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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:

Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles
Timothy J. Nott, Evangelia Petsalaki, Patrick Farber, et al.
Molecular Cell (2015) Vol. 57, Iss. 5, pp. 936-947
Open Access | Times Cited: 1728

Showing 76-100 of 1728 citing articles:

Mapping Local and Global Liquid Phase Behavior in Living Cells Using Photo-Oligomerizable Seeds
Dan Bracha, Mackenzie T. Walls, Ming‐Tzo Wei, et al.
Cell (2018) Vol. 175, Iss. 6, pp. 1467-1480.e13
Open Access | Times Cited: 418
Partitioning of cancer therapeutics in nuclear condensates
Isaac A. Klein, Ann Boija, Lena K. Afeyan, et al.
Science (2020) Vol. 368, Iss. 6497, pp. 1386-1392
Open Access | Times Cited: 417
Structural Ensembles of Intrinsically Disordered Proteins Depend Strongly on Force Field: A Comparison to Experiment
Sarah Rauscher, Vytautas Gapsys, Michał J. Gajda, et al.
Journal of Chemical Theory and Computation (2015) Vol. 11, Iss. 11, pp. 5513-5524
Open Access | Times Cited: 407
Physical principles of intracellular organization via active and passive phase transitions
Joel Berry, Clifford P. Brangwynne, Mikko Haataja
Reports on Progress in Physics (2018) Vol. 81, Iss. 4, pp. 046601-046601
Closed Access | Times Cited: 406
Transport Selectivity of Nuclear Pores, Phase Separation, and Membraneless Organelles
Hermann Broder Schmidt, Dirk Görlich
Trends in Biochemical Sciences (2015) Vol. 41, Iss. 1, pp. 46-61
Closed Access | Times Cited: 404
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
Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions
Georg Krainer, Timothy J. Welsh, Jerelle A. Joseph, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 394
RNA-binding proteins with prion-like domains in health and disease
Alice Ford Harrison, James Shorter
Biochemical Journal (2017) Vol. 474, Iss. 8, pp. 1417-1438
Open Access | Times Cited: 384
A single N‐terminal phosphomimic disrupts TDP‐43 polymerization, phase separation, and RNA splicing
Ailin Wang, Alexander E. Conicella, Hermann Broder Schmidt, et al.
The EMBO Journal (2018) Vol. 37, Iss. 5
Open Access | Times Cited: 384
Phase Separation and Neurodegenerative Diseases: A Disturbance in the Force
Aurélie Zbinden, Manuela Pérez‐Berlanga, Pierre De Rossi, et al.
Developmental Cell (2020) Vol. 55, Iss. 1, pp. 45-68
Open Access | Times Cited: 384
Relationship of Sequence and Phase Separation in Protein Low-Complexity Regions
Erik Martin, Tanja Mittag
Biochemistry (2018) Vol. 57, Iss. 17, pp. 2478-2487
Open Access | Times Cited: 382
Controllable protein phase separation and modular recruitment to form responsive membraneless organelles
Benjamin S. Schuster, Ellen H. Reed, Ranganath Parthasarathy, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 381
DEAD-box ATPases are global regulators of phase-separated organelles
Maria Hondele, Ruchika Sachdev, Stephanie Heinrich, et al.
Nature (2019) Vol. 573, Iss. 7772, pp. 144-148
Closed Access | Times Cited: 381
Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation
Veronica H. Ryan, Gregory L. Dignon, Gül H. Zerze, et al.
Molecular Cell (2018) Vol. 69, Iss. 3, pp. 465-479.e7
Open Access | Times Cited: 380
Self-interaction of NPM1 modulates multiple mechanisms of liquid–liquid phase separation
Diana M. Mitrea, Jaclyn Cika, Christopher B. Stanley, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 380
Emerging Roles for Intermolecular RNA-RNA Interactions in RNP Assemblies
Briana Van Treeck, Roy Parker
Cell (2018) Vol. 174, Iss. 4, pp. 791-802
Open Access | Times Cited: 380
Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs
Yuan Lin, Simon L. Currie, Michael K. Rosen
Journal of Biological Chemistry (2017) Vol. 292, Iss. 46, pp. 19110-19120
Open Access | Times Cited: 377
Enhancer Features that Drive Formation of Transcriptional Condensates
Krishna Shrinivas, Benjamin R. Sabari, Eliot L. Coffey, et al.
Molecular Cell (2019) Vol. 75, Iss. 3, pp. 549-561.e7
Open Access | Times Cited: 370
Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation
Thomas E. Boothby, Hugo Tapia, Alexandra H. Brozena, et al.
Molecular Cell (2017) Vol. 65, Iss. 6, pp. 975-984.e5
Open Access | Times Cited: 367
Properties of Stress Granule and P-Body Proteomes
Ji‐Young Youn, Boris J.A. Dyakov, Jianping Zhang, et al.
Molecular Cell (2019) Vol. 76, Iss. 2, pp. 286-294
Open Access | Times Cited: 364
RGG/RG Motif Regions in RNA Binding and Phase Separation
P. Andrew Chong, Robert M. Vernon, Julie D. Forman‐Kay
Journal of Molecular Biology (2018) Vol. 430, Iss. 23, pp. 4650-4665
Closed Access | Times Cited: 362
Biomolecular Condensates in the Nucleus
Benjamin R. Sabari, Alessandra Dall’Agnese, Richard A. Young
Trends in Biochemical Sciences (2020) Vol. 45, Iss. 11, pp. 961-977
Open Access | Times Cited: 362
The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease
M. Madan Babu
Biochemical Society Transactions (2016) Vol. 44, Iss. 5, pp. 1185-1200
Open Access | Times Cited: 361
Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated Compartments
Jill J. Bouchard, Joel Otero, Daniel C. Scott, et al.
Molecular Cell (2018) Vol. 72, Iss. 1, pp. 19-36.e8
Open Access | Times Cited: 358
LASSI: A lattice model for simulating phase transitions of multivalent proteins
Jeong‐Mo Choi, Furqan Dar, Rohit V. Pappu
PLoS Computational Biology (2019) Vol. 15, Iss. 10, pp. e1007028-e1007028
Open Access | Times Cited: 355

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