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:

Biophysical and Mechanistic Models for Disease-Causing Protein Variants
Amelie Stein, Douglas M. Fowler, Rasmus Hartmann‐Petersen, et al.
Trends in Biochemical Sciences (2019) Vol. 44, Iss. 7, pp. 575-588
Open Access | Times Cited: 165

Showing 1-25 of 165 citing articles:

Predicting multiple conformations via sequence clustering and AlphaFold2
Hannah K. Wayment-Steele, Adedolapo Ojoawo, Renee Otten, et al.
Nature (2023) Vol. 625, Iss. 7996, pp. 832-839
Open Access | Times Cited: 223
Mega-scale experimental analysis of protein folding stability in biology and design
Kotaro Tsuboyama, Justas Dauparas, Jonathan H. Chen, et al.
Nature (2023) Vol. 620, Iss. 7973, pp. 434-444
Open Access | Times Cited: 177
Loss-of-function, gain-of-function and dominant-negative mutations have profoundly different effects on protein structure
Lukas Gerasimavicius, Benjamin Livesey, Joseph A. Marsh
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 173
Revealing enzyme functional architecture via high-throughput microfluidic enzyme kinetics
Craig J. Markin, Daniel A. Mokhtari, Fanny Sunden, et al.
Science (2021) Vol. 373, Iss. 6553
Open Access | Times Cited: 164
Predicting and interpreting large-scale mutagenesis data using analyses of protein stability and conservation
Magnus Haraldson Høie, Matteo Cagiada, Anders Haagen Beck Frederiksen, et al.
Cell Reports (2022) Vol. 38, Iss. 2, pp. 110207-110207
Open Access | Times Cited: 108
Rapid protein stability prediction using deep learning representations
Lasse M. Blaabjerg, Maher M. Kassem, Lydia L. Good, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 103
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
Prediction of multiple conformational states by combining sequence clustering with AlphaFold2
Hannah K. Wayment-Steele, Sergey Ovchinnikov, Lucy J. Colwell, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 72
AlphaFold2 Can Predict Single-Mutation Effects
J. Michael McBride, Konstantin Polev, Amirbek Abdirasulov, et al.
Physical Review Letters (2023) Vol. 131, Iss. 21
Open Access | Times Cited: 47
A mutational atlas for Parkin proteostasis
Lene Clausen, Vasileios Voutsinos, Matteo Cagiada, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 20
High-Throughput Reclassification of SCN5A Variants
Andrew M. Glazer, Yuko Wada, Bian Li, et al.
The American Journal of Human Genetics (2020) Vol. 107, Iss. 1, pp. 111-123
Open Access | Times Cited: 120
Predicting changes in protein thermodynamic stability upon point mutation with deep 3D convolutional neural networks
Bian Li, Yucheng Yang, John A. Capra, et al.
PLoS Computational Biology (2020) Vol. 16, Iss. 11, pp. e1008291-e1008291
Open Access | Times Cited: 109
Identification of pathogenic missense mutations using protein stability predictors
Lukas Gerasimavicius, Xin Liu, Joseph A. Marsh
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 104
SAAFEC-SEQ: A Sequence-Based Method for Predicting the Effect of Single Point Mutations on Protein Thermodynamic Stability
Gen Li, Shailesh Kumar Panday, Emil Alexov
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 2, pp. 606-606
Open Access | Times Cited: 102
Unveiling invisible protein states with NMR spectroscopy
T. Reid Alderson, Lewis E. Kay
Current Opinion in Structural Biology (2019) Vol. 60, pp. 39-49
Closed Access | Times Cited: 96
Understanding the Origins of Loss of Protein Function by Analyzing the Effects of Thousands of Variants on Activity and Abundance
Matteo Cagiada, Kristoffer E. Johansson, Audronė Valančiūtė, et al.
Molecular Biology and Evolution (2021) Vol. 38, Iss. 8, pp. 3235-3246
Open Access | Times Cited: 89
NQO1: A target for the treatment of cancer and neurological diseases, and a model to understand loss of function disease mechanisms
Sarah K. Beaver, Noel Mesa‐Torres, Ángel L. Pey, et al.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2019) Vol. 1867, Iss. 7-8, pp. 663-676
Open Access | Times Cited: 88
On the Potential of Machine Learning to Examine the Relationship Between Sequence, Structure, Dynamics and Function of Intrinsically Disordered Proteins
Kresten Lindorff‐Larsen, Birthe B. Kragelund
Journal of Molecular Biology (2021) Vol. 433, Iss. 20, pp. 167196-167196
Open Access | Times Cited: 76
Assessment of the Diagnostic Yield of Combined Cardiomyopathy and Arrhythmia Genetic Testing
Lisa Dellefave‐Castillo, Allison L. Cirino, Thomas E. Callis, et al.
JAMA Cardiology (2022) Vol. 7, Iss. 9, pp. 966-966
Open Access | Times Cited: 54
MutateX: an automated pipeline for in silico saturation mutagenesis of protein structures and structural ensembles
Matteo Tiberti, Thilde Terkelsen, Kristine Degn, et al.
Briefings in Bioinformatics (2022) Vol. 23, Iss. 3
Open Access | Times Cited: 47
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: 41
Deep mutational scanning: A versatile tool in systematically mapping genotypes to phenotypes
Huijin Wei, Xianghua Li
Frontiers in Genetics (2023) Vol. 14
Open Access | Times Cited: 26
Rosace: a robust deep mutational scanning analysis framework employing position and mean-variance shrinkage
J. N. K. Rao, Ruiqi Xin, Christian B. Macdonald, et al.
Genome biology (2024) Vol. 25, Iss. 1
Open Access | Times Cited: 11
PRKN-linked familial Parkinson’s disease: cellular and molecular mechanisms of disease-linked variants
Lene Clausen, Justyna Okarmus, Vasileios Voutsinos, et al.
Cellular and Molecular Life Sciences (2024) Vol. 81, Iss. 1
Open Access | Times Cited: 9
Deep indel mutagenesis reveals the impact of amino acid insertions and deletions on protein stability and function
Magdalena Topolska, Antoni Beltran, Ben Lehner
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1
Page 1 - Next Page

Scroll to top