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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:

A Solid-State Conceptualization of Information Transfer from Gene to Message to Protein
Masato Kato, Steven L. McKnight
Annual Review of Biochemistry (2017) Vol. 87, Iss. 1, pp. 351-390
Closed Access | Times Cited: 148

Showing 1-25 of 148 citing articles:

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: 872
RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation
Jordina Guillén‐Boixet, Andrii Kopach, Alex S. Holehouse, et al.
Cell (2020) Vol. 181, Iss. 2, pp. 346-361.e17
Open Access | Times Cited: 733
Organization and regulation of gene transcription
Patrick Cramer
Nature (2019) Vol. 573, Iss. 7772, pp. 45-54
Closed Access | Times Cited: 621
Alternative Splicing Regulatory Networks: Functions, Mechanisms, and Evolution
Jernej Ule, Benjamin J. Blencowe
Molecular Cell (2019) Vol. 76, Iss. 2, pp. 329-345
Open Access | Times Cited: 618
RNA polymerase II clustering through carboxy-terminal domain phase separation
Marc Boehning, Claire Dugast‐Darzacq, M. Ranković, et al.
Nature Structural & Molecular Biology (2018) Vol. 25, Iss. 9, pp. 833-840
Open Access | Times Cited: 567
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
A Membraneless Organelle Associated with the Endoplasmic Reticulum Enables 3′UTR-Mediated Protein-Protein Interactions
Weirui Ma, Christine Mayr
Cell (2018) Vol. 175, Iss. 6, pp. 1492-1506.e19
Open Access | Times Cited: 342
Phase separation of ligand-activated enhancers licenses cooperative chromosomal enhancer assembly
Sreejith J. Nair, Yang Lu, Dario Meluzzi, et al.
Nature Structural & Molecular Biology (2019) Vol. 26, Iss. 3, pp. 193-203
Open Access | Times Cited: 308
m6A-binding YTHDF proteins promote stress granule formation
Ye Fu, Xiaowei Zhuang
Nature Chemical Biology (2020) Vol. 16, Iss. 9, pp. 955-963
Open Access | Times Cited: 265
Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation
E.L. Guenther, Qin Cao, Hamilton Trinh, et al.
Nature Structural & Molecular Biology (2018) Vol. 25, Iss. 6, pp. 463-471
Open Access | Times Cited: 235
Cryo-EM structures of four polymorphic TDP-43 amyloid cores
Qin Cao, David R. Boyer, M.R. Sawaya, et al.
Nature Structural & Molecular Biology (2019) Vol. 26, Iss. 7, pp. 619-627
Open Access | Times Cited: 228
Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior
Titus M. Franzmann, Simon Alberti
Journal of Biological Chemistry (2018) Vol. 294, Iss. 18, pp. 7128-7136
Open Access | Times Cited: 208
Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
Xinrui Gui, Feng Luo, Yichen Li, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 197
Dynamic multifactor hubs interact transiently with sites of active transcription in Drosophila embryos
Mustafa Mir, Michael Stadler, Stephan A Ortiz, et al.
eLife (2018) Vol. 7
Open Access | Times Cited: 195
Enzymatic Noncovalent Synthesis
Hongjian He, Weiyi Tan, Jiaqi Guo, et al.
Chemical Reviews (2020) Vol. 120, Iss. 18, pp. 9994-10078
Open Access | Times Cited: 179
Causal roles of mitochondrial dynamics in longevity and healthy aging
Arpit Sharma, Hannah J. Smith, Pallas Yao, et al.
EMBO Reports (2019) Vol. 20, Iss. 12
Open Access | Times Cited: 173
On the role of phase separation in the biogenesis of membraneless compartments
Andrea Musacchio
The EMBO Journal (2022) Vol. 41, Iss. 5
Open Access | Times Cited: 158
Protein Phase Separation as a Stress Survival Strategy
Titus M. Franzmann, Simon Alberti
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 6, pp. a034058-a034058
Open Access | Times Cited: 148
FUS-dependent liquid–liquid phase separation is important for DNA repair initiation
Brunno Rocha Levone, Silvia C. Lenzken, Marco Antonaci, et al.
The Journal of Cell Biology (2021) Vol. 220, Iss. 5
Open Access | Times Cited: 147
A brief guideline for studies of phase-separated biomolecular condensates
Yifei Gao, Xi Li, Pilong Li, et al.
Nature Chemical Biology (2022) Vol. 18, Iss. 12, pp. 1307-1318
Closed Access | Times Cited: 107
Fixation can change the appearance of phase separation in living cells
Shawn Irgen-Gioro, Shawn Yoshida, Victoria Walling, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 94
“Structure”-function relationships in eukaryotic transcription factors: The role of intrinsically disordered regions in gene regulation
John J. Ferrie, Jonathan P. Karr, Robert Tjian, et al.
Molecular Cell (2022) Vol. 82, Iss. 21, pp. 3970-3984
Open Access | Times Cited: 86
Liquid-liquid Phase Separation of α-Synuclein: A New Mechanistic Insight for α-Synuclein Aggregation Associated with Parkinson's Disease Pathogenesis
Semanti Mukherjee, Arunima Sakunthala, Laxmikant Gadhe, et al.
Journal of Molecular Biology (2022) Vol. 435, Iss. 1, pp. 167713-167713
Open Access | Times Cited: 83
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: 79
mRNA stability and m6A are major determinants of subcellular mRNA localization in neurons
Inga Loedige, Artem Baranovskii, Samantha Mendonsa, et al.
Molecular Cell (2023) Vol. 83, Iss. 15, pp. 2709-2725.e10
Open Access | Times Cited: 46
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