Publications
2024 |
|
| 76. |
Lawson CL, Kryshtafovych A, Pintilie GD, Burley SK, Černý J, Chen VB, Emsley P, Gobbi A, Joachimiak A, Noreng S, Prisant MG, Read RJ, Richardson JS, Rohou AL, Schneider B, Sellers BD, Shao C, Sourial E, Williams CI, Williams CJ, Yang Y, Abbaraju V, Afonine PV, Baker ML, Bond PS, Blundell TL, Burnley T, Campbell A, Cao R, Cheng J, Chojnowski G, Cowtan KD, DiMaio F, Esmaeeli R, Giri N, Grubmüller H, Hoh SW, Hou J, Hryc CF, Hunte C, Igaev M, Joseph AP, Kao WC, Kihara D, Kumar D, Lang L, Lin S, Maddhuri Venkata Subramaniya SR, Mittal S, Mondal A, Moriarty NW, Muenks A, Murshudov GN, Nicholls RA, Olek M, Palmer CM, Perez A, Pohjolainen E, Pothula KR, Rowley CN, Sarkar D, Schäfer LU, Schlicksup CJ, Schröder GF, Shekhar M, Si D, Singharoy A, Sobolev OV, Terashi G, Vaiana AC, Vedithi SC, Verburgt J, Wang X, Warshamanage R, Winn MD, Weyand S, Yamashita K, Zhao M, Schmid MF, Berman HM, Chiu W.
Outcomes of the EMDataResource cryo-EM Ligand Modeling Challenge. Nat Methods 2024 21(7):1340-1348 (2024) doi: 10.1038/s41592-024-02321-7. |
| 75. |
Goedert M, Griesinger C, Outeiro TF, Riek R, Schröder GF, Spillantini MG.
Abandon the NAC in α-synuclein. Lancet Neurol. 23(7):669 (2024) doi: 10.1016/S1474-4422(24)00176-5. |
| 74. |
Pesch V, Flores-Fernandez JM, Reithofer S, Ma L, Özdüzenciler P, Busch Y, Sriraman A, Wang Y, Amidian S, Kroepel CVM, Müller L, Lien Y, Rudtke O, Frieg B, Schröder GF, Wille H, Tamgüney G.
Vaccination with structurally adapted fungal protein fibrils induces immunity to Parkinson's disease. Brain 147(5):1644-1652 (2024) doi: 10.1093/brain/awae061. |
| 73. |
Benedikt Frieg*, Mookyoung Han*, Karin Giller, Christian Dienemann, Dietmar Riedel, Stefan Becker, Loren B. Andreas, Christian Griesinger, and Gunnar F. Schröder
Cryo-EM structures of lipidic fibrils of amyloid-β (1-40)
Nat Commun 15(1):1297 (2024) [PDF] |
| 72. |
Lawson CL, Kryshtafovych A, Pintilie GD, Burley SK, Černý J, Chen VB, Emsley P, Gobbi A, Joachimiak A, Noreng S, Prisant M, Read RJ, Richardson JS, Rohou AL, Schneider B, Sellers BD, Shao C, Sourial E, Williams CI, Williams CJ, Yang Y, Abbaraju V, Afonine PV, Baker ML, Bond PS, Blundell TL, Burnley T, Campbell A, Cao R, Cheng J, Chojnowski G, Cowtan KD, DiMaio F, Esmaeeli R, Giri N, Grubmüller H, Hoh SW, Hou J, Hryc CF, Hunte C, Igaev M, Joseph AP, Kao WC, Kihara D, Kumar D, Lang L, Lin S, Maddhuri Venkata Subramaniya SR, Mittal S, Mondal A, Moriarty NW, Muenks A, Murshudov GN, Nicholls RA, Olek M, Palmer CM, Perez A, Pohjolainen E, Pothula KR, Rowley CN, Sarkar D, Schäfer LU, Schlicksup CJ, Schröder GF, Shekhar M, Si D, Singharoy A, Sobolev OV, Terashi G, Vaiana AC, Vedithi SC, Verburgt J, Wang X, Warshamanage R, Winn MD, Weyand S, Yamashita K, Zhao M, Schmid MF, Berman HM, Chiu W.
Outcomes of the EMDataResource Cryo-EM Ligand Modeling Challenge. Nat Methods 21(7):1340-1348 (2024) doi: 10.1038/s41592-024-02321-7. |
2023 |
|
| 71. |
Mara Zielinski*, Fernanda S. Peralta Reyes*, Lothar Gremer, Sarah Schemmert, Benedikt Frieg, Luisa U. Schäfer, Antje Willuweit, Lili Donner, Margitta Elvers, Lars N. G. Nilsson, Stina Syvänen, Dag Sehlin, Martin Ingelsson, Dieter Willbold, Gunnar F. Schröder.
Cryo-EM of Aβ fibrils from mouse models find tg-APPArcSwe fibrils resemble those found in patients with sporadic Alzheimer’s disease
Nat Neurosci 26:2073–2080 (2023) [PDF] |
2022 |
|
| 70. |
Benedikt Frieg, Leif Antonschmidt, Christian Dienemann, James A. Geraets, Eszter E. Najbauer, Dirk Matthes, Bert L. de Groot, Loren B. Andreas, Stefan Becker, Christian Griesinger, and Gunnar F. Schröder.
The 3D structure of lipidic fibrils of α-synuclein.
Nat Commun 13: 6810 (2022) [PDF] |
| 69. |
Benedikt Frieg, James A. Geraets, Timo Strohäker, Christian Dienemann,
Panagiota Mavroeidi, Byung Chul Jung, Woojin S. Kim, Seung-Jae Lee, Maria Xilouri,
Markus Zweckstetter, and Gunnar F. Schröder.
Quaternary structure of patient-homogenate amplified
α-synuclein fibrils modulates seeding of
endogenous α-synuclein.
Commun Biol 5: 1040 (2022) |
| 68. |
L. Antonschmidt, D. Matthes, R. Dervişoğlu, B. Frieg, C. Dienemann, A.
Leonov, E. Nimerovsky, V. Sant, S. Ryazanov, A. Giese, G. F. Schröder, S. Becker, B. L.
de Groot, C. Griesinger, L. B. Andreas.
The clinical drug candidate anle138b binds in a cavity of lipidic α-synuclein fibrils.
Nat Commun 13: 5385 (2022) |
| 67. |
Alain Ibáñez de Opakua, James A. Geraets, Benedikt Frieg, Christian Dienemann, Adriana Savastano, Marija Rankovic, Maria-Sol Cima-Omori, Gunnar F. Schröder, and M. Zweckstetter.
Molecular interactions of FG nucleoporin repeats at high resolution.
Nat Chem 14:1278–1285 (2022) |
| 66. |
Zinke M, Schröder GF, Lange A.
Major tail proteins of bacteriophages of the order Caudovirales.
J Biol Chem (2022) 298(1):101472 |
2021 |
|
| 65. |
Conformational heterogeneity coupled with β-fibril formation of a scaffold protein involved in chronic mental illnesses.
Cukkemane A, Becker N, Zielinski M, Frieg B, Lakomek NA, Heise H, Schröder GF, Willbold D, Weiergräber OH.
Transl Psychiatry(2021) 11(1):639 |
| 64. |
M.P. Schützmann, F. Hasecke, S. Bachmann, M. Zielinski, S. Hänsch, G.F. Schröder, H. Zempel, W. Hoyer. Endo-lysosomal Aβ concentration and pH enable formation of Aβ oligomers that potently induce Tau missorting. Nat Commun (2021) 12, 4634 or on bioRxiv: https://doi.org/10.1101/2020.06.28.175885 |
| 63. |
M. Zielinski, C. Röder, G.F. Schröder.
Challenges in sample preparation and structure determination of amyloids by cryo-EM. JBC Reviews (2021) 297, ISSUE 2, 100938 https://doi.org/10.1016/j.jbc.2021.100938 |
| 62. |
D. Willbold, B. Strodel, G.F. Schröder, W. Hoyer, and H. Heise.
Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids. Chem. Rev. (2021) 121, 13, 8285–8307 |
| 61. |
M Pagnon de la Vega, V. Giedraitis, W. Michno, L. Kilander,
G. Güner, M. Zielinski, M. Löwenmark, R. Brundin, T. Danfors, L. Söderberg, I. Alafuzoff, L.N.G. Nilsson, A. Erlandsson, D. Willbold, S.A. Müller, G.F. Schröder, J. Hanrieder, S.F. Lichtenthaler, L. Lannfelt, D. Sehlin, M. Ingelsson.
The Uppsala APP deletion causes early onset autosomal dominant Alzheimer’s disease by altering APP processing and increasing amyloid-β fibril formation.
Sci. Transl. Med. 13, eabc6184 (2021) |
| 60. |
Pothula KR, Geraets JA, Ferber II, Schröder GF.
Clustering polymorphs of tau and IAPP fibrils with the CHEP algorithm.
Prog Biophys Mol Biol. (2021) 160:16-25. |
| 59. |
Lawson CL, Kryshtafovych A, Adams PD, Afonine PV, Baker ML, Barad BA, Bond P, Burnley T, Cao R, Cheng J, Chojnowski G, Cowtan K, Dill KA, DiMaio F, Farrell DP, Fraser JS, Herzik MA Jr, Hoh SW, Hou J, Hung LW, Igaev M, Joseph AP, Kihara D, Kumar D, Mittal S, Monastyrskyy B, Olek M, Palmer CM, Patwardhan A, Perez A, Pfab J, Pintilie GD, Richardson JS, Rosenthal PB, Sarkar D, Schäfer LU, Schmid MF, Schröder GF, Shekhar M, Si D, Singharoy A, Terashi G, Terwilliger TC, Vaiana A, Wang L, Wang Z, Wankowicz SA, Williams CJ, Winn M, Wu T, Yu X, Zhang K, Berman HM, Chiu W.
Cryo-EM model validation recommendations based on outcomes of the 2019 EMDataResource challenge.
Nat Methods (2021) 18(2):156-164. |
2020 |
|
| 58. |
Cristina Risi, Luisa U. Schäfer, Betty Belknap, Ian Pepper, Howard D. White, Gunnar F. Schröder, and Vitold E. Galkin
High-resolution cryo-EM structure of the cardiac actomyosin complex.
Structure (2020), accepted |
| 57. |
Maximilian Zinke, Katrin A. A. Sachowsky, Carl Öster, Sophie Zinn-Justin, Raimond B.G. Ravelli, Gunnar F. Schröder, Michael Habeck, Adam Lange.
Spinal Column Architecture of the Flexible SPP1 Bacteriophage Tail Tube
Nat Commun 11,5759 (2020) https://doi.org/10.1038/s41467-020-19611-1 See Press Release (english) and Pressemitteilung (deutsch) |
| 56. |
D. Della Corte, H. van Beek, F. Syberg, M. Schallmey, F. Tobola, K. Cormann, C. Schlicker, P. Baumann, K. Krumbach, S. Sokolowsky, C. Morris, A. Grünberger, E. Hofmann, G.F. Schröder, J. Marienhagen.
Engineering and application of a biosensor with focused ligand specificity"
Nat Commun (2020) 11,4851. https://www.nature.com/articles/s41467-020-18400-0 See Press Release (english) Pressemitteilung (deutsch) |
| 55. |
O. Fisette, G.F. Schröder, L.V. Schäfer.
Atomistic structure and dynamics of the human MHC-I peptide-loading complex
PNAS (2020), 117 (34) 20597-20606 https://doi.org/10.1073/pnas.2004445117 See Press Release |
| 54. |
C. Röder, T. Kupreichyk, L. Gremer, L.U. Schäfer, K.R. Pothula, R.B.G. Ravelli, D. Willbold, W. Hoyer and G.F. Schröder.
Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with Aβ fibrils
Nat Struct Mol Biol (2020) 27:660–667 See Press Release (english) und Pressemitteilung (deutsch) |
| 53. |
James A. Geraets, Karunakar R. Pothula and Gunnar F. Schröder
Integrating cryo-EM and NMR data
Curr Opin Struct Biol (2020) 61:173–181 |
2019 |
|
| 52. |
C. Röder, N. Vettore, L. N. Mangels, L. Gremer, R.B.G. Ravelli, D. Willbold, W. Hoyer, A.K. Buell, G.F. Schröder
Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy
Nat. Commun. 10, Article number: 3754 (2019) Download data here: Density Map (EMD-4727) and PDB Model (PDB ID 6R4R). |
| 51. |
Marcel Falke, Julian Victor, Michael M. Wördehoff, Alessia Peduzzo, Tao Zhang, Gunnar F. Schröder, Alexander K. Buell, Wolfgang Hoyer, and Manuel Etzkorn.
α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation
Chem Phys Lipids (2019) 220:57–65 |
2018 |
|
| 50. |
K. R. Pothula,
D. Smyrnova,
G. F. Schröder.
Clustering cryo-EM images of helical protein polymers for helical reconstructions
Ultramicroscopy (2018) 203:132-138 |
| 49. |
C. Möckel, J. Kubiak, O. Schillinger, R. Kühnemuth, D. Della Corte,
G. F. Schröder, D. Willbold, B. Strodel, C. A. M. Seidel,
P. Neudecker.
Integrated NMR, Fluorescence, and Molecular Dynamics Benchmark
Study of Protein Mechanics and Hydrodynamics
J. Phys. Chem. B (2018) 123(7):1453-1480 |
| 48. |
C. Risi, B. Belknap,
E. Forgacs-Lonart,
S. P. Harris,
G. F. Schröder, H. D. White, V. E. Galkin
N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament
Structure (2018) 26:1-8 |
2017 |
|
| 47. |
L. Gremer, D. Schölzel, C. Schenk, E. Reinartz,
Jörg Labahn, R.B.G. Ravelli, M. Tusche, C. Lopez- Iglesias, W. Hoyer, H. Heise, D. Willbold, G.F. Schröder.
Fibril structure of amyloid-ß(1-42) by cryo-electron
microscopy
Science 358:116–119 (2017) See Science Perspectives article by Popich and Raunser |
| 46. |
A. Toulmin, L.E. Baltierra-Jasso, M.J. Morten, T. Sabir, P. McGlynn, G.F. Schröder, B.O. Smith, S.W. Magennis.
Conformational heterogeneity in a fully-complementary DNA three-way junction with a GC-rich branchpoint
Biochemistry (2017) 56(37):4985-4991 |
| 45. |
C. Risi, J. Eisner, B. Belknap, D. H. Heeley, H. D. White, G. F. Schröder, V. E. Galkin.
Ca2+-induced Movement of Tropomyosin on Native Cardiac Thin Filaments Revealed by Cryo Electron Microscopy
PNAS (2017) 114:6782-6787 |
2016 |
|
| 44. |
N. Fischer, P. Neumann, L. V. Bock, C. Maracci, Z. Wang, A. Paleskava, A. L. Konevega, G. F. Schröder, H. Grubmüller, R. Ficner, M. V. Rodnina, and H. Stark.
The pathway to GTPase activation of elongation factor SelB on the ribosome
Nature (2016) 540:80-85 |
| 43. |
E.A. Mirecka, S. Feuerstein, L. Gremer, G. F. Schröder, M. Stoldt, D. Willbold, and W. Hoyer.
β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor
Sci. Rep. (2016) 6, 33474 |
| 42. |
T. Braun, M. Vos, N. Kalisman, N. E. Sherman, R. Rachel, R. Wirth, G.F. Schröder, and E. Egelman.
Archaeal Flagellin Combines a Bacterial Type IV Pilin Domain with an Immunoglobulin-like Domain
PNAS (2016) 113(37):10352-7 |
2015 |
|
| 41. |
A. Wildberg, D. Della Corte, and G.F. Schröder.
Coupling an ensemble of homologs improves refinement of protein homology models
J. Chem. Theo. Comput. (2015), 11(12):5578-5582 |
| 40. |
D. Della Corte, A. Wildberg, and G.F. Schröder.
Protein Structure Refinement with Adaptively Restrained Homologous Replicas
Proteins (2015), doi:10.1002/prot.24939 |
| 39. |
M. Spiegel, A.K. Duraisamy, and G.F. Schröder.
Improving the Visualisation of Cryo-EM Density Reconstructions
J.Struct.Biol. (2015), 191(2):207-213 |
| 38. |
T. Braun,
A. Orlova,
K. Valegård,
A.-C. Lindås,
G.F. Schröder, and
E. H. Egelman.
An Archaeal Actin from a Hyperthermophile Forms a Single-Stranded Filament
PNAS (2015), 112(30): 9340-9345. |
| 37. |
A. Sali,
H. M. Berman,
T. Schwede,
J. Trewhella,
G. Kleywegt,
S. K. Burley,
J. Markley,
H. Nakamura,
P. Adams,
A.M.J.J. Bonvin,
W. Chiu,
M. Dal Peraro,
F. DiMaio,
T. E. Ferrin,
Kay Grünewald,
A. Gutmanas,
R. Henderson,
G. Hummer,
K. Iwasaki,
G. Johnson,
C. L. Lawson,
J. Meiler,
M. A. Marti-Renom,
G. T. Montelione,
M. Nilges,
R. Nussinov,
A. Patwardhan,
J. Rappsilber,
R. J. Read,
H. Saibil,
G.F. Schröder,
C. Schwieters,
C. A. M. Seidel,
D. Svergun,
M. Topf,
E. L. Ulrich,
S. Velankar, and J. D. Westbrook.
Outcome of the First wwPDB Hybrid / Integrative Methods
Task Force Workshop
Structure (2015) 23(7): 1156-1167. |
| 36. |
G.F. Schröder.
Hybrid Methods for Macromolecular Structure Determination: Experiment with Expectations
Curr. Opin. Struct. Biol. (2015) 31: 20-27. Click here to download |
| 35. |
V.E. Galkin, A. Orlova, M.R. Vos, G.F. Schröder, and E.H. Egelman.
Near-Atomic Resolution for One State of F-Actin
Structure (2015) 23(1): 173-182 |
2014 |
|
| 34. |
G.F. Schröder, M.L. Levitt, and A.T. Brunger
Deformable elastic network refinement for low-resolution macromolecular crystallography
Acta Cryst. D (2014) D70: 2241–2255 |
| 33. |
A. Lu, V.G. Magupalli, J. Ruan, Q. Yin, M.K. Atianand, M. Vos, G.F. Schröder, K.A. Fitzgerald, H. Wu, and E.H. Egelman
Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes
Cell (2014) 156(6): 1193–1206 |
| 32. |
J. Kowal, M. Chami, P. Baumgartner, M. Arheit, P.-L. Chiu, M. Rangl, S. Scheuring, G.F. Schröder, C.M. Nimigean, H. Stahlberg.
Ligand-induced structural changes in the cyclic nucleotide-modulated potassium
channel MloK1
Nature Communications (2014) 5, 3106. |
2013 |
|
| 31. |
L.V. Bock, C. Blau, G.F. Schröder, I.I. Davydov, N. Fischer, H. Stark, M.V. Rodnina, A.C. Vaiana, and H. Grubmüller.
Energy barriers and driving forces in tRNA translocation through the ribosome
Nat Struct Mol Biol (2013) 20:1390–1396 |
| 30. |
B. Falkner and G.F. Schröder.
Cross-validation in cryo-electron microscopy based structural modeling
PNAS (2013) 110(22):8930-8935. [PDF] |
| 29. |
D.-H. Chen, D. Madan, J. Weaver, Z. Lin, G.F. Schröder, W. Chiu, H.S. Rye.
Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein
Cell (2013) 153:1354–1365. [PDF] |
| 28. |
N. Kalisman, G.F. Schröder, M. Levitt.
The Crystal Structures of the Eukaryotic Chaperonin CCT Reveal its Functional Partitioning
Structure (2013) 21:540–549. [PDF] |
| 27. |
X. Deng, J. Morris, C. Chaton, G.F. Schröder, W.S. Davidson and T.B. Thompson.
Small-angle X-ray Scattering of Apolipoprotein A-IV Reveals
the Importance of Its Termini for Structural Stability
J. Biol. Chem. (2013) 288(7):4854-4866. [PDF] |
2012 |
|
| 26. |
X. Yu, C. Goforth, C. Meyer, R. Rachel, R. Wirth, G.F. Schröder, and E.H. Egelman.
Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-terminal Type IV Pilin Helices.
J. Mol. Biol. (2012) 422(2): 274-281. [PDF] |
| 25. |
A.T. Brunger, P.D. Adams, P. Fromme, R. Fromme, M. Levitt, and G.F. Schröder.
Improving the accuracy of macromolecular structure refinement at 7 Å resolution.
Structure (2012), 20(6):957-966. [PDF] |
| 24. |
T. Sabir, A. Toulmin, L. Ma, A.C. Jones, P. McGlynn, G.F. Schröder, and S.W. Magennis.
Branchpoint expansion in a fully-complementary three-way DNA junction.
J. Am. Chem. Soc. (2012), 134(14):6280–6285. [PDF] ( See Cover) |
| 23. |
Z. Wang, G.F. Schröder.
Real-space Refinement with DireX: From Global Fitting to Side-chain Improvements.
Biopolymers (2012), 97(9):687-697. [PDF] |
| 22. |
R. Henderson, A. Sali, M.L. Baker, B. Carragher, B. Devkota, K.H. Downing, E.H. Egelman, Z. Feng, J. Frank, N. Grigorieff, W. Jiang, S.J. Ludtke, O. Medalia, P.A. Penczek, P.B. Rosenthal, M.G. Rossmann, M.F. Schmid, G.F. Schröder, A.C. Steven, D.L. Stokes, J.D. Westbrook, W. Wriggers, H. Yang, J. Young, H.M. Berman, W. Chiu, G.J. Kleywegt, C.L. Lawson.
Outcome of the First Electron Microscopy Validation Task Force Meeting.
Structure (2012) 20:205-214. [PDF] |
| 21. |
D.J. O'Donovan, I. Stokes-Rees, Y. Nam, S. Blacklow, G.F. Schröder, A.T. Brunger, Piotr Sliz.
A grid-enabled web service for low-resolution crystal structure refinement.
Acta Cryst. (2012) D68:268-276. [PDF] |
| 20. |
A.T. Brunger, D. Das, A.M. Deacon, J. Grant, T.C. Terwilliger, R.J. Read, P.D. Adams, M. Levitt and G.F. Schröder.
Application of DEN-Refinement And Automated Model-Building To A Difficult Case Of Molecular Replacement Phasing: The Structure Of A Putative Succinyl-Diaminopimelate Desuccinylase From Corynebacterium Glutamicum.
Acta Cryst. (2012). D68, 391-403 [PDF] |
2011 |
|
| 19. | V.E. Galkin, A. Orlova, D. Kudryashov, A. Solodukhin, E. Reisler, G.F. Schröder, and E.H. Egelman.
Remodeling of Actin Filaments by ADF/Cofilin Proteins.
PNAS (2011) 108(51):20568-20572 . [PDF] |
| 18. | S. Gao, A. von der Malsburg, A. Dick, K. Faelber, G.F. Schröder, O. Haller, G. Kochs, O. Daumke.
Three domain architecture of dynamin-like MxA GTPase.
Immunity (2011) 35:514-525. [PDF] |
| 17. | Y. Cong, G.F. Schröder, A.S. Meyer, J. Jakana, B. Ma, M.T. Dougherty, M.F. Schmid, S. Reissmann, M. Levitt, S.L. Ludtke, J. Frydman, and W. Chiu.
Symmetry-Free Cryo-EM Structures of the Chaperonin TRiC Along its ATPase-Driven Conformational Cycle.
EMBO J (2011) 31:720-730. [PDF] |
| 16. | E. Jaenicke, K. Büchler, H. Decker, J. Markl, T. Barends, and G.F. Schröder.
The Refined Structure of Functional Unit h of Keyhole Limpet
Hemocyanin (KLH1-h) Reveals Disulfide Bridges.
IUBMB Life (2011) 63(3):183-187. [PDF] |
| 15. | L. Zerrad, A. Merli, G.F. Schröder, A. Varga, E. Gráczer, P. Pernot, A. Round, M. Vas, and M.W. Bowler.
A Spring Loaded Release Mechanism Regulates Domain Movement and Catalysis in
Phosphoglycerate Kinase.
JBC (2011) 286:14040-14048. [PDF] |
| 14. | T. Sabir, G.F. Schröder, A. Toulmin, P. McGlynn, and S.W. Magennis.
Global Structure of Forked DNA in Solution Revealed
by High-Resolution Single-Molecule Fluorescence Resonance Energy Transfer.
J. Am. Chem. Soc. (2011) 133(5):1188-1191. [PDF] |
2010 |
|
| 13. | V.E. Galkin, A. Orlova, G.F. Schröder, E.H. Egelman.
Structural Polymorphism in F-actin.
Nat Struct Mol Biol (2010) 17:1318-1323. [PDF] |
| 12. | G.F. Schröder, M. Levitt, A.T. Brunger.
Super-resolution biomolecular crystallography with low-resolution data.
Nature (2010) 464:1218-1222. [PDF] See also "Preview" by Randy J. Read "From Poor Resolution to Rich Insight" Structure (2010) 18:664-665. |
| 11. | J. Zhang, M.L. Baker, G.F. Schröder, N.R. Douglas,
S. Reissmann, J. Jakana, M. Dougherty, C.J. Fu, M. Levitt, S.J. Ludtke,
J. Frydman, and W. Chiu.
Mechanism of folding chamber closure in a group II chaperonin. Nature (2010) 463:379-383. [PDF] |
2001 - 2009 |
|
| 10. | A. K. Wozniak, G.F. Schröder, H. Grubmüller, C.A.M. Seidel, F. Oesterhelt.
Single molecule FRET measures bends and kinks in DNA. PNAS (2008) 105(47):18337-18342. [PDF] |
| 9. |
O.F. Lange, N.-A. Lakomek, C. Fares, G.F. Schröder, S. Becker, J. Meiler, H. Grubmüller,
C. Griesinger, B.L. de Groot. Atomistic residual dipolar coupling
ensemble of ubiquitin reveals molecular recognition dynamics up to the
microsecond timescale. Science (2008) 320:1471-1475. [PDF] |
| 8. |
G.F. Schröder, A.T. Brunger, and M. Levitt. Combining Efficient Conformational Sampling
with a Deformable Elastic Network Model Facilitates Structure Refinement at Low Resolution. Structure (2007) 15:1630-1641. [PDF] |
| 7. |
G. F. Schröder, U. Alexiev, and H. Grubmüller.
Simulation of fluorescence anisotropy experiments
Probing protein flexibility. Biophys. J. (2005) 89:3757-3770. [PDF] |
| 6. |
A. Wozniak, S. Nottrott, E. Kühn-Hölsken, G. F. Schröder, H. Grubmüller, R. Lührmann,
A. M. Seidel and F. Oesterhelt. Detecting protein-induced folding of the U4 snRNA kinkturn
by single-molecule multiparameter FRET measurements. RNA (2005) 11:1545-1554. [PDF] |
| 5. | G.F. Schröder; Simulation of Fluorescence Spectroscopy Experiments , PhD Thesis, Universität Göttingen, 2004. [PDF] |
| 4. |
M. Margittai, J. Widengren, E. Schweinberger, G.F. Schröder, S. Felekyan, E. Haustein, M.
König, D. Fasshauer, H. Grubmüller, R. Jahn, and C. A. M. Seidel. Single-molecule fluorescence
resonance energy transfer reveals a dynamic equilibrium between closed and
open conformations of Syntaxin 1. PNAS (2003) 100(26):15516-15521. [PDF] |
| 3. |
G.F. Schröder and H. Grubmüller. Maximum likelihood trajectories from single molecule
fluorescence resonance energy transfer experiments. J. Chem. Phys. (2003) 119(18):9920-9924. [PDF] |
| 2. |
G.F. Schröder and H. Grubmüller. FRETsg : Biomolecular structure model building from
multiple FRET experiments. Comp. Phys. Comm. (2003) 158:150-157. [PDF] |
| 1. | G.F. Schröder Molekulardynamiksimulation der Flexibilität und Fluoreszenzanisotropie eines an ein Protein gebundenen Farbstoffs, Diploma Thesis, Universität Göttingen, 2001. [PDF] |
