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 separation provides a mechanism to reduce noise in cells
Adam Kłosin, Florian Oltsch, Tyler S. Harmon, et al.
Science (2020) Vol. 367, Iss. 6476, pp. 464-468
Open Access | Times Cited: 304

Showing 1-25 of 304 citing articles:

mRNAs, proteins and the emerging principles of gene expression control
Christopher Buccitelli, Matthias Selbach
Nature Reviews Genetics (2020) Vol. 21, Iss. 10, pp. 630-644
Closed Access | Times Cited: 928

Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing
Simon Alberti, Anthony A. Hyman
Nature Reviews Molecular Cell Biology (2021) Vol. 22, Iss. 3, pp. 196-213
Closed Access | Times Cited: 871

A framework for understanding the functions of biomolecular condensates across scales
Andrew S. Lyon, William B. Peeples, Michael K. Rosen
Nature Reviews Molecular Cell Biology (2020) Vol. 22, Iss. 3, pp. 215-235
Open Access | Times Cited: 686

Composition-dependent thermodynamics of intracellular phase separation
Joshua A. Riback, Lian Zhu, Mylene C. Ferrolino, et al.
Nature (2020) Vol. 581, Iss. 7807, pp. 209-214
Open Access | Times Cited: 599

Evaluating phase separation in live cells: diagnosis, caveats, and functional consequences
David T. McSwiggen, Mustafa Mir, Xavier Darzacq, et al.
Genes & Development (2019) Vol. 33, Iss. 23-24, pp. 1619-1634
Open Access | Times Cited: 543

RNA contributions to the form and function of biomolecular condensates
Christine Roden, Amy S. Gladfelter
Nature Reviews Molecular Cell Biology (2020) Vol. 22, Iss. 3, pp. 183-195
Open Access | Times Cited: 527

A conceptual framework for understanding phase separation and addressing open questions and challenges
Tanja Mittag, Rohit V. Pappu
Molecular Cell (2022) Vol. 82, Iss. 12, pp. 2201-2214
Open Access | Times Cited: 500

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

The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum
G Elif Karagöz, Diego Acosta‐Alvear, Peter Walter
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 9, pp. a033886-a033886
Open Access | Times Cited: 266

Biomolecular Condensates and Cancer
Ann Boija, Isaac A. Klein, Richard A. Young
Cancer Cell (2021) Vol. 39, Iss. 2, pp. 174-192
Open Access | Times Cited: 246

Coacervates as models of membraneless organelles
N. Amy Yewdall, Alain A.M. André, Tiemei Lu, et al.
Current Opinion in Colloid & Interface Science (2020) Vol. 52, pp. 101416-101416
Open Access | Times Cited: 245

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

Modulating biomolecular condensates: a novel approach to drug discovery
Diana M. Mitrea, Matthäus Mittasch, Beatriz Ferreira Gomes, et al.
Nature Reviews Drug Discovery (2022) Vol. 21, Iss. 11, pp. 841-862
Open Access | Times Cited: 236

Intrinsically disordered protein regions and phase separation: sequence determinants of assembly or lack thereof
Erik Martin, Alex S. Holehouse
Emerging Topics in Life Sciences (2020) Vol. 4, Iss. 3, pp. 307-329
Closed Access | Times Cited: 225

Phase-separating RNA-binding proteins form heterogeneous distributions of clusters in subsaturated solutions
Mrityunjoy Kar, Furqan Dar, Timothy J. Welsh, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 28
Open Access | Times Cited: 210

Improved coarse‐grained model for studying sequence dependent phase separation of disordered proteins
Roshan Mammen Regy, J Thompson, Young C. Kim, et al.
Protein Science (2021) Vol. 30, Iss. 7, pp. 1371-1379
Open Access | Times Cited: 183

NORAD-induced Pumilio phase separation is required for genome stability
Mahmoud Elguindy, Joshua T. Mendell
Nature (2021) Vol. 595, Iss. 7866, pp. 303-308
Open Access | Times Cited: 176

Evidence for and against Liquid-Liquid Phase Separation in the Nucleus
A Peng, Stephanie C. Weber
Non-Coding RNA (2019) Vol. 5, Iss. 4, pp. 50-50
Open Access | Times Cited: 147

Programmable protein circuit design
Zibo Chen, Michael B. Elowitz
Cell (2021) Vol. 184, Iss. 9, pp. 2284-2301
Open Access | Times Cited: 106

Engineering synthetic biomolecular condensates
Yifan Dai, Lingchong You, Ashutosh Chilkoti
Nature Reviews Bioengineering (2023) Vol. 1, Iss. 7, pp. 466-480
Open Access | Times Cited: 101

DNA-based programmable gate arrays for general-purpose DNA computing
Hui Lv, Nuli Xie, Mingqiang Li, et al.
Nature (2023) Vol. 622, Iss. 7982, pp. 292-300
Closed Access | Times Cited: 90

Amyloid formation as a protein phase transition
Thomas C. T. Michaels, Daoyuan Qian, Anđela Šarić, et al.
Nature Reviews Physics (2023) Vol. 5, Iss. 7, pp. 379-397
Closed Access | Times Cited: 83

Formation, function, and pathology of RNP granules
Nina Ripin, Roy Parker
Cell (2023) Vol. 186, Iss. 22, pp. 4737-4756
Closed Access | Times Cited: 80

Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu
Manisha Poudyal, Komal Patel, Laxmikant Gadhe, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 78

Molecular and environmental determinants of biomolecular condensate formation
José A. Villegas, Meta Heidenreich, Emmanuel D. Levy
Nature Chemical Biology (2022) Vol. 18, Iss. 12, pp. 1319-1329
Closed Access | Times Cited: 77

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