NMRPipe: A multidimensional spectral processing system based on UNIX pipes

The Activity and Stability of the Intrinsically Disordered Cip/Kip Protein Family AreRegulated by Non-Receptor TyrosineKinases

Huang, Y., Yoon, M.-K., Otieno, S., Lelli, M., & Kriwacki, R. W. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.11.011 · Cited by 36

Surface-Binding to Cardiolipin Nanodomains Triggers Cytochrome c Pro-apoptotic Peroxidase Activity via Localized Dynamics

Li, M., Mandal, A., Tyurin, V. A., DeLucia, M., Ahn, J., Kagan, V. E., & van der Wel, P. C. A. (2019) · Structure · doi:10.1016/j.str.2019.02.007 · Cited by 41

Solution NMR Insights into Docking Interactions Involving Inactive ERK2

Piserchio, A., Warthaka, M., Devkota, A. K., Kaoud, T. S., Lee, S., Abramczyk, O., Ren, P., Dalby, K. N., & Ghose, R. (2011) · Biochemistry · doi:10.1021/bi2000559 · Cited by 41

A distal regulatory region of a class I human histone deacetylase

Werbeck, N. D., Shukla, V. K., Kunze, M. B. A., Yalinca, H., Pritchard, R. B., Siemons, L., Mondal, S., Greenwood, S. O. R., Kirkpatrick, J., Marson, C. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17610-w · Cited by 40

Crystal Structures and RNA-binding Properties of the RNA Recognition Motifs of Heterogeneous Nuclear Ribonucleoprotein L

Zhang, W., Zeng, F., Liu, Y., Zhao, Y., Lv, H., Niu, L., Teng, M., & Li, X. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.463901 · Cited by 40

Preoperative Metabolic Signatures of Prostate Cancer Recurrence Following Radical Prostatectomy

Clendinen, C. S., Gaul, D. A., Monge, M. E., Arnold, R. S., Edison, A. S., Petros, J. A., & Fernández, F. M. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00926 · Cited by 39

Cooperative interaction between the DNA-binding domains of PU.1 and IRF4

Yee, A. A., Yin, P., Siderovski, D. P., Mak, T. W., Litchfield, D. W., & Arrowsmith, C. H. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1838 · Cited by 38

GC1118, an Anti-EGFR Antibody with a Distinct Binding Epitope and Superior Inhibitory Activity against High-Affinity EGFR Ligands

Lim, Y., Yoo, J., Kim, M.-S., Hur, M., Lee, E. H., Hur, H.-S., Lee, J.-C., Lee, S.-N., Park, T. W., Lee, K., et al. (2016) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0679 · Cited by 38

HIV-1 fusion inhibitors targeting the membrane-proximal external region of Env spikes

Xiao, T., Frey, G., Fu, Q., Lavine, C. L., Scott, D. A., Seaman, M. S., Chou, J. J., & Chen, B. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0496-y · Cited by 38

Evidence for aggregation-independent, PrP C -mediated Aβ cellular internalization

Foley, A. R., Roseman, G. P., Chan, K., Smart, A., Finn, T. S., Yang, K., Lokey, R. S., Millhauser, G. L., & Raskatov, J. A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009238117 · Cited by 38

An Autoinhibited Noncanonical Mechanism of GTP Hydrolysis by Rheb Maintains mTORC1 Homeostasis

Mazhab-Jafari, M. T., Marshall, C. B., Ishiyama, N., Ho, J., Di Palma, V., Stambolic, V., & Ikura, M. (2012) · Structure · doi:10.1016/j.str.2012.06.013 · Cited by 37

Genetically encoded live-cell sensor for tyrosinated microtubules

Kesarwani, S., Lama, P., Chandra, A., Reddy, P. P., Jijumon, A. S., Bodakuntla, S., Rao, B. M., Janke, C., Das, R., & Sirajuddin, M. (2020) · Journal of Cell Biology · doi:10.1083/jcb.201912107 · Cited by 37

Structural characterization of the PIT-1/ETS-1 interaction: PIT-1 phosphorylation regulates PIT-1/ETS-1 binding

Augustijn, K. D., Duval, D. L., Wechselberger, R., Kaptein, R., Gutierrez-Hartmann, A., & van der Vliet, P. C. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192693499 · Cited by 33

Beads-on-a-String, Characterization of Ets-1 Sumoylated within Its Flexible N-terminal Sequence

Macauley, M. S., Errington, W. J., Schärpf, M., Mackereth, C. D., Blaszczak, A. G., Graves, B. J., & McIntosh, L. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510488200 · Cited by 36

A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins

Aiyer, S., Swapna, G. V. T., Ma, L.-C., Liu, G., Hao, J., Chalmers, G., Jacobs, B. C., Montelione, G. T., & Roth, M. J. (2021) · Structure · doi:10.1016/j.str.2021.01.010 · Cited by 35

Solution NMR Structure and Histone Binding of the PHD Domain of Human MLL5

Lemak, A., Yee, A., Wu, H., Yap, D., Zeng, H., Dombrovski, L., Houliston, S., Aparicio, S., & Arrowsmith, C. H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077020 · Cited by 36

Structural Basis for Substrate Preference of SMYD3, a SET Domain-containing Protein Lysine Methyltransferase

Fu, W., Liu, N., Qiao, Q., Wang, M., Min, J., Zhu, B., Xu, R.-M., & Yang, N. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.709832 · Cited by 38

Modifications Modulate Anticodon Loop Dynamics and Codon Recognition of E. coli tRNAArg1,2

Cantara, W. A., Bilbille, Y., Kim, J., Kaiser, R., Leszczyńska, G., Malkiewicz, A., & Agris, P. F. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.054 · Cited by 36

Differential responses of the backbone and side-chain conformational dynamics in FKBP12 upon binding the transition-state analog FK506: implications for transition-state stabilization and target protein recognition

Brath, U., & Akke, M. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.047 · Cited by 36

A pleckstrin homology‐related domain in SHIP1 mediates membrane localization during Fcγ receptor‐induced phagocytosis

Ming‐Lum, A., Shojania, S., So, E., McCarrell, E., Shaw, E., Vu, D., Wang, I., McIntosh, L. P., & Mui, A. L. ‐. (2012) · The FASEB Journal · doi:10.1096/fj.11-201475 · Cited by 34

Instability of the Human Cytochrome P450 Reductase A287P Variant Is the Major Contributor to Its Antley-Bixler Syndrome-like Phenotype

McCammon, K. M., Panda, S. P., Xia, C., Kim, J.-J. P., Moutinho, D., Kranendonk, M., Auchus, R. J., Lafer, E. M., Ghosh, D., Martasek, P., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.716019 · Cited by 33

Conformational Dynamics of Asparagine at Coiled-Coil Interfaces

Thomas, F., Niitsu, A., Oregioni, A., Bartlett, G. J., & Woolfson, D. N. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00848 · Cited by 33

Cyclic peptide inhibitors of HIV-1 capsid-human lysyl-tRNA synthetase interaction

Dewan, V., Liu, T., Chen, K.-M., Qian, Z., Xiao, Y., Kleiman, L., Mahasenan, K. V., Li, C., Matsuo, H., Pei, D., et al. (2012) · ACS Chemical Biology · doi:10.1021/cb200450w · Cited by 33

Multi-timescale dynamics study of FKBP12 along the rapamycin–mTOR binding coordinate

Sapienza, P. J., Mauldin, R. V., & Lee, A. L. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.10.037 · Cited by 32

Structural Determinants for Binding of Sorting Nexin 17 (SNX17) to the Cytoplasmic Adaptor Protein Krev Interaction Trapped 1 (KRIT1)

Stiegler, A. L., Zhang, R., Liu, W., & Boggon, T. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.584011 · Cited by 32

Identification and Structural Characterization of a CBP/p300-Binding Domain from the ETS Family Transcription Factor GABPα

Kang, H.-S., Nelson, M. L., Mackereth, C. D., Schärpf, M., Graves, B. J., & McIntosh, L. P. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.054 · Cited by 25

Solution Structure and Molecular Determinants of Hemoglobin Binding of the First NEAT Domain of IsdB in Staphylococcus aureus

Fonner, B. A., Tripet, B. P., Eilers, B. J., Stanisich, J., Sullivan-Springhetti, R. K., Moore, R., Liu, M., Lei, B., & Copié, V. (2014) · Biochemistry · doi:10.1021/bi5005188 · Cited by 31

PH domain-mediated autoinhibition and oncogenic activation of Akt

Bae, H., Viennet, T., Park, E., Chu, N., Salguero, A., Eck, M. J., Arthanari, H., & Cole, P. A. (2022) · eLife · doi:10.7554/elife.80148 · Cited by 31

1H-detected characterization of carbon–carbon networks in highly flexible protonated biomolecules using MAS NMR

Bahri, S., Safeer, A., Adler, A., Smedes, H., van Ingen, H., & Baldus, M. (2023) · Journal of Biomolecular NMR · doi:10.1007/s10858-023-00415-6 · Cited by 31

Structural features of Dnase1L3 responsible for serum antigen clearance

McCord, J. J., Engavale, M., Masoumzadeh, E., Villarreal, J., Mapp, B., Latham, M. P., Keyel, P. A., & Sutton, R. B. (2022) · Communications Biology · doi:10.1038/s42003-022-03755-5 · Cited by 31

Structural basis of HIV-1 maturation inhibitor binding and activity

Sarkar, S., Zadrozny, K. K., Zadorozhnyi, R., Russell, R. W., Quinn, C. M., Kleinpeter, A., Ablan, S., Meshkin, H., Perilla, J. R., Freed, E. O., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36569-y · Cited by 28

Resistance to pyridine-based inhibitor KF116 reveals an unexpected role of integrase in HIV-1 Gag-Pol polyprotein proteolytic processing

Hoyte, A. C., Jamin, A. V., Koneru, P. C., Kobe, M. J., Larue, R. C., Fuchs, J. R., Engelman, A. N., & Kvaratskhelia, M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.816645 · Cited by 30

The Charged Linker Modulates the Conformations and Molecular Interactions of Hsp90

López, A., Elimelech, A. R., Klimm, K., & Sattler, M. (2021) · ChemBioChem · doi:10.1002/cbic.202000699 · Cited by 30

Proteolytic Activation of Human Cathepsin A

Kolli, N., & Garman, S. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.524280 · Cited by 30

Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A

Göbl, C., Morris, V. K., van Dam, L., Visscher, M., Polderman, P. E., Hartlmüller, C., de Ruiter, H., Hora, M., Liesinger, L., Birner-Gruenberger, R., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2019.101316 · Cited by 29

Structural Changes in the Carboxyl Terminus of the Gap Junction Protein Connexin40 Caused by the Interaction with c-Src and Zonula Occludens-1

Bouvier, D., Kieken, F., Kellezi, A., & Sorgen, P. L. (2008) · Cell Communication & Adhesion · doi:10.1080/15419060802014347 · Cited by 29

Dynamic design: manipulation of millisecond timescale motions on the energy landscape of cyclophilin A

(2020) · doi:10.1039/c9sc04696h · Cited by 29

Structure and Mechanism of LcpA, a Phosphotransferase That Mediates Glycosylation of a Gram-Positive Bacterial Cell Wall-Anchored Protein

Siegel, S. D., Amer, B. R., Wu, C., Sawaya, M. R., Gosschalk, J. E., Clubb, R. T., & Ton-That, H. (2019) · mBio · doi:10.1128/mbio.01580-18 · Cited by 29

Equilibrium Conformational Ensemble of the Intrinsically Disordered Peptide n16N: Linking Subdomain Structures and Function in Nacre

Brown, A. H., Rodger, P. M., Evans, J. S., & Walsh, T. R. (2014) · Biomacromolecules · doi:10.1021/bm501263s · Cited by 28

Structural and sequencing analysis of local target DNA recognition by MLV integrase

Aiyer, S., Rossi, P., Malani, N., Schneider, W. M., Chandar, A., Bushman, F. D., Montelione, G. T., & Roth, M. J. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv410 · Cited by 25

Ton motor conformational switch and peptidoglycan role in bacterial nutrient uptake

Zinke, M., Lejeune, M., Mechaly, A., Bardiaux, B., Boneca, I. G., Delepelaire, P., & Izadi-Pruneyre, N. (2024) · Nature Communications · doi:10.1038/s41467-023-44606-z · Cited by 27

Mutants of Cytochrome P450 Reductase Lacking Either Gly-141 or Gly-143 Destabilize Its FMN Semiquinone

Rwere, F., Xia, C., Im, S., Haque, M. M., Stuehr, D. J., Waskell, L., & Kim, J.-J. P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.724625 · Cited by 26

Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex

Foucher, A.-E., Touat-Todeschini, L., Juarez-Martinez, A. B., Rakitch, A., Laroussi, H., Karczewski, C., Acajjaoui, S., Soler-López, M., Cusack, S., Mackereth, C. D., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32542-3 · Cited by 26

Structure of the Lectin Mannose 6-Phosphate Receptor Homology (MRH) Domain of Glucosidase II, an Enzyme That Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum

Olson, L. J., Orsi, R., Alculumbre, S. G., Peterson, F. C., Stigliano, I. D., Parodi, A. J., D'Alessio, C., & Dahms, N. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.450239 · Cited by 24

The Structural Flexibility of PR-10 Food Allergens

Führer, S., Unterhauser, J., Zeindl, R., Eidelpes, R., Fernández-Quintero, M. L., Liedl, K. R., & Tollinger, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158252 · Cited by 24

Dynamics in the p38α MAP Kinase–SB203580 Complex Observed by Liquid‐State NMR Spectroscopy

Honndorf, V. S., Coudevylle, N., Laufer, S., Becker, S., & Griesinger, C. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200705614 · Cited by 22

Large-scale discovery, analysis and design of protein energy landscapes

Ferrari, Á. J. R., Dixit, S. M., Thibeault, J., Garcia, M., Houliston, S., Ludwig, R. W., Notin, P., Phoumyvong, C. M., Martell, C. M., Jung, M. D., et al. (2026) · Nature · doi:10.1038/s41586-026-10465-z · Cited by 22

The prolactin receptor scaffolds Janus kinase 2 via co-structure formation with phosphoinositide-4,5-bisphosphate

(2023) · doi:10.7554/elife.84645 · Cited by 22

Anticodon-like binding of the HIV-1 tRNA-like element to human lysyl-tRNA synthetase

Liu, S., Comandur, R., Jones, C. P., Tsang, P., & Musier-Forsyth, K. (2016) · RNA · doi:10.1261/rna.058081.116 · Cited by 22

Structural insights into Cn‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water

Santana, M. J., de Oliveira, A. L., Queiroz Júnior, L. H. K., Mandal, S. M., Matos, C. O., de O. Dias, R., Franco, O. L., & Lião, L. M. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.01.029 · Cited by 21

Characterization of a glycan-binding complex of minor pilins completes the analysis of Streptococcus sanguinis type 4 pili subunits

Shahin, M., Sheppard, D., Raynaud, C., Berry, J.-L., Gurung, I., Silva, L. M., Feizi, T., Liu, Y., & Pelicic, V. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2216237120 · Cited by 21

Identification of RING E3 pseudoligases in the TRIM protein family

(2025) · doi:10.1038/s41467-025-58807-1 · Cited by 20

Nuclear magnetic resonance- and gas chromatography/mass spectrometry-based metabolomic characterization of water-soluble and volatile compound profiles in cabbage vinegar

Ishihara, S., Inaoka, T., Nakamura, T., Kimura, K., Sekiyama, Y., & Tomita, S. (2018) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2018.02.003 · Cited by 19

Structural basis of Pseudomonas biofilm-forming functional amyloid FapC formation

Hansen, K. H., Golcuk, M., Byeon, C. H., Tunc, A., Plechinger, E. B., Dueholm, M. K. D., Conway, J. F., Andreasen, M., Gur, M., & Akbey, Ü. (2025) · Science Advances · doi:10.1126/sciadv.adx7829 · Cited by 18

Structural Insights into the Unique Modes of Relaxin-Binding and Tethered-Agonist Mediated Activation of RXFP1 and RXFP2

Sethi, A., Bruell, S., Ryan, T., Yan, F., Tanipour, M. H., Mok, Y.-F., Draper-Joyce, C., Khandokar, Y., Metcalfe, R. D., Griffin, M. D. W., et al. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167217 · Cited by 18

Structure-based analysis of CysZ-mediated cellular uptake of sulfate

Assur Sanghai, Z., Liu, Q., Clarke, O. B., Belcher-Dufrisne, M., Wiriyasermkul, P., Giese, M. H., Leal-Pinto, E., Kloss, B., Tabuso, S., Love, J., et al. (2018) · eLife · doi:10.7554/elife.27829 · Cited by 18

Structural insights into a StART-like domain in Lam4 and its interaction with sterol ligands

Gatta, A. T., Sauerwein, A. C., Zhuravleva, A., Levine, T. P., & Matthews, S. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.12.109 · Cited by 18

Rational design of 19F NMR labelling sites to probe protein structure and interactions

Streit, J. O., Chan, S. H. S., Daya, S., & Christodoulou, J. (2025) · Nature Communications · doi:10.1038/s41467-025-59105-6 · Cited by 17

Short RNA chaperones promote aggregation-resistant TDP-43 conformers to mitigate neurodegeneration

Copley, K. E., Mauna, J. C., Danielson, H. L., Chen, Q., Ozguney, B., Ngo, M., Xie, L., Smirnov, A., Davis, M., Mayne, L., et al. (2026) · Science · doi:10.1126/science.adv3301 · Cited by 16

Robust automated backbone triple resonance NMR assignments of proteins using Bayesian-based simulated annealing

Bishop, A. C., Torres-Montalvo, G., Kotaru, S., Mimun, K., & Wand, A. J. (2023) · Nature Communications · doi:10.1038/s41467-023-37219-z · Cited by 16

Exploration of O-GlcNAc transferase glycosylation sites reveals a target sequence compositional bias

(2023) · doi:10.1016/j.jbc.2023.104629 · Cited by 16

Solution structure of the Hop TPR2A domain and investigation of target druggability by NMR, biochemical and in silico approaches

Darby, J. F., Vidler, L. R., Simpson, P. J., Al-Lazikani, B., Matthews, S. J., Sharp, S. Y., Pearl, L. H., Hoelder, S., & Workman, P. (2020) · Scientific Reports · doi:10.1038/s41598-020-71969-w · Cited by 17

Structural basis of conformational transitions in the active site and 80′s loop in the FK506-binding protein FKBP12

Mustafi, S. M., Brecher, M., Zhang, J., Li, H., Lemaster, D. M., & Hernández, G. (2014) · Biochemical Journal · doi:10.1042/bj20131429 · Cited by 15

Structural Basis for the Regulation of the Mitogen-activated Protein (MAP) Kinase p38α by the Dual Specificity Phosphatase 16 MAP Kinase Binding Domain in Solution

Kumar, G. S., Zettl, H., Page, R., & Peti, W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.499178 · Cited by 12

Validated determination of NRG1 Ig-like domain structure by mass spectrometry coupled with computational modeling

(2022) · doi:10.1038/s42003-022-03411-y · Cited by 14

The Listeria monocytogenes persistence factor ClpL is a potent stand-alone disaggregase

Bohl, V., Hollmann, N. M., Melzer, T., Katikaridis, P., Meins, L., Simon, B., Flemming, D., Sinning, I., Hennig, J., & Mogk, A. (2024) · eLife · doi:10.7554/elife.92746 · Cited by 14

Vibrio cholerae’s ToxRS bile sensing system

Gubensäk, N., Sagmeister, T., Buhlheller, C., Geronimo, B. D., Wagner, G. E., Petrowitsch, L., Gräwert, M. A., Rotzinger, M., Berger, T. M. I., Schäfer, J., et al. (2023) · eLife · doi:10.7554/elife.88721 · Cited by 14

A suicidal and extensively disordered luciferase with a bright luminescence

Dijkema, F. M., Escarpizo‐Lorenzana, M. I., Nordentoft, M. K., Rabe, H. C., Sahin, C., Landreh, M., Branca, R. M., Sørensen, E. S., Christensen, B., Prestel, A., et al. (2024) · Protein Science · doi:10.1002/pro.5115 · Cited by 14

The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection

Vieira, M. F. M., Hernandez, G., Zhong, Q., Arbesú, M., Veloso, T., Gomes, T., Martins, M. L., Monteiro, H., Frazão, C., Frankel, G., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-05856-9 · Cited by 14

Assessment of Metabolic Changes in Mycobacterium smegmatis Wild-Type and alr Mutant Strains: Evidence of a New Pathway of d-Alanine Biosynthesis

Marshall, D. D., Halouska, S., Zinniel, D. K., Fenton, R. J., Kenealy, K., Chahal, H. K., Rathnaiah, G., Barletta, R. G., & Powers, R. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00871 · Cited by 13

A lever hypothesis for Synaptotagmin-1 action in neurotransmitter release

Jaczynska, K., Esser, V., Xu, J., Sari, L., Lin, M. M., Rosenmund, C., & Rizo, J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2417941121 · Cited by 13

Post-fibrillization nitration of alpha-synuclein abolishes its seeding activity and pathology formation in primary neurons and in vivo

Donzelli, S., OSullivan, S. A., Mahul-Mellier, A.-L., Ulusoy, A., Fusco, G., Kumar, S. T., Chiki, A., Burtscher, J., Boussouf, M. L. D., Rostami, I., et al. (2023) · doi:10.1101/2023.03.24.534149 · Cited by 13

A substrate-interacting region of Parkin directs ubiquitination of the mitochondrial GTPase Miro1

Koszela, J., Rintala-Dempsey, A., Salzano, G., Pimenta, V., Kamarainen, O., Gabrielsen, M., Parui, A. L., Shaw, G. S., & Walden, H. (2025) · Journal of Cell Biology · doi:10.1083/jcb.202408025 · Cited by 13

Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation

Hernandez, G., Martins, M. L., Fernandes, N. P., Veloso, T., Lopes, J., Gomes, T., & Cordeiro, T. N. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf502 · Cited by 12

Pseudomonas aeruginosa AlgF is a protein–protein interaction mediator required for acetylation of the alginate exopolysaccharide

Low, K. E., Gheorghita, A. A., Tammam, S. D., Whitfield, G. B., Li, Y. E., Riley, L. M., Weadge, J. T., Caldwell, S. J., Chong, P. A., Walvoort, M. T. C., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105314 · Cited by 11

An integrative characterization of proline cis and trans conformers in a disordered peptide

(2024) · doi:10.1016/j.bpj.2024.09.028 · Cited by 9

Control of Munc13-1 Activity by Autoinhibitory Interactions Involving the Variable N-terminal Region

Xu, J., Esser, V., Gołębiowska-Mendroch, K., Bolembach, A. A., & Rizo, J. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168502 · Cited by 8

Cryo-EM reveals the structure and dynamics of a 723-residue malate synthase G

Ho, M.-R., Wu, Y.-M., Lu, Y.-C., Ko, T.-P., & Wu, K.-P. (2023) · Journal of Structural Biology · doi:10.1016/j.jsb.2023.107958 · Cited by 8

Promiscuous and multivalent interactions between Eps15 and partner protein Dab2 generate a complex interaction network

Papagiannoula, A., Vedel, I. M., Motzny, K., Tengo, M., Saiti, A., & Milles, S. (2025) · Nature Communications · doi:10.1038/s41467-025-63090-1 · Cited by 8

The SH protein of mumps virus is a druggable pentameric viroporin

Devantier, K., Toft-Bertelsen, T. L., Prestel, A., Kjær, V. M. S., Sahin, C., Giulini, M., Louka, S., Spiess, K., Manandhar, A., Qvortrup, K., et al. (2025) · Science Advances · doi:10.1126/sciadv.ads3071 · Cited by 8

Synthetic ZFTA fusions pinpoint disordered protein domain acquisition as a mechanism of brain tumorigenesis

Arabzade, A., Shirnekhi, H. K., Varadharajan, S., Ippagunta, S. M., Phillips, A. H., Laboe, N., Baggett, D. W., Wahiduzzaman, Jo, M., Zheng, T., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01745-3 · Cited by 7

4D structural biology–quantitative dynamics in the eukaryotic RNA exosome complex

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