transmembrane domain recognition by type VI secretion system chaperones.  Elife  
Source

Vinayagam D, Quentin D, Yu-Strzelczyk J, Sitsel O, Merino F, Stabrin M, Hofnagel O, Yu M, Ledeboer MW, Nagel G, Malojcic G, Raunser S. (2020). Structural basis of TRPC4 regulation by calmodulin and pharmacological agents Elife  
Source

Belyy A, Merino F, Sitsel O, Raunser S. (2020). Structure of the Lifeact-F-actin complex PLoS Biol.  
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Stabrin M, Schoenfeld F, Wagner T, Pospich S, Gatsogiannis C, Raunser S (2020). TranSPHIRE: automated and feedback-optimized on-the-fly processing for cryo-EM Nat Commun 
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Antoni C, Quentin D, Lang AE, Aktories K, Gatsogiannis C, Raunser S (2020). Cryo-EM structure of the fully-loaded asymmetric anthrax lethal toxin in its heptameric pre-pore state PLoS Path 
doi:10.1371/journal.ppat.1008530

Roderer D, Bröcker F, Sitsel O, Kaplonek P, Leidreiter F, Seeberger PH, Raunser S (2020). Glycan-dependent cell adhesion mechanism of Tc toxins. Nat Commun 
doi:10.1038/s41467-020-16536-7

Pospich S, Merino F, Raunser S (2020). Structural Effects and Functional Implications of Phalloidin and Jasplakinolide Binding to Actin Filaments. Structure 
doi:10.1016/j.str.2020.01.014

Wagner T, Raunser S (2020). The evolution of SPHIRE-crYOLO particle picking and its application in automated cryo-EM processing workflows. Communications Biology
doi:10.1038/s42003-020-0790-y

Wagner T, Lusnig L, Pospich S, Stabrin M, Schönfeld F, Raunser S (2020).Two particle-picking procedures for filamentous proteins: SPHIRE-crYOLO filament mode and SPHIRE-STRIPER. Acta Cryst Sect D Struct Biol.
Source

Klink BU, Gatsogiannis C, Hofnagel O, Wittinghofer A, Raunser S (2020). Structure of the human BBSome core complex Elife
doi:10.7554/eLife.53910


2019

Merino F, Pospich S, Raunser S (2019). Towards a structural understanding of the remodeling of the actin cytoskeleton Semin Cell Dev Biol
https://doi.org/10.1016/j.semcdb.2019.11.018

Roderer D, Schubert E, Sitsel O, Raunser S (2019). Towards the application of Tc toxins as a universal protein translocation system Nat Comms
doi: 10.1038/s41467-019-13253-8

Roderer D, Hofnagel O, Benz R, Raunser S (2019). Structure of a Tc holotoxin pore provides insights into the translocation mechanism. PNAS
doi: 10.1073/pnas.1909821116.

Leidreiter F, Roderer D, Meusch D, Gatsogiannis C, R. Benz R, Raunser S (2019). Common architecture of Tc toxins from human and insect pathogenic bacteria. Science Advances
doi: 10.1126/sciadv.aax6497.

Gatsogiannis C, Balogh D, Merino F, Sieber SA, Raunser S (2019). Cryo-EM structure of the ClpXP protein degradation machinery. Nat Struct Mol Bio
doi: 10.1038/s41594-019-0304-0.

Raisch T, Chang CT, Levdansky Y, Muthukumar S, Raunser S, Valkov E (2019). Reconstitution of recombinant human CCR4-NOT reveals molecular insights into regulated deadenylation. Nature Communications
doi: 10.1038/s41467-019-11094-z.

Raisch T, Chang CT, Levdansky Y, Muthukumar S, Raunser S, Valkov E (2019). Reconstitution of recombinant human CCR4-NOT reveals molecular insights into regulated deadenylation. Nature Communications
doi: 10.1038/s41467-019-11094-z.

Škopić MK, Götte K, Gramse C, Dieter M, Pospich S, Raunser S, Weberskirch R, Brunschweiger A. (2019). Micellar Brønsted Acid Mediated Synthesis of DNA-Tagged Heterocycles. J Am Chem Soc
doi: 10.1021/jacs.9b05696.

Wagner T, Merino F, Stabrin S, Moriya T, Antoni C, Apelbau A, Hagel P, Sitsel O, Raisch T, Prumbaum D, Quentin D, Roderer D, Tacke S, Siebolds B, Schubert E, Shaikh TR, Lill P, Gatsogiannis C, Raunser S (2019). SPHIRE-crYOLO is a fast and accurate fullyautomated particle picker for cryo-EM. Communications Biology

doi: ttps://doi.org/10.1038/s42003-019-0437.

Roderer D, Raunser S (2019). Tc Toxin Complexes: Assembly, Membrane Permeation, and Protein Translocation. Annu Rev Microbiol
doi: 10.1146/annurev-micro-102215-095531.

Tanaka Y, Kato S, Stabrin M, Raunser S, Matsui T, Gatsogiannis C (2019). Cryo-EM reveals the asymmetric assembly of squid hemocyanin. IUCrJ
doi: 10.1107/S205225251900321X.

Sitsel O, Raunser S (201 9). Bis insights from tiny crystals. Nat Chem 
doi: 10.1038/s41557-019-0211-3. 


2018

Ludwig AK, De Miroschedji K, Doeppner TR, Börger V, Ruesing J, Rebmann V, Durst S, Jansen S, Bremer M, Behrmann E, Singer BB, Jastrow H, Kuhlmann JD, El Magraoui F, Meyer HE, Hermann DM, Opalka B, Raunser S, Epple M, Horn PA, Giebel B (2018). Precipitation with polyethylene glycol followed by washing and pelleting by ultracentrifugation enriches extracellular vesicles from tissue culture supernatants in small and large scales. J Extracell Vesicles
doi: 10.1080/20013078.2018.1528109.

Gatsogiannis C, Merino F, Roderer D, Balchin D, Schubert E, Kuhlee A, Hayer-Hartl M, Raunser S. (2018). Tc toxin activation requires unfolding and refolding of a β-propeller. Nature
doi: 10.1038/s41586-018-0556-6.

Quentin D, Ahmad S, Shanthamoorthy P, Mougous JD, Whitney JC, Raunser S (2018). Mechanism of loading and translocation of type VI secretion system effector Tse6. Nat Microbiol
doi: 10.1038/s41564-018-0238-z.

Pesenti ME, Prumbaum D, Auckland P, Smith CM, Faesen AC, Petrovic A, Erent M, Maffini S, Pentakota S, Weir JR, Lin YC, Raunser S, McAinsh AD, Musacchio A (2018). Reconstitution of a 26-Subunit Human Kinetochore Reveals Cooperative Microtubule Binding by CENP-OPQUR and NDC80. Mol Cell
doi: 10.1016/j.molcel.2018.07.038.

Pospich S, Raunser S (2018). Single particle cryo-EM-an optimal tool to study cytoskeletal proteins. Curr Opin Struct Bio
doi: 10.1016/j.sbi.2018.07.006.

Schubert E, Vetter IR, Prumbaum D, Penczek PA, Raunser S (2018). Membrane insertion of α-xenorhabdolysin in near-atomic detail. eLife
doi: 10.7554/eLife.38017.

Merino F, Pospich S, Funk J, Wagner T, Küllmer F, Arndt HD, Bieling P & Raunser S (2018). Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM. Nat Struct Mol Biol
doi: 10.1038/s41594-018-0074-0.

Quentin D, Raunser S (2018). Electron cryomicroscopy as a powerful tool in biomedical research. J Mol Med
doi: 10.1007/s00109-018-1640-y.

Vinayagam D, Mager T, Apelbaum A, Bothe A, Merino F, Hofnagel O, Gatsogiannis C, Raunser S (2018). Electron cryo-microscopy structure of the canonical TRPC4 ion channel. eLife
doi: 10.7554/eLife.36615.

Yavuz H, Kattan I, Hernandez JM, Hofnagel O, Witkowska A, Raunser S, Walla PJ, Jahn R (2018). Arrest of trans-SNARE zippering uncovers loosely and tightly docked intermediates in membrane fusion. J Biol Chem
doi: 10.1074/jbc.RA118.003313.

Merino F, Raunser S (2018). The complex simplicity of the bacterial cytoskeleton. PNAS(52):16450-16452
doi: 10.1073/pnas.1801783115.


2017

Raunser S (2017). Cryo-EM Revolutionizes the Structure Determination of Biomolecules. Angew Chem Int Ed Engl56(52):16450-16452
doi: 10.1002/anie.201710679.

Klink BU, Zent E, Juneja P, Kuhlee A, Raunser S, Wittinghofer A. (2017). A recombinant BBSome core complex and how it interacts with ciliary cargo. eLife
doi: 10.7554/eLife.27434.

Chen M, Kato K, Kubo Y, Tanaka Y, Liu Y, Long F, Whitman WB, Lill P, Gatsogiannis C, Raunser S, Shimizu N, Shinoda A, Nakamura A, Tanaka I, Yao M (2017). Structural basis for tRNA-dependent cysteine biosynthesis. Nat Commun
doi: 10.1038/s41467-017-01543-y.

Pospich S, Raunser S. (2017). The molecular basis of Alzheimer's plaques. Science
doi: 10.1126/science.aap8002.

Pospich S, Kumpula EP, von der Ecken J, Vahokoski J, Kursula I, Raunser S. (2017). Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability. Proc Natl Acad Sci U S A
doi: 10.1073/pnas.1707506114

Efremov RG, Gatsogiannis C, Raunser S (2017). Lipid Nanodiscs as a Tool for High-Resolution Structure Determination of Membrane Proteins by Single-Particle Cryo-EM. Methods in Enzymology
doi: https://doi.org/10.1016/bs.mie.2017.05.007.

Moriya T, Saur M, Stabrin M, Merino F, Voicu H, Huang Z, Penczek PA, Raunser S, Gatsogiannis C (2017). High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE. J Vis Exp
doi: 10.3791/55448.

Orekhov P, Bothe A, Steinhoff HJ, Shaitan KV, Raunser S, Fotiadis D, Schlesinger R, Klare JP, Engelhard M (2017). Sensory Rhodopsin I and Sensory Rhodopsin II Form Trimers of Dimers in Complex with their Cognate Transducers. Photochem Photobiol 93(3):796-804.
doi: 10.1111/php.12763.

Mosalaganti S, Keller J, Altenfeld A, Winzker M, Rombaut P, Saur M, Petrovic A, Wehenkel A, Wohlgemuth S, Müller F, Maffini S, Bange T, Herzog F, Waldmann H, Raunser S & Musacchio A (2017). Structure of the RZZ complex and molecular basis of its interaction with Spindly. J Cell Bio 216(4):961-981
doi: 10.1083/jcb.201611060.

Purushothaman LK, Arlt H, Kuhlee A, Raunser S, Ungermann C (2017). Retromer-driven membrane tubulation separates endosomal recycling from Rab7/Ypt7-dependent fusion. Mol Biol Cell pii: mbc.E16-08-0582.
doi: doi: 10.1091/mbc.E16-08-0582.

Kiontke S, Langemeyer L, Kuhlee A, Schuback S, Raunser S, Ungermann C, Kümmel D (2017). Architecture and mechanism of the late endosomal Rab7-like Ypt7 guanine nucleotide exchange factor complex Mon1-Ccz1. Nat Commun 8:14034.
doi: 10.1038/ncomms14034.


2016

Merino F, Raunser S (2016). The mother of all actins? eLife. 5: e23354.
doi: 10.7554/eLife.23354.

Merino F, Raunser S (2016). Cryo-EM as a tool for structure-based drug development. Angew Chem Int Ed Engl
doi: 10.1002/anie.201608432

Gatsogiannis C, Merino F, Serdiuk T, Prumbaum D, Roderer D, Leidreiter F, Meusch D, Müller DJ, and Raunser S (2016). Membrane insertion of a Tc toxin in atomic detail. Nature Structural and Molecular Biology 23(10):884-890.
doi: 10.1038/nsmb.3281
freely available!

von der Ecken J, Heissler SM, Pathan-Chhatbar S, Manstein DJ & Raunser S (2016).Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution. Nature 534(7609):724-28.
doi: 10.1038/nature18295
freely available!

Friese A, Faesen AC, Huis in´t Veld PJ, Fischböck J, Prumbaum D, Petrovic A, Raunser S, Herzog F, Musacchio A (2016). Molecular requirements for the inter-subunit interaction and kinetochore recruitment of SKAP and Astrin. Nature Communications 7, 11407:1 - 11407:12.
doi: 10.1038/ncomms11407
freely available!

Liu Y, Petrovic A, Rombaut P, Mosalaganti S, Keller J, Raunser S, Herzog F, Musacchio A (2016). Insights from the reconstitution of the divergent outer kinetochore of Drosophila melanogaster. Open Biology 6 (2), S. 1-11.
doi: 10.1038/nsmb.3281


2015

von der Ecken J, Müller M, Lehman W, Manstein DJ, Penczek PA, Raunser S (2015). Structure of the F-actin-tropomyosin complex. Nature 519(7541):114-7.
doi: 10.1038/nature14033
freely available!

Frisch H, Nie Y, Raunser S, Besenius P (2015). pH-Regulated Selectivity in Supramolecular Polymerizations: Switching between Co- and Homopolymers. Chemistry – A European Journal 21 (8), S. 3304-3309.
doi: 10.1002/chem.201406281

Gao M, Berghaus M, von der Ecken J, Raunser S, Winter R (2015). Condensation Agents Determine the Temperature-Pressure Stability of F-Actin Bundles. Angewandte Chemie International Edition 54 (38), S. 11088-11092.
doi: 10.1002/anie.201504247

Kuhlee A, Raunser S, Ungermann C (2015). Functional homologies in vesicle tethering. FEBS Letters 589 (19 Pt A), S. 2487-2497.
doi: 10.1016/j.febslet.2015.06.001

Lürick A, Kuhlee A, Bröcker C, Kümmel D, Raunser S, Ungermann C (2015). The HABC domain of the snare vam3 interacts with the hops tethering complex to facilitate vacuole fusion. The Journal of Biological Chemistry 290 (9), S. 5405-5413.
doi: 10.1074/jbc.M114.631465

Patasi C, Godočíková J, Michlíková S, Nie Y, Káčeriková R, Kválová K, Raunser S, Farkašovský M (2015). The role of Bni5 in the regulation of septin higher-order structure formation. Biological Chemistry 396 (12), S. 1325-1337.
doi: 10.1515/hsz-2015-0165

Poepsel S, Sprengel A, Sacca B, Kaschani F, Kaiser M, Gatsogiannis C, Raunser S, Clausen T, Ehrmann M (2015). Determinants of amyloid fibril degradation by the PDZ protease HTRA1. Nature Chemical Biology 11 (11), S. 862-869.
doi: 10.1038/nchembio.1931
freely available!

Raunser S, Gatsogiannis C (2015). Deciphering the Tubulin Code. Cell 161 (5), S. 960-961.
doi: 10.1016/j.cell.2015.05.004

Whitney JC, Quentin D, Sawai S, LeRoux M, Harding B, Ledvina HE, Tran BQ, Robinson H, Goo YA, Goodlett DR, Raunser S, Mougous JD (2015). An Interbacterial NAD(P)+ Glycohydrolase Toxin Requires Elongation Factor Tu for Delivery to Target Cells. Cell 163 (3), S. 607-619.
doi: 10.1016/j.cell.2015.09.027

Efremov R, Hofnagel O, Raunser S (2015). Architecture and Conformational Switch Mechanism of the Ryanodine Receptor. Nature 517(7532):39-43.
doi: 10.1038/nature13916
freely available!

Gatsogiannis C, Hofnagel O, Markl J, Raunser S (2015). Structure of Mega-Hemocyanin Reveals Protein Origami in Snails. Structure 23 (1), S. 93-103.
doi: 10.1016/j.str.2014.10.013


2014

Basilico F, Maffini S, Weir J, Prumbaum D, Rojas AM, Zimniak T, De Antoni A, Jeganathan S, Voss B, Van Gerwen S, Krnn V, Massimiliano L, Valencia A, Vetter IR, Herzog F, Raunser S, Pasqualato S, Musacchio A (2014). The pseudo GTPase CENP-M drives human kinetochore assembly. eLife 3, e02978:1 - e02978:28.
doi: 10.7554/eLife.02978

Behrmann H, Lürick A, Kuhlee A, Balderhaar HK, Bröcker C, Kümmel D, Engelbrecht-Vandré S, Gohlke U, Raunser S, Heinemann U, Ungermann C (2014). Structural identification of the VPS18 β-propeller reveals a critical role in the HOPS complex stability and function. The Journal of Biological Chemistry 289 (48), S. 33503-33512.
doi: 10.1074/jbc.M114.602714

Kapoor S, Berghaus M, Suladze S, Prumbaum D, Grobelny S, Degen P, Raunser S, Winter R (2014). Prebiotic Cell Membranes that Survive Extreme Environmental Pressure Conditions. Angewandte Chemie International Edition 53 (32), S. 8397-8401.
doi: 10.1002/anie.201404254

Meusch D, Gatsogiannis C, Efremov R, Lang A, Hofnagel O, Vetter I, Aktories K, Raunser S (2014). Mechanism of Tc toxin action revealed in molecular detail. Nature 508(7494):61-5.
doi: 10.1038/nature13015
freely available!

Petrovic A, Mosalaganti S, Keller J, Mattiuzzo M, Overlack K, Krenn V, De Antoni A, Wohlgemuth S, Cecatiello V, Pasqualato S, Raunser S, Musacchio A (2014). Modular Assembly of RWD Domains on the Mis12 Complex Underlies Outer Kinetochore Organization. Molecular Cell 53 (4), S. 591-605.
doi: 10.1016/j.molcel.2014.01.019

Rosin C, Erlkamp M, von der Ecken J, Raunser S, Winter R (2014). Exploring the stability limits of actin and its suprastructures. Biophysical Journal 107 (12), S. 2982-2992.
doi: 10.1016/j.bpj.2014.11.006

Thakur HC, Singh M, Nagel-Steger L, Kremer J, Prumbaum D, Fansa EK, Ezzahoini H, Nouri K, Gremer L, Abts A, Schmitt L, Raunser S, Ahmadian MR, Piekorz RP (2014). The Centrosomal Adaptor TACC3 and the Microtubule Polymerase chTOG Interact via Defined C-terminal Subdomains in an Aurora-A Kinase-independent Manner. The Journal of Biological Chemistry 289 (1), S. 74-88.
doi: 10.1074/jbc.M113.532333


2013

Erkelenz M, Bauer DM, Meyer R, Gatsogiannis C, Raunser S, Saccà B, Niemeyer CM (2013). A Facile Method for Preparation of Tailored Scaffolds for DNA-Origami. Small 10 (1), S. 73-77.
doi: 10.1002/smll.201300701

Gatsogiannis C, Lang A, Meusch D, Pfaumann V, Hofnagel O, Benz R, Aktories K, Raunser S (2013). A syringe-like injection mechanism in Photorhabdus luminescens toxins. Nature. 495(7442):520-23
doi: 10.1038/nature11987
freely available!

Lakshminarasimhan M, Curth U, Moniot S, Mosalaganti S, Raunser S, Steegborn C (2013). Molecular architecture of the human protein deacetylase Sirt1 and its regulation by AROS and resveratrol. Bioscience Reports 33 (3) pii:e00037, S. 395-407.
doi: 10.1042/BSR20120121

Lehman W, Orzechowski M, Li XE, Fischer S, Raunser S (2013). Gestalt-Binding of tropomyosin on actin during thin filament activation. Journal of Muscle Research and Cell Motility 34 (3-4), S. 155-163.
doi: 10.1007/s10974-013-9342-0

Sadian Y, Gatsogiannis C, Patasi C, Hofnagel O, Goody RS, Farkasovský M, Raunser S (2013). The role of Cdc42 and Gic1 in the regulation of septin filament formation and dissociation. eLife 2, e01085:1 - e01085:26.
doi: 10.7554/eLife.01085

Schönichen A, Mannherz HG, Behrmann E, Mazur AJ, Kühn S, Silván U, Schoenenberger C-A, Fackler OT, Raunser S, Dehmelt L, Geyer M (2013). FHOD1 is a combined actin filament capping and bundling factor that selectively associates with actin arcs and stress fibers. Journal of Cell Science 126 (Pt8), S. 1891-1901.
doi: 10.1242/jcs.126706

Sot B, Behrmann E, Raunser S, Wittinghofer A (2013). Ras GTPase activating (RasGAP) activity of the dual specificity GAP protein Rasal requires colocalization and C2 domain binding to lipid membranes. PNAS 110 (1), S. 111-116.
doi: 10.1073/pnas.1201658110

Taft MH, Behrmann E, Munske-Weidemann L-C, Thiel C, Raunser S, Manstein DJ (2013). Functional Characterization of Human Myosin-18A and Its Interaction with F-actin and GOLPH3. he Journal of Biological Chemistry 288 (42), S. 30029-30041.
doi: 10.1074/jbc.M113.497180

Thakur HC, Singh M, Nagel-Steger L, Prumbaum D, Fansa EK, Gremer L, Ezzahoini H, Abts A, Schmitt L, Raunser S, Ahmadian MR, Piekorz RP (2013). Role of centrosomal adaptor proteins of the TACC family in the regulation of microtubule dynamics during mitotic cell division. Biological Chemistry 394 (11), S. 1411-1423.
doi: 10.1515/hsz-2013-0184


2012

Behrmann E, Müller M, Penczek PA, Mannherz HG, Manstein DJ, Raunser S (2012). Structure of the Rigor Actin-Tropomyosin-Myosin Complex. Cell 150 (2), S. 327-338.
doi: 10.1016/j.cell.2012.05.037

Behrmann E, Tao G, Stokes DL, Egelman EH, Raunser S, Penczek PA (2012). Real-space processing of helical filaments in SPARX. Journal of Structural Biology 177 (2), S. 302-313.
doi: 10.1016/j.jsb.2011.12.020

Bröcker C, Kuhlee A, Gatsogiannis C, kleine Balderhaar HJ, Hönscher C, Engelbrecht-Vandré S, Ungermann C, Raunser S (2012). Molecular architecture of the multisubunit homotypic fusion and vacuole protein sorting (HOPS) tethering complex. PNAS 109 (6), S. 1991-1996.
doi: 10.1073/pnas.1117797109

Hernandez JM, Stein A, Behrmann E, Riedel D, Cypionka A, Farsi Z, Walla PJ, Raunser S, Jahn R (2012). Membrane Fusion Intermediates via Directional and Full Assembly of the SNARE Complex. Science 336 (6088), S. 1581-1584.
doi: 10.1126/science.1221976

Müller M, Mazur AJ, Behrmann E, Diensthuber RP, Radke MB, Qu Z, Littwitz C, Raunser S, Schoenenberger C-A, Manstein DJ, Mannherz HG (2012). Functional characterization of the human α-cardiac actin mutations Y166C and M305L involved in hypertrophic cardiomyopathy. Cellular and Molecular Life Sciences 69 (20), S. 3457-3479.
doi: 10.1007/s00018-012-1030-5


2011

Schneider R, Schumacher MC, Mueller H, Nand D, Klaukien V, Heise H, Riedel D, Wolf G, Behrmann E, Raunser S, Seidel R, Engelhard M, Baldus M (2011). Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy. Journal of Molecular Biology 412 (1), S. 121-136.
doi: 10.1016/j.jmb.2011.06.045


before 2011

Wang L, Yang JK, Kabaleeswaran V, Rice AJ, Cruz AC, Park AY, Yin Q, Damko E, Jang SB, Raunser S, Robinson CV, Siegel RM, Walz T, Wu H (2010). The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature Structural and Molecular Biology 17 (11), S. 1324-1329.
doi: 10.1038/nsmb.1920

Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS (2009). STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1. Cell 136 (5), S. 876-890.
doi: 10.1016/j.cell.2009.02.014

Raunser S, Magnani R, Huang Z, Houtz RL, Trievel RC, Penczek PA, Walz T (2009). Rubisco in complex with Rubisco large subunit methyltransferase. PNAS 106 (9), S. 3160-3165.
doi: 10.1073/pnas.0810563106

Raunser S, Walz T (2009). Electron Crystallography as a Technique to Study the Structure on Membrane Proteins in a Lipidic Environment. Annual Review of Biophysics 38, S. 89-105.
doi: 10.1016/j.cell.2009.02.014

Raunser S, Mathai JC, Abeyrathne PD, Rice AJ, Zeidel ML, Walz T (2009). Oligomeric structure and functional characterization of the urea transporter from Actinobacillus pleuropneumoniae. Journal of Molecular Biology 387 (3), S. 619-627.
doi: 10.1016/j.jmb.2009.02.005

Bankovich AJ, Raunser S, Juo ZS, Walz T, Davis MM, Garcia KC (2007). Structural insight into pre-B cell receptor function. Science 316 (5822), S. 291-294.
doi: 10.1126/science.1139412

Hite RK, Raunser S, Walz T (2007). Revival of electron crystallography. Current Opinion in Structural Biology 17 (4), S. 389-395.
doi: 10.1016/j.sbi.2007.06.006

Park HH, Logette E, Raunser S, Cuenin S, Walz T, Tschopp J, Wu H (2007). Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex. Cell 128 (3), S. 533-546.
doi: 10.1016/j.cell.2007.01.019

Yildiz Ö, Kalthoff C, Raunser S, Kühlbrandt W (2007). Structure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptake. EMBO Journal 26 (2), S. 589-599.
doi: 10.1038/sj.emboj.7601492

Hobe S, Trostmann I, Raunser S, Paulsen H (2006). Assembly of the major light-harvesting chlorophyll-a/b complex: Thermodynamics and kinetics of neoxanthin binding. The Journal of Biological Chemistry 281 (35), S. 25156-25166.
doi: 10.1074/jbc.M604828200

Kim Y-G, Raunser S, Munger C, Wagner J, Song Y-L, Cygler M, Walz T, Oh B-H, Sacher M (2006). The architecture of the multisubunit TRAPP I complex suggests a model for vesicle tethering. Cell 127 (4), S. 817-830.
doi: 10.1016/j.cell.2006.09.029

Mougous JD, Cuff ME, Raunser S, Shen A, Zhou M, Gifford CA, Goodman AL, Joachimiak G, Ordonez CL, Lory S, Walz T, Joachimiak A, Mekalanos JJ (2006). A virulence locus of Pseudomonas aeruginosa encodes a protein secretion apparatus. Science 312 (5779), S. 1526-1530.
doi: 10.1126/science.1128393

Raunser S, Appel M, Ganea C, Geldmacher-Kaufer U, Fendler K, Kühlbrandt W (2006). Structure and function of prokaryotic glutamate transporters from Escherichia coli and Pyrococcus horikoshii. Biochemistry 45 (42), S. 12796-12805.
doi: 10.1021/bi061008

Raunser S, Haase W, Franke C, Eckert GP, Müller WE, Kühlbrandt W (2006). Heterologously Expressed GLT-1 Associates in approximately 200-nm Protein-Lipid Islands. Biophysical Journal 91 (10), S. 3718-3726.
doi: 10.1529/biophysj.106.086900

Vinothkumar KR, Raunser S, Jung H, Kühlbrandt W (2006).Oligomeric structure of the carnitine transporter CaiT from Escherichia coli. The Journal of Biological Chemistry 281(8), S. 4795-4801.
doi: 10.1074/jbc.M508993200

Raunser S, Haase W, Bostina M, Parcej DN, Kühlbrandt W (2005). High-yield expression, reconstitution and structure of the recombinant, fully functional glutamate transporter GLT-1 from Rattus norvegicus. Journal of Molecular Biology351(3), S. 598-613.
doi: 10.1016/j.jmb.2005.06.036

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