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A dive into the unknome,
J. Rappsilber,
Trends in Genetics
2024,
40,
15–16,
10.1016/j.tig.2023.10.011
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Structure of the native γ-tubulin ring complex capping spindle microtubules,
T. Dendooven, S. Yatskevich, A. Burt, Z. A. Chen, D. Bellini, J. Rappsilber, J. V. Kilmartin, D. Barford,
Nature structural & molecular biology
2024,
10.1038/s41594-024-01281-y
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ATP-Triggered Fe(CN) CO Synthon Transfer from the Maturase HypCD to the Active Site of Apo-[NiFe]-Hydrogenase,
A. Kwiatkowski, G. Caserta, A. C. Schulz, S. Frielingsdorf, V. Pelmenschikov, K. Weisser, A. Belsom, J. Rappsilber, I. Sergueev, C. Limberg, M. A. Mroginski, I. Zebger, O. Lenz,
Journal of the American Chemical Society
2024,
10.1021/jacs.4c09791
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Rescuing error control in crosslinking mass spectrometry,
L. Fischer, J. Rappsilber,
Molecular Systems Biology
2024,
20,
1076–1084,
10.1038/s44320-024-00057-2
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PLK1-mediated phosphorylation cascade activates Mis18 complex to ensure centromere inheritance,
P. Parashara, B. Medina-Pritchard, M. A. Abad, P. Sotelo-Parrilla, R. Thamkachy, D. Grundei, J. Zou, C. Spanos, C. N. Kumar, C. Basquin, V. Das, Z. Yan, A. A. Al-Murtadha, D. A. Kelly, T. McHugh, A. Imhof, J. Rappsilber, A. A. Jeyaprakash,
Science
2024,
385,
1098–1104,
10.1126/science.ado8270
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Dual-Bioorthogonal Catalysis by a Palladium Peptide Complex,
A. M. Pérez-López, A. Belsom, L. Fiedler, X. Xin, J. Rappsilber,
Journal of Medicinal Chemistry
2023,
66,
3301–3311,
10.1021/acs.jmedchem.2c01689
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Protein structure prediction with in-cell photo-crosslinking mass spectrometry and deep learning,
K. Stahl, A. Graziadei, T. Dau, O. Brock, J. Rappsilber,
Nature Biotechnology
2023,
10.1038/s41587-023-01704-z
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Light-Induced Orthogonal Fragmentation of Crosslinked Peptides,
L. Kolbowski, A. Belsom, A. M. Pérez-López, T. Ly, J. Rappsilber,
JACS Au
2023,
3,
2123–2130,
10.1021/jacsau.3c00199
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Establishment of dsDNA-dsDNA interactions by the condensin complex,
M. Tang, G. Pobegalov, H. Tanizawa, Z. A. Chen, J. Rappsilber, M. Molodtsov, K. i. Noma, F. Uhlmann,
Molecular Cell
2023,
83,
3787–3800000000000,
10.1016/j.molcel.2023.09.019
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Protein complexes in cells by ‐assisted structural proteomics,
F. J. O'Reilly, A. Graziadei, C. Forbrig, R. Bremenkamp, K. Charles, S. Lenz, C. Elfmann, L. Fischer, J. Stülke, J. Rappsilber,
Molecular Systems Biology
2023,
19,
10.15252/msb.202311544
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Cleavable Cross-Linkers Redefined by a Novel MS -Trigger Algorithm,
L. Kolbowski, L. Fischer, J. Rappsilber,
Analytical Chemistry
2023,
95,
15461–15464,
10.1021/acs.analchem.3c01673
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Generation of glycan-specific nanobodies,
S. K. Khilji, F. Goerdeler, K. Frensemeier, D. Warschkau, J. Lühle, Z. Fandi, F. Schirmeister, Z. A. Chen, O. Turak, A. Mallagaray, S. Boerno, B. Timmermann, J. Rappsilber, P. H. Seeberger, O. Moscovitz,
Cell Chemical Biology
2022,
29,
1353–1361,
10.1016/j.chembiol.2022.05.007
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Structural insights into Cullin4-RING ubiquitin ligase remodelling by Vpr from simian immunodeficiency viruses,
S. Banchenko, F. Krupp, C. Gotthold, J. Bürger, A. Graziadei, F. J. O’Reilly, L. Sinn, O. Ruda, J. Rappsilber, C. M. T. Spahn, T. Mielke, I. A. Taylor, D. Schwefel,
PLOS Pathogens
2021,
17,
10.1371/journal.ppat.1009775
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Reliable identification of protein-protein interactions by crosslinking mass spectrometry,
S. Lenz, L. R. Sinn, F. J. O’Reilly, L. Fischer, F. Wegner, J. Rappsilber,
Nature Communications
2021,
12,
10.1038/s41467-021-23666-z
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Retention time prediction using neural networks increases identifications in crosslinking mass spectrometry,
S. H. Giese, L. R. Sinn, F. Wegner, J. Rappsilber,
Nature Communications
2021,
12,
10.1038/s41467-021-23441-0
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Proteinanalytik mittels Crosslinking-Massenspektrometrie Synergistische Kombination von kovalenter Bindungsknüpfung und LC-MS,
L. Sinn, J. Rappsilber,
GIT Labor-Fachzeitschrift
2021,
59,
17–20,
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Shulin packages axonemal outer dynein arms for ciliary targeting,
G. R. Mali, F. A. Ali, C. K. Lau, F. Begum, J. Boulanger, J. D. Howe, Z. A. Chen, J. Rappsilber, M. Skehel, A. P. Carter,
Science
2021,
371,
910–916,
10.1126/science.abe0526
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The structure of human thyroglobulin,
F. Coscia, A. Taler-Verčič, V. T. Chang, L. Sinn, F. J. O’Reilly, T. Izoré, M. Renko, I. Berger, J. Rappsilber, D. Turk, J. Löwe,
Nature
2020,
578,
627–630,
10.1038/s41586-020-1995-4
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Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism,
B. G. Lee, F. Merkel, M. Allegretti, M. Hassler, C. Cawood, L. Lecomte, F. J. O’Reilly, L. R. Sinn, P. Gutierrez-Escribano, M. Kschonsak, S. Bravo, T. Nakane, J. Rappsilber, L. Aragon, M. Beck, J. Löwe, C. H. Haering,
Nature structural & molecular biology
2020,
27,
743–751,
10.1038/s41594-020-0457-x
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In-cell architecture of an actively transcribing-translating expressome,
F. J. O’Reilly, L. Xue, A. Graziadei, L. Sinn, S. Lenz, D. Tegunov, C. Blötz, N. Singh, W. J. H. Hagen, P. Cramer, J. Stülke, J. Mahamid, J. Rappsilber,
Science
2020,
369,
554–557,
10.1126/science.abb3758
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Multiomics Analysis Provides Insight into the Laboratory Evolution of toward the Metabolic Usage of Fluorinated Indoles,
F. Agostini, L. Sinn, D. Petras, C. J. Schipp, V. Kubyshkin, A. A. Berger, P. C. Dorrestein, J. Rappsilber, N. Budisa, B. Koksch,
ACS Central Science
2020,
7,
81–92,
10.1021/acscentsci.0c00679
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In Situ Structural Restraints from Cross-Linking Mass Spectrometry in Human Mitochondria,
P. S. J. Ryl, M. Bohlke-Schneider, S. Lenz, L. Fischer, L. Budzinski, M. Stuiver, M. M. L. Mendes, L. Sinn, F. J. O’Reilly, J. Rappsilber,
Journal of Proteome Research
2019,
19,
327–336,
10.1021/acs.jproteome.9b00541
