Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

The functional importance of structure in unstructured protein regions
Norman E. Davey
Current Opinion in Structural Biology (2019) Vol. 56, pp. 155-163
Open Access | Times Cited: 89

Showing 1-25 of 89 citing articles:

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: 235
DisProt: intrinsic protein disorder annotation in 2020
András Hatos, Borbála Hajdu-Soltész, Alexander Miguel Monzón, et al.
Nucleic Acids Research (2019)
Open Access | Times Cited: 224
Co-condensation between transcription factor and coactivator p300 modulates transcriptional bursting kinetics
Liang Ma, Ze-Yue Gao, Jiegen Wu, et al.
Molecular Cell (2021) Vol. 81, Iss. 8, pp. 1682-1697.e7
Open Access | Times Cited: 120
Impact of protein conformational diversity on AlphaFold predictions
Tadeo E. Saldaño, Nahuel Escobedo, Julia Marchetti, et al.
Bioinformatics (2022) Vol. 38, Iss. 10, pp. 2742-2748
Open Access | Times Cited: 120
Intrinsically Disordered Proteins: An Overview
Rakesh Trivedi, Hampapathalu Adimurthy Nagarajaram
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 22, pp. 14050-14050
Open Access | Times Cited: 107
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: 95
In-Cell Structural Biology by NMR: The Benefits of the Atomic Scale
François‐Xavier Theillet
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9497-9570
Open Access | Times Cited: 81
Protein generation with evolutionary diffusion: sequence is all you need
Sarah Alamdari, Nitya Thakkar, Rianne van den Berg, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 64
Intrinsically disordered regions are poised to act as sensors of cellular chemistry
David Moses, Garrett M. Ginell, Alex S. Holehouse, et al.
Trends in Biochemical Sciences (2023) Vol. 48, Iss. 12, pp. 1019-1034
Open Access | Times Cited: 56
Interaction modules that impart specificity to disordered protein
Kateřina Čermáková, H. Courtney Hodges
Trends in Biochemical Sciences (2023) Vol. 48, Iss. 5, pp. 477-490
Open Access | Times Cited: 49
Structural biases in disordered proteins are prevalent in the cell
David Moses, Karina Guadalupe, Feng Yu, et al.
Nature Structural & Molecular Biology (2024)
Open Access | Times Cited: 38
Mechanisms and consequences of subcellularRNAlocalization across diverse cell types
Krysta L. Engel, Ankita Arora, Raeann Goering, et al.
Traffic (2020) Vol. 21, Iss. 6, pp. 404-418
Open Access | Times Cited: 79
Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities
Thomas Kruse, Caroline Benz, Dimitriya H. Garvanska, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 65
RosettaDDGPrediction for high‐throughput mutational scans: From stability to binding
Valentina Sora, Adrian Otamendi Laspiur, Kristine Degn, et al.
Protein Science (2022) Vol. 32, Iss. 1
Open Access | Times Cited: 44
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
T. Reid Alderson, Iva Pritišanac, Đesika Kolarić, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 41
A Unified Description of Intrinsically Disordered Protein Dynamics under Physiological Conditions Using NMR Spectroscopy
Wiktor Adamski, Nicola Salvi, Damien Maurin, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 44, pp. 17817-17829
Open Access | Times Cited: 63
Sequence- and chemical specificity define the functional landscape of intrinsically disordered regions
Iris Langstein-Skora, Andrea Schmid, Frauke Huth, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Closed Access | Times Cited: 38
In-cell NMR: Why and how?
François‐Xavier Theillet, Enrico Luchinat
Progress in Nuclear Magnetic Resonance Spectroscopy (2022) Vol. 132-133, pp. 1-112
Open Access | Times Cited: 38
Discovering molecular features of intrinsically disordered regions by using evolution for contrastive learning
Alex X. Lu, Amy X. Lu, Iva Pritišanac, et al.
PLoS Computational Biology (2022) Vol. 18, Iss. 6, pp. e1010238-e1010238
Open Access | Times Cited: 35
The molecular grammar of protein disorder guiding genome-binding locations
Felix Jonas, Miri Carmi, Beniamin Krupkin, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 10, pp. 4831-4844
Open Access | Times Cited: 22
Mining of a novel esterase (est3S) gene from a cow rumen metagenomic library with organosphosphorus insecticides degrading capability: Catalytic insights by site directed mutations, docking, and molecular dynamic simulations
Hee Yul Lee, Du Yong Cho, Iqrar Ahmad, et al.
International Journal of Biological Macromolecules (2021) Vol. 190, pp. 441-455
Closed Access | Times Cited: 36
Folded domain charge properties influence the conformational behavior of disordered tails
Ishan Taneja, Alex S. Holehouse
Current Research in Structural Biology (2021) Vol. 3, pp. 216-228
Open Access | Times Cited: 35
Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins
Jhullian J. Alston, Andrea Soranno, Alex S. Holehouse
Methods (2021) Vol. 193, pp. 116-135
Open Access | Times Cited: 33
ATP and nucleic acids competitively modulate LLPS of the SARS-CoV2 nucleocapsid protein
Mei Dang, Tongyang Li, Jianxing Song
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 16
BRCA1/BARD1 intrinsically disordered regions facilitate chromatin recruitment and ubiquitylation
Samuel R. Witus, Lisa M. Tuttle, Wenjing Li, et al.
The EMBO Journal (2023) Vol. 42, Iss. 15
Open Access | Times Cited: 16
Page 1 - Next Page

Scroll to top