Allosteric post-translational modification codes

The language of covalent histone modifications

Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679

The Universal Protein Resource (UniProt)

Bairoch, A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki070 · Cited by 3,774

How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers

Taverna, S. D., Li, H., Ruthenburg, A. J., Allis, C. D., & Patel, D. J. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1338 · Cited by 1,476

The FoxO code

Calnan, D. R., & Brunet, A. (2008) · Oncogene · doi:10.1038/onc.2008.21 · Cited by 1,170

HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor

Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153

Quantitative Proteomics Reveals the Function of Unconventional Ubiquitin Chains in Proteasomal Degradation

Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, A. J., Hochstrasser, M., Finley, D. J., & Peng, J. (2009) · Cell · doi:10.1016/j.cell.2009.01.041 · Cited by 1,125

Chromatin remodelling during development

Ho, L., & Crabtree, G. R. (2010) · Nature · doi:10.1038/nature08911 · Cited by 1,114

Nonproteolytic Functions of Ubiquitin in Cell Signaling

Chen, Z. J., & Sun, L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.014 · Cited by 948

Is allostery an intrinsic property of all dynamic proteins?

Gunasekaran, K., Ma, B., & Nussinov, R. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20232 · Cited by 896

Post-translational modifications in signal integration

Deribe, Y. L., Pawson, T., & Dikic, I. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1842 · Cited by 876

Allostery and Missense Mutations as Intermittently Linked Promising Aspects of Modern Computational Drug Discovery

Bishop, Ö. T., Musyoka, T. M., & Barozi, V. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167610 · Cited by 23

Spatial and Temporal Effects in Protein Post-translational Modification Distributions in the Developing Mouse Brain

Edwards, A. V. G., Edwards, G. J., Schwämmle, V., Saxtorph, H., & Larsen, M. R. (2014) · Journal of Proteome Research · doi:10.1021/pr4002977 · Cited by 22

Characteristics of Allosteric Proteins, Sites, and Modulators

He, X., Ni, D., Lu, S., & Zhang, J. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-8719-7_6 · Cited by 22

Identification and Inhibition of the Druggable Allosteric Site of SARS-CoV-2 NSP10/NSP16 Methyltransferase through Computational Approaches

Faisal, S., Badshah, S. L., Kubra, B., Sharaf, M., Emwas, A.-H. M., Jaremko, M., & Abdalla, M. (2022) · Molecules · doi:10.3390/molecules27165241 · Cited by 22

Single‐residue posttranslational modification sites at the N‐terminus, C‐terminus or in‐between: To be or not to be exposed for enzyme access

Sirota, F. L., Maurer‐Stroh, S., Eisenhaber, B., & Eisenhaber, F. (2015) · PROTEOMICS · doi:10.1002/pmic.201400633 · Cited by 20

Molecular dynamics shows complex interplay and long-range effects of post-translational modifications in yeast protein interactions

Šoštarić, N., & van Noort, V. (2021) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1008988 · Cited by 23

Targeting the Post-translational Proteome with Intrabodies

Cattaneo, A., & Chirichella, M. (2018) · Trends in biotechnology · doi:10.1016/j.tibtech.2018.11.009 · Cited by 20

Mass spectrometry-based proteomics analyses of post-translational modifications and proteoforms in human pituitary adenomas

Li, J., & Zhan, X. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140584 · Cited by 22

Post-Translational Modifications Modulate Ligand Recognition by the Third PDZ Domain of the MAGUK Protein PSD-95

Murciano‐Calles, J., Corbi‐Verge, C., Candel, A. M., Luque, I., & Martínez, J. C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090030 · Cited by 21

Interrogating Regulatory Mechanisms in Signaling Proteins by Allosteric Inhibitors and Activators: A Dynamic View Through the Lens of Residue Interaction Networks

Astl, L., Tse, A., & Verkhivker, G. M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-8719-7_9 · Cited by 18

Abnormal expression and the significant prognostic value of aquaporins in clear cell renal cell carcinoma

Li, M., He, M., Xu, F., Guan, Y., Tian, J., Wan, Z., Zhou, H., Gao, M., & Chong, T. (2022) · PLoS ONE · doi:10.1371/journal.pone.0264553 · Cited by 20

The Loss and Gain of Functional Amino Acid Residues Is a Common Mechanism Causing Human Inherited Disease

Lugo-Martinez, J., Pejaver, V. R., Pagel, K. A., Jain, S., Mort, M. E., Cooper, D. N., Mooney, S. D., & Predrag Radivojac, A. (2016) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005091 · Cited by 20

Dynamics of Post-Translational Modification Inspires Drug Design in the Kinase Family.

Zhang, H., He, J.-X., Hu, G., Zhu, F., Jiang, H., Gao, J., Zhou, H., Lin, H., Wang, Y.-J., Chen, K.-F., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01076 · Cited by 9

Artificial Intelligence Transforming Post-Translational Modification Research

Kim, D. N., Yin, T., Zhang, T., Im, A. K., Cort, J., Rozum, J. C., Pollock, D. D., Qian, W., & Feng, S. (2024) · Bioengineering · doi:10.3390/bioengineering12010026 · Cited by 19

Allosteric Modulation of SERCA Pumps in Health and Disease: Structural Dynamics, Posttranslational Modifications, and Therapeutic Potential

Viskupičová, J., & Espinoza-Fonseca, M. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169200 · Cited by 19

Advances in deubiquitinating enzymes in lung adenocarcinoma

Zhou, X., Li, R., Liu, X., & Qu, Y.-Q. (2021) · Journal of Cancer · doi:10.7150/jca.56532 · Cited by 19

Dynamic Protein Allosteric Regulation and Disease

Nussinov, R., Tsai, C.-J., & Jang, H. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-13-8719-7_2 · Cited by 18

Global comparative structural analysis of responses to protein phosphorylation

Marrero, M. C., Mello, V. H., Sartori, P., & Beltrão, P. (2025) · Nature Communications · doi:10.1038/s41467-025-64116-4 · Cited by 18

Towards understanding the crosstalk between protein post‐translational modifications: Homo‐ and heterotypic PTM pair distances on protein surfaces are not random

Korkuć, P., & Walther, D. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25200 · Cited by 19

Leveraging Protein Dynamics to Identify Functional Phosphorylation Sites using Deep Learning Models

Zhu, F., Yang, S., Meng, F., Zheng, Y., Ku, X., Luo, C., Hu, G., & Liang, Z. T. (2022) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c00484 · Cited by 18

Phosphoproteome Study of Escherichia coli Devoid of Ser/Thr Kinase YeaG During the Metabolic Shift From Glucose to Malate

Sultan, A., Jers, C., Ganief, T. A., Shi, L., Senissar, M., Køhler, J. B., Maček, B., & Mijakovic̀, I. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.657562 · Cited by 19

Pairwise detection of site-specific receptor phosphorylations using single-molecule blotting

Kim, K. L., Kim, D., Lee, S., Kim, S.-J., Noh, J. E., Kim, J., Chae, Y. C., Lee, J., & Ryu, S. H. (2016) · Nature Communications · doi:10.1038/ncomms11107 · Cited by 17

Crystallographic mining of ASK1 regulators to unravel the intricate PPI interfaces for the discovery of small molecule

Agrahari, A. K., Dikshit, M., & Asthana, S. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.07.008 · Cited by 18

PTMOracle: A Cytoscape App for Covisualizing and Coanalyzing Post-Translational Modifications in Protein Interaction Networks

Tay, A. P., Pang, C. N. I., Winter, D. L., & Wilkins, M. R. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b01052 · Cited by 18

Deciphering Combinatorial Genetics

Wong, A. S. L., Choi, G. C. G., & Lu, T. K. (2016) · Annual Review of Genetics · doi:10.1146/annurev-genet-120215-034902 · Cited by 17

Drug resistance and tumor heterogeneity: cells and ensembles

Nussinov, R., Yavuz, B. R., & Jang, H. (2025) · Biophysical Reviews · doi:10.1007/s12551-025-01320-y · Cited by 18

The GhMPK7 ‐ GhSDIRIP1 module enhances drought tolerance in cotton by regulating ABA signaling

Gao, Z., Gao, Y., Jia, H., Wang, W., Xue, B., Su, Y. H., Guo, X., & Wang, C. (2025) · New Phytologist · doi:10.1111/nph.70497 · Cited by 16

Hyperglycemia exacerbates osteoarthritis by impairing macrophage efferocytosis through modulation of CD11b lactylation

Zhou, H., Xiao, Y., Xue, X., Liu, J., Xu, H., Wang, J., Zhou, J., Zuo, Q., Liang, W.-W., Song, H., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-67473-2 · Cited by 16

A Web of Possibilities: Network-Based Discovery of Protein Interaction Codes

Winter, D. L., Erce, M. A., & Wilkins, M. R. (2014) · Journal of Proteome Research · doi:10.1021/pr500585p · Cited by 16

Identification and Phenotypic Characterization of Hsp90 Phosphorylation Sites That Modulate Virulence Traits in the Major Human Fungal Pathogen Candida albicans

Alaalm, L., Crunden, J. L., Butcher, M. C., Obst, U., Whealy, R. N., Williamson, C. E., O’Brien, H., Schaffitzel, C., Ramage, G., SPENCER, J. M., et al. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.637836 · Cited by 16

Microsecond molecular dynamics simulations provide insight into the ATP‐competitive inhibitor‐induced allosteric protection of Akt kinase phosphorylation

Mou, L., Cui, T., Liu, W., Zhang, H., Cai, Z., Lu, S., & Gao, G. (2016) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12895 · Cited by 15

Controllable Activation of Nanoscale Dynamics in a Disordered Protein Alters Binding Kinetics

Callaway, D. J. E., Matsui, T., Weiss, T. M., Stingaciu, L. R., Stanley, C. B., Heller, W. T., & Bu, Z. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.003 · Cited by 17

Phosphoproteome Analysis Identifies a Synaptotagmin-1-Associated Complex Involved in Ischemic Neuron Injury

Jiang, W., Zhang, P., Yang, P. H., Kang, N., Liu, J., Aihemaiti, Y., & Tu, H. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100222 · Cited by 17

PEIMAN 1.0: Post-translational modification Enrichment, Integration and Matching ANalysis

Nickchi, P., Jafari, M., & Kalantari, S. (2015) · Database · doi:10.1093/database/bav037 · Cited by 16

Insights into Phosphorylation-Induced Protein Allostery and Conformational Dynamics of Glycogen Phosphorylase via Integrative Structural Mass Spectrometry and In Silico Modeling

Huang, J., Chu, X., Luo, Y., Wang, Y., Zhang, Y., Zhang, Y., & Li, H. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00393 · Cited by 13

PPICT: an integrated deep neural network for predicting inter-protein PTM cross-talk

Zhu, F., Deng, L., Dai, Y., Zhang, G., Meng, F., Luo, C., Hu, G., & Liang, Z. T. (2023) · Briefings in Bioinformatics · doi:10.1093/bib/bbad052 · Cited by 14

Neuronal process structure and growth proteins are targets of heavy PTM regulation during brain development

Edwards, A. V. G., Schwämmle, V., & Larsen, M. R. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2014.02.010 · Cited by 14

Structural Data in Synthetic Biology Approaches for Studying General Design Principles of Cellular Signaling Networks

Kiel, C., & Serrano, L. G. (2012) · Structure · doi:10.1016/j.str.2012.10.002 · Cited by 14

In vitro biological characterization of IFN- -1a major glycoforms

Mastrangeli, R., Rossi, M., Mascia, M., Palinsky, W., Datola, A., Terlizzese, M., & Bierau, H. (2014) · Glycobiology · doi:10.1093/glycob/cwu082 · Cited by 14

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

Eichmann, C., Tzitzilonis, C., Nakamura, T., Kwiatkowski, W., Maslennikov, I., Choe, S., Lipton, S. A., & Riek, R. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.07.010 · Cited by 16

Cullin neddylation may allosterically tune polyubiquitin chain length and topology

Onel, M., Sumbul, F., Liu, J., Nussinov, R., & Haliloǧlu, T. (2017) · Biochemical Journal · doi:10.1042/bcj20160748 · Cited by 14

FuncPhos-STR: An integrated deep neural network for functional phosphosite prediction based on AlphaFold protein structure and dynamics

Zhang, G., Zhang, C., Cai, M., Luo, C., Zhu, F., & Liang, Z. T. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.131180 · Cited by 14

Prediction of Functionally Important Phospho-Regulatory Events in Xenopus laevis Oocytes

Johnson, J. R., Santos, S. D. M., Johnson, T. L., Pieper, U., Strumillo, M., Wagih, O., Šali, A., Krogan, N. J., & Beltrão, P. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004362 · Cited by 13

Effect of different arginine methylations on the thermodynamics of Tat peptide binding to HIV-1 TAR RNA

Kumar, S., & Maiti, S. (2013) · Biochimie · doi:10.1016/j.biochi.2013.03.008 · Cited by 13

Decoding protein structures with residue interaction networks

Begue, S. C., Leonardi, E., & Tosatto, S. C. E. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2025.08.006 · Cited by 13

Multilayered allosteric modulation of coupled folding and binding by phosphorylation, peptidyl-prolyl cis/trans isomerization, and diversity of interaction partners

Buholzer, K., McIvor, J. A. P., Zosel, F., Teppich, C., Nettels, D., Mercadante, D., & Schuler, B. (2022) · The Journal of Chemical Physics · doi:10.1063/5.0128273 · Cited by 13

Phosphorylation of P-stalk proteins defines the ribosomal state for interaction with auxiliary protein factors

Filipek, K., Blanchet, S., Molestak, E., Zaciura, M., Wu, C. C., Horbowicz‐Drożdżal, P., Grela, P., Zalewski, M., Kmiecik, S., Ibarra, A. A. G., et al. (2024) · EMBO Reports · doi:10.1038/s44319-024-00297-1 · Cited by 10

ERK Allosteric Activation: The Importance of Two Ordered Phosphorylation Events

Regev, C., Jang, H., & Nussinov, R. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169130 · Cited by 11

Allosteric therapies for lung cancer

Ye, L., Jing, M., & Wang, X. (2015) · Cancer and Metastasis Reviews · doi:10.1007/s10555-015-9567-z · Cited by 12

Biomolecular Systems Engineering: Unlocking the Potential of Engineered Allostery via the Lactose Repressor Topology

Groseclose, T. M., Rondon, R. E., Hersey, A. N., Milner, P. T., Kim, D., Zhang, F., Realff, M. J., & Wilson, C. J. (2021) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-090820-101708 · Cited by 11

Allosteric Regulation of the Soluble Epoxide Hydrolase by Nitro Fatty Acids: a Combined Experimental and Computational Approach

Qiu, Q., Abis, G., Mattingly-Peck, F., Lynham, S., Fraternali, F., & Conte, M. R. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167600 · Cited by 11

Engineering allosteric communication

Herde, Z. D., Short, A. E., Kay, V. E., Huang, B. D., Realff, M. J., & Wilson, C. J. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.05.004 · Cited by 11

Insights into Conformational Dynamics and Allostery in DNMT1-H3Ub/USP7 Interactions

Zhu, Y., Ye, F., Zhou, Z., Liu, W., Liang, Z. T., & Hu, G. (2021) · Molecules · doi:10.3390/molecules26175153 · Cited by 11

Lectins as a promising therapeutic agent for breast cancer: A review

Singh, K., Agrawal, L., Gupta, R., Singh, D., Kathpalia, M., & Kaur, N. (2024) · Breast Disease · doi:10.3233/bd-230047 · Cited by 10

A comprehensive in silico analysis of the deleterious nonsynonymous SNPs of human FOXP2 protein

Akter, M., Khan, S. F., Sajib, A. A., & Rima, F. S. (2022) · PLoS ONE · doi:10.1371/journal.pone.0272625 · Cited by 10

Considerations for defining +80 Da mass shifts in mass spectrometry-based proteomics: phosphorylation and beyond

Daly, L. A., Clarke, C. J., Po, A., Oswald, S. O., & Eyers, C. E. (2023) · Chemical Communications · doi:10.1039/d3cc02909c · Cited by 11

Spatial proximity statistics suggest a regulatory role of protein phosphorylation on compound binding

Korkuć, P., & Walther, D. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25001 · Cited by 10

How residence time works in allosteric drugs

Nussinov, R., & Jang, H. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103149 · Cited by 10

Allosteric Modulators

Lu, S., & Zhang, J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12324-8 · Cited by 9

Specifics of Metabolite-Protein Interactions and Their Computational Analysis and Prediction

Walther, D. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2624-5_12 · Cited by 9

DEFB126 polymorphisms and association with idiopathic asthenozoospermia in China

He, J., Peng, J., Li, Q., Lin, X., Cui, Y., Ma, S.-Y., Fan, S.-Y., Liu, Y.-R., Song, Z., Deng, J.-H., et al. (2022) · Asian Journal of Andrology · doi:10.4103/aja2021115 · Cited by 8

Visualizing Post‐Translational Modifications in Protein Interaction Networks Using PTMOracle

Tay, A. P., Liang, A., Wilkins, M. R., & Pang, C. N. I. (2019) · Current Protocols in Bioinformatics · doi:10.1002/cpbi.71 · Cited by 9

Dose-response regulation system for improving renal injury in diabetic nephropathy by buckwheat hull flavonoids

Tang, Y., Li, T., Peng, L., Liu, J., Wang, Y., & Piao, C. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.103561 · Cited by 8

Energy landscapes in molecular biology: History, principles, and perspectives

Nussinov, R., Regev, C., & Jang, H. (2026) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583526100134 · Cited by 8

Proteins with cognition-associated structural changes in a rat model of aging exhibit reduced refolding capacity

Tarbox, H. E., Branch, A., & Fried, S. D. (2025) · Science Advances · doi:10.1126/sciadv.adt3778 · Cited by 8

Allostery in Biomolecular Condensates

Nussinov, R., Regev, C., & Jang, H. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169446 · Cited by 6

Monitoring Functional Posttranslational Modifications Using a Data‐Driven Proteome Informatic Pipeline

Nickchi, P., Vadadokhau, U., Mirzaie, M., Baumann, M., Saei, A. A., & Jafari, M. (2025) · PROTEOMICS · doi:10.1002/pmic.202400238 · Cited by 6

Phosphorylation of the conserved C‐terminal domain of ribosomal P‐proteins impairs the mode of interaction with plant toxins

Horbowicz‐Drożdżal, P., Kamel, K., Kmiecik, S., Borkiewicz, L., Tumer, N. E., Shaw, P., Tchórzewski, M., & Grela, P. (2021) · FEBS Letters · doi:10.1002/1873-3468.14170 · Cited by 6

Comprehensive Analysis of Lysine β-Hydroxybutyrylation Modification in Ischemia–reperfusion Injury in Mouse Heart Transplantation

Cheng, C., Meng, Y., Pan, Y., Zhang, Y., He, S.-Y. R., Baral, K., & Zhao, M. (2025) · Transplantation · doi:10.1097/tp.0000000000005432 · Cited by 5

Lysine acetylproteome analysis reveals the lysine acetylation in developing fruit and a key acetylated protein involved in sucrose accumulation in Rosa roxburghii Tratt.

Zhang, X., Lu, M., & An, H. (2024) · Journal of Proteomics · doi:10.1016/j.jprot.2024.105248 · Cited by 5

PlantMWpIDB: a database for the molecular weight and isoelectric points of the plant proteomes

Mohanta, T. K., Kamran, M. S., Omar, M., Anwar, W., & Choi, G. S. (2022) · Scientific Reports · doi:10.1038/s41598-022-11077-z · Cited by 5

Exploring Pathogenic Mutation in Allosteric Proteins: The Prediction and Beyond

Zhang, H., Ju, Z., Zhang, J., Li, X., Xiao, H., Chen, X., Li, Y., Wang, X., & Wei, Y. (2025) · Tsinghua Science and Technology · doi:10.26599/tst.2024.9010226 · Cited by 4

Improving phosphopeptide identification in shotgun proteomics by supervised filtering of peptide-spectrum matches

Li, S., Arnold, R. J., Tang, H., & Predrag Radivojac, A. (2013) · ACM International Conference on Bioinformatics, Computational Biology, and Health Informatics (ACM-BCB) · doi:10.1145/2506583.2506634 · Cited by 4

Histone deacetylase inhibitor (HDACi) upregulates activin A and activates the Smad signaling pathway in melanomas

Lee, J., Ko, J., & Yi, J. Y. (2017) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2017.12.011 · Cited by 4

Quantifying Proteome and Protein Modifications in Activated T Cells by Multiplexed Isobaric Labeling Mass Spectrometry

Tan, H., Blanco, D. B., Xie, B., Li, Y., Wu, Z., Chi, H., & Peng, J. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1311-5_23 · Cited by 5

Malonylome analysis uncovers the association of lysine malonylation with metabolism and acidic stress in pathogenic Mycobacterium tuberculosis

Bi, J., Guo, Q., Zhou, Z., Huang, X., Qin, L., Tao, X., Ye, T., Chen, L., Li, G., Wang, Z., et al. (2022) · Microbiological Research · doi:10.1016/j.micres.2022.127209 · Cited by 4

Local Hydration Control and Functional Implications Through S-Nitrosylation of Proteins: Kirsten Rat Sarcoma Virus (K-RAS) and Hemoglobin (Hb)

Turan, H. T., & Meuwly, M. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c07371 · Cited by 4

Protein kinase A controls the hexosamine pathway by tuning the feedback inhibition of GFAT-1Preprint

Ruegenberg, S., Mayr, F. A. M. C., Miethe, S., Atanassov, I., Baumann, U., & Denzel, M. S. (2020) · Research Square · doi:10.21203/rs.3.rs-49753/v1 · Cited by 4

Phosphorylation induces altered protonation states and allosterically regulates Rac1– RhoGDI complex

Sinha, K., Kumawat, A., Jang, H., Nussinov, R., & Chakrabarty, S. (2025) · Protein Science · doi:10.1002/pro.70413 · Cited by 4

Deubiquitinase USP37 enhances the anti-HIV-2/SIV ability of the host restriction factor SAMHD1

Cui, W., Wang, H., Gao, Y., Zhang, X., Xin, J., Li, Z., Li, G., Gao, W., & Zhang, W. (2024) · Journal of Virology · doi:10.1128/jvi.01858-24 · Cited by 3

O- GlcNAcylation regulates tyrosine hydroxylase serine 40 phosphorylation and l -DOPA levels

Rodrigues, B. D. C., Lucena, M. C., Costa, A. C. R., Oliveira, I. D. A., Thaumaturgo, M. A. S., Paes-Colli, Y., Beckman, D., Ferreira, S. T., Mello, F. G. D., Reis, R. A. D. M., et al. (2025) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00215.2024 · Cited by 3

Unveiling the pathogenicity of allosteric protein mutations via multifaceted feature ensembling

Zhang, H., Li, X., Huang, J., Li, Y., Cai, S., Wang, H., & Wei, Y. (2025) · Methods · doi:10.1016/j.ymeth.2025.07.014 · Cited by 3

Phosphorylation of multifunctional galectins by protein kinases CK1, CK2, and PKA

Kübler, H.-D., Seidler, J., André, S., Kumar, S., Schwartz‐Albiez, R., Lehmann, W., & Gabius, H. (2013) · Analytical Biochemistry · doi:10.1016/j.ab.2013.12.006 · Cited by 3

Statistical characterization of therapeutic protein modifications

Tsai, T., Hao, Z., Hong, Q., Moore, B. N., Stella, C., Zhang, J. H., Chen, Y., Kim, M. T.-J., Koulis, T., Ryslik, G., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-08333-y · Cited by 3

Measuring proteomes with long strings: A new, unconstrained paradigm in mass spectrum interpretationPreprint

Devabhaktuni, A., Olsson, N., Gonzales, C., Rawson, K., Swaminathan, K., & Elias, J. E. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/282624 · Cited by 3

Harnessing natural diversity to identify key amino acid residues in prolidasePreprint

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