Identification of cross-linked peptides from complex samples

A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis

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Chemical Cross-Linking and Mass Spectrometry As a Low-Resolution Protein Structure Determination Technique

Singh, P., Panchaud, A., & Goodlett, D. R. (2010) · Analytical Chemistry · doi:10.1021/ac1000724 · Cited by 113

Protein Analysis by Shotgun/Bottom-up Proteomics

Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491

Structure and mechanogating mechanism of the Piezo1 channel

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CasX enzymes comprise a distinct family of RNA-guided genome editors

Liu, J.-J., Orlova, N., Oakes, B. L., Ma, E., Spinner, H. B., Baney, K. L. M., Chuck, J., Tan, D., Knott, G. J., Harrington, L. B., et al. (2019) · Nature · doi:10.1038/s41586-019-0908-x · Cited by 446

Structure of activated transcription complex Pol II–DSIF–PAF–SPT6

Vos, S. M., Farnung, L., Boehning, M., Wigge, C., Linden, A., Urlaub, H., & Cramer, P. (2018) · Nature · doi:10.1038/s41586-018-0440-4 · Cited by 432

Structure and conformational dynamics of the human spliceosomal Bact complex

Haselbach, D., Komarov, I., Agafonov, D. E., Hartmuth, K., Graf, B., Dybkov, O., Urlaub, H., Kastner, B., Lührmann, R., & Stark, H. (2018) · Cell · doi:10.1016/j.cell.2018.01.010 · Cited by 218

The diverse and expanding role of mass spectrometry in structural and molecular biology

Lössl, P., van de Waterbeemd, M., & Heck, A. J. (2016) · The EMBO Journal · doi:10.15252/embj.201694818 · Cited by 222

Comprehensive structure and functional adaptations of the yeast nuclear pore complex

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Structure of complete Pol II–DSIF–PAF–SPT6 transcription complex reveals RTF1 allosteric activation

Vos, S. M., Farnung, L., Linden, A., Urlaub, H., & Cramer, P. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0437-1 · Cited by 160

Structural basis of TFIIH activation for nucleotide excision repair

Kokic, G., Chernev, A., Tegunov, D., Dienemann, C., Urlaub, H., & Cramer, P. (2019) · Nature Communications · doi:10.1038/s41467-019-10745-5 · Cited by 163

Reliable identification of protein-protein interactions by crosslinking mass spectrometry

Lenz, S., Sinn, L. R., O’Reilly, F. J., Fischer, L., Wegner, F., & Rappsilber, J. (2021) · Nature Communications · doi:10.1038/s41467-021-23666-z · Cited by 157

Cryo-EM structure of the exocyst complex

Mei, K., Li, Y., Wang, S., Shao, G., Wang, J., Ding, Y., Luo, G., Yue, P., Liu, J.-J., Wang, X., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0016-2 · Cited by 156

Mass spectrometry supported determination of protein complex structure

Walzthoeni, T., Leitner, A., Stengel, F., & Aebersold, R. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.02.008 · Cited by 146

Towards elucidating the stability, dynamics and architecture of the nucleosome remodeling and deacetylase complex by using quantitative interaction proteomics

Kloet, S. L., Baymaz, H. I., Makowski, M., Groenewold, V., Jansen, P. W. T. C., Berendsen, M., Niazi, H., Kops, G. J., & Vermeulen, M. (2015) · The FEBS Journal · doi:10.1111/febs.12972 · Cited by 107

XL-MS: protein cross-linking coupled with mass spectrometry

Holding, A. N. (2015) · Methods · doi:10.1016/j.ymeth.2015.06.010 · Cited by 107

Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

Oroz, J., Chang, B. J., Wysoczanski, P., Lee, C.-T., Pérez-Lara, Á., Chakraborty, P., Hofele, R. V., Baker, J. D., Blair, L. J., Biernat, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06880-0 · Cited by 100

Proteomics-Based Methods for Discovery, Quantification, and Validation of Protein–Protein Interactions

Miteva, Y. V., Budayeva, H. G., & Cristea, I. M. (2013) · Analytical Chemistry · doi:10.1021/ac3033257 · Cited by 105

The RNA helicase Aquarius exhibits structural adaptations mediating its recruitment to spliceosomes

De, I., Bessonov, S., Hofele, R., dos Santos, K., Will, C. L., Urlaub, H., Lührmann, R., & Pena, V. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2951 · Cited by 89

The molecular architecture of the nuclear basket

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Structural and functional characterization of the Spo11 core complex

Claeys Bouuaert, C., Tischfield, S. E., Pu, S., Mimitou, E. P., Arias-Palomo, E., Berger, J. M., & Keeney, S. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-00534-w · Cited by 87

The interaction network of the YidC insertase with the SecYEG translocon, SRP and the SRP receptor FtsY

Petriman, N.-A., Jauß, B., Hufnagel, A., Franz, L., Sachelaru, I., Drepper, F., Warscheid, B., & Koch, H.-G. (2018) · Scientific Reports · doi:10.1038/s41598-017-19019-w · Cited by 66

The evolving contribution of mass spectrometry to integrative structural biology

Faini, M., Stengel, F., & Aebersold, R. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1382-4 · Cited by 44

Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding

Scacioc, A., Schmidt, C., Hofmann, T., Urlaub, H., Kühnel, K., & Pérez-Lara, Á. (2017) · Scientific Reports · doi:10.1038/s41598-017-14337-5 · Cited by 44

Diverse modes of H3K36me3-guided nucleosomal deacetylation by Rpd3S

Guan, H., Wang, P., Zhang, P., Ruan, C., Ou, Y., Peng, B., Zheng, X., Lei, J., Li, B., Yan, C., et al. (2023) · Nature · doi:10.1038/s41586-023-06349-1 · Cited by 40

Neuronal RNA granules are ribosome complexes stalled at the pre-translocation state

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Glucocorticoid receptor complexes form cooperatively with the Hsp90 co-chaperones Pp5 and FKBPs

Kaziales, A., Barkovits, K., Marcus, K., & Richter, K. (2020) · Scientific Reports · doi:10.1038/s41598-020-67645-8 · Cited by 24

CLMSVault: A software suite for protein cross-linking mass-spectrometry data analysis and visualization

Courcelles, M., Coulombe-Huntington, J., Cossette, É., Gingras, A.-C., Thibault, P., & Tyers, M. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00205 · Cited by 21

Structure of a Rhs effector clade domain provides mechanistic insights into type VI secretion system toxin delivery

Hayes, B. K., Harper, M., Venugopal, H., Lewis, J. M., Wright, A., Lee, H.-C., Steele, J. R., Steer, D. L., Schittenhelm, R. B., Boyce, J. D., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52950-x · Cited by 15

Improved Peptide Search for Identification of SUMO and Sequence-Based Modifiers, in MaxSBM

Lennartsson, C., Kyriakidou, P., Nielsen, M. L., Olsen, J. V., Cox, J., & Hendriks, I. A. (2026) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2026.101589