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:

Evaluating Protein Engineering Thermostability Prediction Tools Using an Independently Generated Dataset
Peishan Huang, Simon K. S. Chu, Henrique N. Frizzo, et al.
ACS Omega (2020) Vol. 5, Iss. 12, pp. 6487-6493
Open Access | Times Cited: 62

Showing 1-25 of 62 citing articles:

Engineering functional thermostable proteins using ancestral sequence reconstruction
Raine E. S. Thomson, Saskya E. Carrera-Pacheco, Elizabeth M. J. Gillam
Journal of Biological Chemistry (2022) Vol. 298, Iss. 10, pp. 102435-102435
Open Access | Times Cited: 48
Accurate Prediction of Enzyme Thermostabilization with Rosetta Using AlphaFold Ensembles
Francesca Peccati, Sara Alunno-Rufini, Gonzalo Jiménez‐Osés
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 3, pp. 898-909
Open Access | Times Cited: 26
Toward generalizable prediction of antibody thermostability using machine learning on sequence and structure features
Ameya Harmalkar, Roshan Rao, Yuxuan Richard Xie, et al.
mAbs (2023) Vol. 15, Iss. 1
Open Access | Times Cited: 25
Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review
Bei Ouyang, Guoping Wang, Nian Zhang, et al.
Molecules (2023) Vol. 28, Iss. 13, pp. 4990-4990
Open Access | Times Cited: 18
Predicting protein stability changes upon mutation using a simple orientational potential
Iván Martín Hernández, Yves Dehouck, Ugo Bastolla, et al.
Bioinformatics (2023) Vol. 39, Iss. 1
Open Access | Times Cited: 16
ELASPIC2 (EL2): Combining Contextualized Language Models and Graph Neural Networks to Predict Effects of Mutations
Alexey Strokach, Tianyu Lu, Philip M. Kim
Journal of Molecular Biology (2021) Vol. 433, Iss. 11, pp. 166810-166810
Open Access | Times Cited: 35
In-depth analysis of biocatalysts by microfluidics: An emerging source of data for machine learning
Michal Vasina, David Kovář, Jiřı́ Damborský, et al.
Biotechnology Advances (2023) Vol. 66, pp. 108171-108171
Closed Access | Times Cited: 12
Predicting protein stability and solubility changes upon mutations: data perspective
Stanislav Mazurenko
ChemCatChem (2020) Vol. 12, Iss. 22, pp. 5590-5598
Open Access | Times Cited: 31
Machine Learning Enables Selection of Epistatic Enzyme Mutants for Stability Against Unfolding and Detrimental Aggregation
Guangyue Li, Youcai Qin, Nicolas Fontaine, et al.
ChemBioChem (2020) Vol. 22, Iss. 5, pp. 904-914
Open Access | Times Cited: 31
Protein Function Analysis through Machine Learning
Chris Avery, John A. Patterson, Tyler Grear, et al.
Biomolecules (2022) Vol. 12, Iss. 9, pp. 1246-1246
Open Access | Times Cited: 19
SCONES: Self-Consistent Neural Network for Protein Stability Prediction Upon Mutation
Yashas B. L. Samaga, Shampa Raghunathan, U. Deva Priyakumar
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 38, pp. 10657-10671
Closed Access | Times Cited: 25
Reviewing Challenges of Predicting Protein Melting Temperature Change Upon Mutation Through the Full Analysis of a Highly Detailed Dataset with High-Resolution Structures
Benjamin B. V. Louis, Luciano A. Abriata
Molecular Biotechnology (2021) Vol. 63, Iss. 10, pp. 863-884
Open Access | Times Cited: 23
Engineering stable carbonic anhydrases for CO2 capture: a critical review
Mirfath Sultana Mesbahuddin, Aravindhan Ganesan, Subha Kalyaanamoorthy
Protein Engineering Design and Selection (2021) Vol. 34
Open Access | Times Cited: 23
Large-scale application of free energy perturbation calculations for antibody design
Fangqiang Zhu, Feliza Bourguet, William F. Bennett, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 16
Enhancement of quality and quantity of woody biomass produced in forests using machine learning algorithms
Wei Peng, Omid Karimi Sadaghiani
Biomass and Bioenergy (2023) Vol. 175, pp. 106884-106884
Open Access | Times Cited: 9
The role of data imbalance bias in the prediction of protein stability change upon mutation
Jianwen Fang
PLoS ONE (2023) Vol. 18, Iss. 3, pp. e0283727-e0283727
Open Access | Times Cited: 8
Efficient and feasible biocatalysts: Strategies for enzyme improvement. A review
Samah Hashim Albayati, Nima Ghahremani Nezhad, Abdulrahman M Taki, et al.
International Journal of Biological Macromolecules (2024) Vol. 276, pp. 133978-133978
Closed Access | Times Cited: 2
Genome-scale metabolic modeling of P. thermoglucosidasius NCIMB 11955 reveals metabolic bottlenecks in anaerobic metabolism
Viviënne Mol, Martyn Bennett, Benjamín J. Sánchez, et al.
Metabolic Engineering (2021) Vol. 65, pp. 123-134
Open Access | Times Cited: 17
A review on the applications of machine learning and deep learning in agriculture section for the production of crop biomass raw materials
Wei Peng, Omid Karimi Sadaghiani
Energy Sources Part A Recovery Utilization and Environmental Effects (2023) Vol. 45, Iss. 3, pp. 9178-9201
Closed Access | Times Cited: 6
Prediction of Enzyme Catalysis by Computing Reaction Energy Barriers via Steered QM/MM Molecular Dynamics Simulations and Machine Learning
Daniel Platero-Rochart, Tatyana Krivobokova, Michael Gastegger, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 15, pp. 4623-4632
Closed Access | Times Cited: 6
Thermogenetics: Applications come of age
Wai Kit David Chee, Jing Wui Yeoh, Viet Linh Dao, et al.
Biotechnology Advances (2022) Vol. 55, pp. 107907-107907
Closed Access | Times Cited: 11
Machine learning for sustainable reutilization of waste materials as energy sources – a comprehensive review
Wei Peng, Omid Karimi Sadaghiani
International Journal of Green Energy (2023) Vol. 21, Iss. 7, pp. 1641-1666
Closed Access | Times Cited: 5
High-Temperature Tolerance Protein Engineering through Deep Evolution
Huanyu Chu, Zhenyang Tian, Lingling Hu, et al.
BioDesign Research (2024) Vol. 6
Open Access | Times Cited: 1
Molecular characterization of the PhiKo endolysin from Thermus thermophilus HB27 bacteriophage phiKo and its cryptic lytic peptide RAP-29
Monika Szadkowska, Aleksandra M. Kocot, Daria Sowik, et al.
Frontiers in Microbiology (2024) Vol. 14
Open Access | Times Cited: 1
A Novel Non‐Destructive Rapid Tool for Estimating Amino Acid Composition and Secondary Structures of Proteins in Solution
Narangerel Altangerel, Benjamin W. Neuman, Philip Hemmer, et al.
Small Methods (2024) Vol. 8, Iss. 7
Open Access | Times Cited: 1
Page 1 - Next Page

Scroll to top