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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water
Joshua A. Riback, Micayla A. Bowman, Adam M. Zmyslowski, et al.
Science (2017) Vol. 358, Iss. 6360, pp. 238-241
Open Access | Times Cited: 229

Showing 1-25 of 229 citing articles:

Valence and patterning of aromatic residues determine the phase behavior of prion-like domains
Erik Martin, Alex S. Holehouse, Ivan Peran, et al.
Science (2020) Vol. 367, Iss. 6478, pp. 694-699
Open Access | Times Cited: 995
Sequence determinants of protein phase behavior from a coarse-grained model
Gregory L. Dignon, Wenwei Zheng, Young C. Kim, et al.
PLoS Computational Biology (2018) Vol. 14, Iss. 1, pp. e1005941-e1005941
Open Access | Times Cited: 587
Biomolecular Phase Separation: From Molecular Driving Forces to Macroscopic Properties
Gregory L. Dignon, Robert B. Best, Jeetain Mittal
Annual Review of Physical Chemistry (2020) Vol. 71, Iss. 1, pp. 53-75
Open Access | Times Cited: 552
Deciphering how naturally occurring sequence features impact the phase behaviours of disordered prion-like domains
Anne Bremer, Mina Farag, Wade M. Borcherds, et al.
Nature Chemistry (2021) Vol. 14, Iss. 2, pp. 196-207
Open Access | Times Cited: 400
Relation between single-molecule properties and phase behavior of intrinsically disordered proteins
Gregory L. Dignon, Wenwei Zheng, Robert B. Best, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 40, pp. 9929-9934
Open Access | Times Cited: 378
Accurate model of liquid–liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties
Giulio Tesei, Thea K. Schulze, Ramón Crehuet, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 44
Open Access | Times Cited: 289
Advances in targeting ‘undruggable’ transcription factors with small molecules
Matthew J. Henley, Angela N. Koehler
Nature Reviews Drug Discovery (2021) Vol. 20, Iss. 9, pp. 669-688
Closed Access | Times Cited: 267
The molecular basis for cellular function of intrinsically disordered protein regions
Alex S. Holehouse, Birthe B. Kragelund
Nature Reviews Molecular Cell Biology (2023) Vol. 25, Iss. 3, pp. 187-211
Open Access | Times Cited: 237
Conformational Ensembles of an Intrinsically Disordered Protein Consistent with NMR, SAXS, and Single-Molecule FRET
Gregory-Neal W. Gomes, Mickaël Krzeminski, Ashley Namini, et al.
Journal of the American Chemical Society (2020) Vol. 142, Iss. 37, pp. 15697-15710
Open Access | Times Cited: 166
Sequence Effects on Size, Shape, and Structural Heterogeneity in Intrinsically Disordered Proteins
Upayan Baul, Debayan Chakraborty, Mauro L. Mugnai, et al.
The Journal of Physical Chemistry B (2019) Vol. 123, Iss. 16, pp. 3462-3474
Open Access | Times Cited: 163
Condensates formed by prion-like low-complexity domains have small-world network structures and interfaces defined by expanded conformations
Mina Farag, Samuel R. Cohen, Wade M. Borcherds, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 150
Interplay of folded domains and the disordered low-complexity domain in mediating hnRNPA1 phase separation
Erik Martin, F. Emil Thomasen, Nicole M. Milkovic, et al.
Nucleic Acids Research (2021) Vol. 49, Iss. 5, pp. 2931-2945
Open Access | Times Cited: 134
A Data-Driven Hydrophobicity Scale for Predicting Liquid–Liquid Phase Separation of Proteins
Thomas Dannenhoffer-Lafage, Robert B. Best
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 16, pp. 4046-4056
Closed Access | Times Cited: 126
Improving Martini 3 for Disordered and Multidomain Proteins
F. Emil Thomasen, Francesco Pesce, Mette Ahrensback Roesgaard, et al.
Journal of Chemical Theory and Computation (2022) Vol. 18, Iss. 4, pp. 2033-2041
Open Access | Times Cited: 126
Mechanisms and pathology of protein misfolding and aggregation
Nikolaos Louros, Joost Schymkowitz, Frédéric Rousseau
Nature Reviews Molecular Cell Biology (2023) Vol. 24, Iss. 12, pp. 912-933
Closed Access | Times Cited: 116
Direct prediction of intrinsically disordered protein conformational properties from sequence
Jeffrey M. Lotthammer, Garrett M. Ginell, Daniel Griffith, et al.
Nature Methods (2024) Vol. 21, Iss. 3, pp. 465-476
Open Access | Times Cited: 105
Post-translational modifications in liquid-liquid phase separation: a comprehensive review
Jingxian Li, Mengdi Zhang, Weirui Ma, et al.
Molecular Biomedicine (2022) Vol. 3, Iss. 1
Open Access | Times Cited: 103
NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
Aldo R. Camacho‐Zarco, Vincent Schnapka, Serafima Guseva, et al.
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9331-9356
Open Access | Times Cited: 96
Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range
Giulio Tesei, Kresten Lindorff‐Larsen
Open Research Europe (2023) Vol. 2, pp. 94-94
Open Access | Times Cited: 83
Phase Separation in Biology and Disease; Current Perspectives and Open Questions
Steven Boeynaems, Shasha Chong, Jörg Gsponer, et al.
Journal of Molecular Biology (2023) Vol. 435, Iss. 5, pp. 167971-167971
Open Access | Times Cited: 53
BioXTAS RAW 2: new developments for a free open-source program for small-angle scattering data reduction and analysis
Jesse B. Hopkins
Journal of Applied Crystallography (2024) Vol. 57, Iss. 1, pp. 194-208
Open Access | Times Cited: 46
HDX–MS finds that partial unfolding with sequential domain activation controls condensation of a cellular stress marker
Ruofan Chen, Hendrik Glauninger, Darren N. Kahan, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 13
Open Access | Times Cited: 20
Rescaling protein-protein interactions improves Martini 3 for flexible proteins in solution
F. Emil Thomasen, Tórur Skaalum, Ashutosh Kumar, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 19
Effective concentrations enforced by intrinsically disordered linkers are governed by polymer physics
Charlotte S. Sørensen, Magnus Kjærgaard
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 46, pp. 23124-23131
Open Access | Times Cited: 144
Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions
Alex S. Holehouse, Rohit V. Pappu
Annual Review of Biophysics (2018) Vol. 47, Iss. 1, pp. 19-39
Open Access | Times Cited: 118
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