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Recent advances suggest increased influence of selective pressure in allostery

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OPTIMIZATION OF ENZYME PARAMETERS FOR FERMENTATIVE PRODUCTION OF BIORENEWABLE FUELS AND CHEMICALS

Jarboe, L. R., Liu, P., Kautharapu, K. B., & Ingram, L. O. (2012) · Computational and Structural Biotechnology Journal · doi:10.5936/csbj.201210005 · Cited by 14 · see citing works

CASBench: A Benchmarking Set of Proteins with Annotated Catalytic and Allosteric Sites in Their Structures

Zlobin, A. S., Suplatov, D. A., Kopylov, K., & Švedas, V. K. (2019) · Acta Naturae · doi:10.32607/20758251-2019-11-1-74-80 · Cited by 14 · see citing works

Exploring the ameliorative role of α7 neuronal nicotinic acetylcholine receptor modulation in epilepsy and associated comorbidities in post-PTZ-kindled mice

Sharma, N., Kaur, S., & Goel, R. K. (2020) · Epilepsy & Behavior · doi:10.1016/j.yebeh.2019.106862 · Cited by 14 · see citing works

Known allosteric proteins have central roles in genetic disease

Abrusán, G., Ascher, D. B., & Inouye, M. (2022) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009806 · Cited by 13 · see citing works

Structural analysis of protein tyrosine phosphatase 1B reveals potentially druggable allosteric binding sites

Kumar, A. P., Nguyen, M. N., Verma, C. S., & Lukman, S. (2017) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25440 · Cited by 13 · see citing works

Mutation in the Pro-Peptide Region of a Cysteine Protease Leads to Altered Activity and Specificity—A Structural and Biochemical Approach

Dutta, S., Choudhury, D., Roy, S., Dattagupta, J. K., & Biswas, S. (2016) · PLoS ONE · doi:10.1371/journal.pone.0158024 · Cited by 12 · see citing works

Allosteric regulation of metabolism in cancer: endogenous mechanisms and considerations for drug design

Macpherson, J. A., & Anastasiou, D. (2017) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2017.03.022 · Cited by 12 · see citing works

Allosteric Modulators of Potential Targets Related to Alzheimer's Disease: a Review

Silva, G. M., Barcelos, M. P., Poiani, J. G. C., Hage-Melim, L. I. D. S., & da Silva, C. H. T. D. P. (2019) · ChemMedChem · doi:10.1002/cmdc.201900299 · Cited by 11 · see citing works

Positive allosteric modulators of the α7 nicotinic acetylcholine receptor potentiate glutamate release in the prefrontal cortex of freely-moving rats

Bortz, D. M., Upton, B. A., Mikkelsen, J. D., & Bruno, J. P. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.08.033 · Cited by 11 · see citing works

Use of Nicotinamide Mononucleotide as Non-Natural Cofactor

Naaz, T., & Kim, B. S. (2025) · Catalysts · doi:10.3390/catal15010037 · Cited by 9 · see citing works

Main methods and tools for peptide development based on protein-protein interactions (PPIs)

Baeza, J., Bedoya, M., Cruz, P., Ojeda, P., Adasme-Carreño, F., Cerda, O., & González, W. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151623 · Cited by 8 · see citing works

An enzyme activation network reveals extensive regulatory crosstalk between metabolic pathways

Zubaidi, S. M. A., Nasar, M. I., Notebaart, R. A., Ralser, M., & Alam, M. T. (2025) · Molecular Systems Biology · doi:10.1038/s44320-025-00111-7 · Cited by 8 · see citing works

The development of novel polypharmacological agents targeting the multiple binding sites of nicotinic acetylcholine receptors

Reyes-Parada, M. I., & Iturriaga‐Vásquez, P. (2016) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2016.1227317 · Cited by 8 · see citing works

Allosteric pluripotency: challenges and opportunities

Akimoto, M., Pomier, K. M., VanSchouwen, B., Byun, J. A., Khamina, M., & Melacini, G. (2022) · Biochemical Journal · doi:10.1042/bcj20210528 · Cited by 8 · see citing works

High-Throughput Screening for Positive Allosteric Modulators Identified Potential Therapeutics against Acetylcholinesterase Inhibition

Chapleau, R. R., McElroy, C. A., Ruark, C. D., Fleming, E. J., Ghering, A. B., Schlager, J. J., Poeppelman, L. D., & Gearhart, J. M. (2015) · SLAS DISCOVERY · doi:10.1177/1087057115591006 · Cited by 8 · see citing works

A three-level regulatory mechanism of the aldo-keto reductase subfamily AKR12D

Xiao, Z., Zha, J., Yang, X., Huang, T., Huang, S., Liu, Q., Wang, X., Zhong, J., Zheng, J., Liang, R., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46363-z · Cited by 7 · see citing works

Allosteric properties of Geobacillus maltogenic amylase

Parvaneh, R., Sajedi, R. H., Zamani, P., Rahmani, H., & Khajeh, K. (2016) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2016.09.011 · Cited by 7 · see citing works

The evolution of allostery in a protein familyPreprint

Martí-Aranda, A., & Lehner, B. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.20.660748 · Cited by 6 · see citing works

The role of microglia in Zika virus pathogenesis: Possible diagnostic and therapeutic strategies

Paul, S., Patra, S., Mondal, A., Adhikari, G. S., Ghosh, P., Bysack, M., & Dey, R. (2024) · The Microbe · doi:10.1016/j.microb.2024.100180 · Cited by 5 · see citing works

Chemical and Biophysical Approaches to Allosteric Modulation

Civera, M., Moroni, E., Sorrentino, L., Vasile, F., & Sattin, S. (2021) · European Journal of Organic Chemistry · doi:10.1002/ejoc.202100506 · Cited by 6 · see citing works

An integrative approach to improving the biocatalytic reactions of whole cells expressing recombinant enzymes

Shin, K., & Oh, D. (2021) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-021-03075-6 · Cited by 4 · see citing works

Resistance to Allosteric Inhibitors

Outhwaite, I. R., Kwan, I., Leyte-Vidal, A., Shah, N. P., Bahar, İ., & Seeliger, M. A. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169133 · Cited by 4 · see citing works

Molecular dynamics simulations of allosteric motions and competitive inhibition of the Zika virus helicase

Raubenolt, B. A., Wong, K., & Rick, S. W. (2021) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2021.108001 · Cited by 3 · see citing works

Enzyme engineering for advanced treatment of textile wastewater

Inamdar, S., Vanarase, K., & Inamdar, S. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-91235-8.00010-3 · Cited by 3 · see citing works

The structure of DNA methyltransferase DNMT3C reveals an activity-tuning mechanism for DNA methylation

Khudaverdyan, N., Lu, J., Chen, X., Herle, G., & Song, J. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107633 · Cited by 3 · see citing works

Single‐Molecule DNA Tweezers Enable Programmable Control of Enzyme Activity via Arbitrary Molecular Cues

Godhulayyagari, S., Nixon, S. R., & Samanta, D. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202513154 · Cited by 2 · see citing works

Allosteric modulation of Plasmodium falciparum Isoleucyl tRNA synthetase by South African natural compounds

Chepsiror, C., Veldman, W., Olotu, F. A., & Bishop, Ö. T. (2025) · PLoS ONE · doi:10.1371/journal.pone.0321444 · Cited by 2 · see citing works

High-Throughput Screening of Acyl-CoA Thioesterase I Mutants Using a Fluid Array Platform

Lim, J. W., Shin, K. S., Ryu, Y. S., Lee, Y., Lee, S. K., & Kim, T. (2019) · ACS Omega · doi:10.1021/acsomega.9b02826 · Cited by 2 · see citing works

Single‐Molecule DNA Tweezers Enable Programmable Control of Enzyme Activity via Arbitrary Molecular Cues

Godhulayyagari, S., Nixon, S. R., & Samanta, D. (2025) · Angewandte Chemie · doi:10.1002/ange.202513154 · Cited by 1 · see citing works

Hot CoFi Blot: A High-Throughput Colony-Based Screen for Identifying More Thermally Stable Protein Variants

Asial, I., Nordlund, P., & Dahlroth, S. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9624-7_14 · Cited by 1 · see citing works

An enzyme activation network provides evidence for extensive regulatory crosstalk between metabolic pathwaysPreprint

Zubaidi, S. M. A., Nasar, M. I., Ralser, M., Notebaart, R. A., & Alam, M. T. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.16.567372 · Cited by 1 · see citing works

Organic codes and their identification : is the histone code a true organic code

Kühn, S. (2014) · SUNScholar (Stellenbosch University)

α7 Nicotinic Receptor Modulation Alters Glutamate Release: Implications for Cognitive Deficits in Schizophrenia

Upton, B. A. (2015) · The Knowledge Bank (The Ohio State University)

Modeling O2-dependent Heme Enzymes: A Quick Guide for Non-experts

Sancho, F., Santiago, G., Amengual-Rigo, P., & Guallar, V. (2018) · Royal Society of Chemistry eBooks · doi:10.1039/9781788012911-00222

Inhibition of Biotin Carboxylase by Three Antibacterial Compounds

Craft, M. (2022) · doi:10.31390/gradschool_dissertations.5751

Identification de nouvelles voies d'inhibition ciblant les mouvements fonctionnels de protéines : application à la transition allostérique du récepteur nicotinique de l'acétylcholine

Monet, D. (2018) · doi:10.70675/347d5472zc8a1z421aza884z5cff11a0fc15

Engineering allosteric regulation in ionotropic glutamate receptors to generate molecular tools for investigating synaptic functions

Gupta, A. K., Parmar, R., G, M. S. M., Vinnakota, R., & Kumar, J. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-44536-1.00018-3

BindingDB Entry 50009378: Allosteric Modulator Discovery: From Serendipity to Structure-Based Design.

BindingDB (2021) · UC San Diego · doi:10.7270/q2c53q9m

Funding:...

Yang, J., Seo, S. W., Jang, S., Jung, G. Y., & Kim, S. (2012)

Engineering Allosteric Regulation into Biological Catalysts

Fastrez, J. (2009) · ChemBioChem · doi:10.1002/cbic.200900590 · Cited by 38 · see citing works

Integrating molecular dynamics and co-evolutionary analysis for reliable target prediction and deregulation of the allosteric inhibition of aspartokinase for amino acid production

Chen, Z., Rappert, S., Sun, J., & Zeng, A. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2011.05.005 · Cited by 54 · see citing works

Design of a switchable eliminase

Korendovych, I. V., Kulp, D. W., Wu, Y., Cheng, H., Röder, H., & DeGrado, W. F. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018191108 · Cited by 126 · see citing works

Engineering allosteric control to an unregulated enzyme by transfer of a regulatory domain

Cross, P. J., Allison, T. M., Dobson, R. C. J., Jameson, G. B., & Parker, E. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217923110 · Cited by 49 · see citing works