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 in Disease and in Drug Discovery

Nussinov, R., & Tsai, C. (2013) · Cell · doi:10.1016/j.cell.2013.03.034 · Cited by 769

Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436

The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery

Papaleo, E., Saladino, G., Lambrughi, M., Lindorff‐Larsen, K., Gervasio, F. L., & Nussinov, R. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00623 · Cited by 434

Protein Language: Post-Translational Modifications Talking to Each Other.

Vu, L. D., Gevaert, K., & Smet, I. D. (2018) · Trends in Plant Science · doi:10.1016/j.tplants.2018.09.004 · Cited by 340

The structural and functional signatures of proteins that undergo multiple events of post‐translational modification

Pejaver, V., Hsu, W., Xin, F., Dunker, A. K., Uversky, V. N., & Radivojac, P. (2014) · Protein Science · doi:10.1002/pro.2494 · Cited by 349

The next level of complexity: Crosstalk of posttranslational modifications

Venne, A. S., Kollipara, L., & Zahedi, R. P. (2013) · PROTEOMICS · doi:10.1002/pmic.201300344 · Cited by 331

Effects of N-glycosylation on protein conformation and dynamics: Protein Data Bank analysis and molecular dynamics simulation study

Lee, H.-S., Qi, Y., & Im, W. (2015) · Scientific Reports · doi:10.1038/srep08926 · Cited by 270

The switches.ELM Resource: A Compendium of Conditional Regulatory Interaction Interfaces

Roey, K. V., Dinkel, H., Weatheritt, R. J., Gibson, T. J., & Davey, N. E. (2013) · Science Signaling · doi:10.1126/scisignal.2003345 · Cited by 247

Physicochemical mechanisms of protein regulation by phosphorylation

Nishi, H., Shaytan, A. К., & Panchenko, A. R. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00270 · Cited by 223

Allostery without a conformational change? Revisiting the paradigm

Nussinov, R., & Tsai, C.-J. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.11.005 · Cited by 202

Post-translational regulation of inflammasomes

Yang, J., Liu, Z., & Xiao, T. S. (2016) · Cellular and Molecular Immunology · doi:10.1038/cmi.2016.29 · Cited by 211

Hot spots in protein–protein interfaces: Towards drug discovery

Cukuroglu, E., Engin, H. B., Gürsoy, A., & Keskin, Ö. (2014) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2014.06.003 · Cited by 184

Update: Post-translational protein modifications in plant metabolism

Friso, G., & van Wijk, K. J. (2015) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.01378 · Cited by 186

Allosteric Modulator Discovery: From Serendipity to Structure-Based Design

Lu, S., He, X., Ni, D., & Zhang, J. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01749 · Cited by 179

SERCA2a: a key protein in the Ca2+ cycle of the heart failure

Liu, Z., Ni, J., Lan, L., Michael, S., Rui, G., Bian, X., Liu, X., & Guanwei, F. (2019) · Heart Failure Reviews · doi:10.1007/s10741-019-09873-3 · Cited by 173

The Underappreciated Role of Allostery in the Cellular Network

Nussinov, R., Tsai, C., & Ma, B. (2013) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-083012-130257 · Cited by 176

Principles of Allosteric Interactions in Cell Signaling

Nussinov, R., Tsai, C.-J., & Liu, J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja510028c · Cited by 154

Harnessing Allostery: A Novel Approach to Drug Discovery

Lu, S., Li, S., & Zhang, J. (2014) · Medicinal Research Reviews · doi:10.1002/med.21317 · Cited by 148

Lysine Malonylation Is Elevated in Type 2 Diabetic Mouse Models and Enriched in Metabolic Associated Proteins

Du, Y., Cai, T., Li, T., Xue, P., Zhou, B., He, X., Peng, W., Liu, P., Yang, F., & Wei, T. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.041947 · Cited by 134

TagGraph reveals vast protein modification landscapes from large tandem mass spectrometry datasets

Devabhaktuni, A., Lin, S., Zhang, L., Swaminathan, K., Gonzalez, C. G., Olsson, N., Pearlman, S. M., Rawson, K., & Elias, J. E. (2019) · Nature Biotechnology · doi:10.1038/s41587-019-0067-5 · Cited by 134

Disordered Proteinaceous Machines

Fuxreiter, M., Tóth-Petróczy, Á., Kraut, D. A., Matouschek, A. T., Lim, R. Y. H., Xue, B., Kurgan, L., & Uversky, V. N. (2014) · Chemical Reviews · doi:10.1021/cr4007329 · Cited by 138

Multiple conformational selection and induced fit events take place in allosteric propagation

Nussinov, R., Ma, B., & Tsai, C. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.10.002 · Cited by 132

Review: Precision medicine and driver mutations: Computational methods, functional assays and conformational principles for interpreting cancer drivers

Nussinov, R., Jang, H., Tsai, C., & Cheng, F. (2019) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006658 · Cited by 134

Serine-129 phosphorylation of α-synuclein is an activity-dependent trigger for physiologic protein-protein interactions and synaptic function

(2023) · doi:10.1016/j.neuron.2023.11.020 · Cited by 127

Complex regulatory mechanisms mediated by the interplay of multiple post-translational modifications

Csizmók, V., & Forman-Kay, J. D. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.10.013 · Cited by 127

The Design of Covalent Allosteric Drugs

Nussinov, R., & Tsai, C.-J. (2015) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010814-124401 · Cited by 112

Protein conformational ensembles in function: roles and mechanisms

Nussinov, R., Liu, Y., Zhang, W., & Jang, H. (2023) · RSC Chemical Biology · doi:10.1039/d3cb00114h · Cited by 122

Protein flexibility in the light of structural alphabets

Craveur, P., Joseph, A. P., Esque, J., Narwani, T., Noël, F., Shinada, N. K., Goguet, M., Léonard, S., Poulain, P., Bertrand, O., et al. (2015) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2015.00020 · Cited by 109

PTMcode v2: a resource for functional associations of post-translational modifications within and between proteins

Mínguez, P., Letunić, I., Parca, L., García‐Alonso, L., Dopazo, J., Huerta‐Cepas, J., & Bork, P. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1081 · Cited by 106

Forcefield_PTM:Ab InitioCharge and AMBER Forcefield Parameters for Frequently Occurring Post-Translational Modifications

Khoury, G. A., Thompson, J. P., Smadbeck, J. B., Kieslich, C. A., & Floudas, C. A. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct400556v · Cited by 104

ASD v2.0: updated content and novel features focusing on allosteric regulation

Huang, Z., Mou, L., Shen, Q., Lu, S., Li, C., Liu, X., Wang, G., Li, S., Geng, L., Liu, Y., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1247 · Cited by 101

Protein ensembles link genotype to phenotype

Nussinov, R., Tsai, C., & Jang, H. (2019) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006648 · Cited by 102

Hepatic glucose sensing and integrative pathways in the liver

Oosterveer, M. H., & Schoonjans, K. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1505-z · Cited by 102

‘Latent drivers’ expand the cancer mutational landscape

Nussinov, R., & Tsai, C. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.01.004 · Cited by 88

The Structural Basis of ATP as an Allosteric Modulator

Lu, S., Huang, W., Wang, Q., Shen, Q., Li, S., Nussinov, R., & Zhang, J. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003831 · Cited by 88

Role of Computational Methods in Going beyond X-ray Crystallography to Explore Protein Structure and Dynamics

Srivastava, A., Nagai, T., Srivastava, A., Miyashita, O., & Tama, F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113401 · Cited by 87

Metabolic Modelling as a Framework for Metabolomics Data Integration and Analysis

Volkova, S., Matos, M. R. A., Mattanovich, M., & de Mas, I. M. (2020) · Metabolites · doi:10.3390/metabo10080303 · Cited by 77

An overview of recent advances in structural bioinformatics of protein–protein interactions and a guide to their principles

Sudha, G., Nussinov, R., & Srinivasan, N. (2014) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2014.07.004 · Cited by 70

The Mechanism of ATP-Dependent Allosteric Protection of Akt Kinase Phosphorylation

Lu, S., Deng, R., Jiang, H., Song, H., Li, S., Shen, Q., Huang, W., Nussinov, R., Yu, J., & Zhang, J. (2015) · Structure · doi:10.1016/j.str.2015.06.027 · Cited by 69

Allostery: Allosteric Cancer Drivers and Innovative Allosteric Drugs

Nussinov, R., Zhang, M., Maloney, R., Liu, Y., Tsai, C.-J., & Jang, H. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167569 · Cited by 66

Post-translational modifications as key regulators of bacterial metabolic fluxes

Pisithkul, T., Patel, N. M., & Amador‐Noguez, D. (2015) · Current Opinion in Microbiology · doi:10.1016/j.mib.2014.12.006 · Cited by 66

PRMT5-mediated arginine methylation stabilizes GPX4 to suppress ferroptosis in cancer

Fan, Y., Wang, Y., Dan, W., Zhang, Y., Nie, L., Ma, Z., Zhuang, Y., Liu, B., Li, M., Liu, T., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01610-3 · Cited by 62

Co-occurring protein phosphorylation are functionally associated

Li, Y., Zhou, X., Zhai, Z., & Li, T. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005502 · Cited by 59

Same but not alike: Structure, flexibility and energetics of domains in multi-domain proteins are influenced by the presence of other domains

Vishwanath, S., de Brevern, A. G., & Srinivasan, N. (2018) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006008 · Cited by 59

Drug design targeting active posttranslational modification protein isoforms

Meng, F., Liang, Z. T., Zhao, K., & Luo, C. (2020) · Medicinal Research Reviews · doi:10.1002/med.21774 · Cited by 56

Allosteric Conformational Barcodes Direct Signaling in the Cell

Nussinov, R., Ma, B., Tsai, C.-J., & Csermely, P. (2013) · Structure · doi:10.1016/j.str.2013.06.002 · Cited by 55

Precision medicine review: rare driver mutations and their biophysical classification

Nussinov, R., Jang, H., Tsai, C., & Cheng, F. (2019) · Biophysical Reviews · doi:10.1007/s12551-018-0496-2 · Cited by 56

PTM-SD: a database of structurally resolved and annotated posttranslational modifications in proteins

Craveur, P., Rebehmed, J., & de Brevern, A. G. (2014) · Database · doi:10.1093/database/bau041 · Cited by 54

Turnover of protein phosphorylation evolving under stabilizing selection

Landry, C. R., Freschi, L., Zarin, T., & Moses, A. M. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00245 · Cited by 51

Lessons from computer simulations of Ras proteins in solution and in membrane

Prakash, P., & Gorfe, A. A. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.07.024 · Cited by 49

Dissecting Structure-Encoded Determinants of Allosteric Cross-Talk between Post-Translational Modification Sites in the Hsp90 Chaperones

Stetz, G., Tse, A., & Verkhivker, G. M. (2018) · Scientific Reports · doi:10.1038/s41598-018-25329-4 · Cited by 50

Regulation of Lignin Biosynthesis by Post-translational Protein Modifications

Sulis, D. B., & Wang, J. P. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.00914 · Cited by 50

Protein function machinery: from basic structural units to modulation of activity

Berezovsky, I. N., Guarnera, E., Zheng, Z., Eisenhaber, B., & Eisenhaber, F. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.10.021 · Cited by 51

Posttranslational modifications and proteinopathies: how guardians of the proteome are defeated

Olzscha, H. (2019) · Biological Chemistry · doi:10.1515/hsz-2018-0458 · Cited by 51

The spatial structure of cell signaling systems

Nussinov, R. (2013) · Physical Biology · doi:10.1088/1478-3975/10/4/045004 · Cited by 49

Relaxation dispersion NMR spectroscopy for the study of protein allostery

Farber, P. J., & Mittermaier, A. (2015) · Biophysical Reviews · doi:10.1007/s12551-015-0166-6 · Cited by 48

Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma

Kulkarni, P., Leite, V. B. P., Roy, S., Bhattacharyya, S., Mohanty, A. R., Achuthan, S., Singh, D., Appadurai, R., Govindan Rangarajan, C., Weninger, K., et al. (2022) · Biophysics Reviews · doi:10.1063/5.0080512 · Cited by 49

Multisite Phosphorylation of S6K1 Directs a Kinase Phospho-code that Determines Substrate Selection

Arif, A., Jia, J., Willard, B. B., Li, X., & Fox, P. L. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.11.017 · Cited by 50

Why Are Some Driver Mutations Rare?

Nussinov, R., Tsai, C., & Jang, H. (2019) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2019.10.003 · Cited by 47

Functional Divergence and Evolutionary Turnover in Mammalian Phosphoproteomes

Freschi, L., Osseni, M. A., & Landry, C. R. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004062 · Cited by 44

Autoinhibition in Ras effectors Raf, PI3Kα, and RASSF5: a comprehensive review underscoring the challenges in pharmacological intervention

Nussinov, R., Zhang, M., Tsai, C., Liao, T.-J., Fushman, D., & Jang, H. (2018) · Biophysical Reviews · doi:10.1007/s12551-018-0461-0 · Cited by 47

Exogenous H2S reduces the acetylation levels of mitochondrial respiratory enzymes via regulating the NAD+-SIRT3 pathway in cardiac tissues of db/db mice

Sun, Y., Teng, Z., Sun, X., Zhang, L., Chen, J., Wang, B., Lu, F., Liu, N., Yu, M., Peng, S., et al. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00326.2018 · Cited by 46

Temperature-induced changes in the wheat phosphoproteome reveal temperature-regulated interconversion of phosphoforms

Vu, L. D., Zhu, T., Verstraeten, I., van de Cotte, B., IWGSC, Gevaert, K., & Smet, I. D. (2018) · Journal of Experimental Botany · doi:10.1093/jxb/ery204 · Cited by 46

The free energy landscape in translational science: how can somatic mutations result in constitutive oncogenic activation?

Tsai, C., & Nussinov, R. (2014) · Physical Chemistry Chemical Physics · doi:10.1039/c3cp54253j · Cited by 47

Structural Systems Pharmacology: The Role of 3D Structures in Next-Generation Drug Development

Duran‐Frigola, M., Mosca, R., & Aloy, P. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.03.004 · Cited by 44

A broad view of scaffolding suggests that scaffolding proteins can actively control regulation and signaling of multienzyme complexes through allostery

Nussinov, R., Ma, B., & Tsai, C. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.12.014 · Cited by 45

Engineered control of enzyme structural dynamics and function

Boehr, D. D., D’Amico, R. N., & O’Rourke, K. F. (2018) · Protein Science · doi:10.1002/pro.3379 · Cited by 45

Oligomerization and nanocluster organization render specificity

Nussinov, R., Jang, H., & Tsai, C. (2014) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12124 · Cited by 44

From glycophenotyping by (plant) lectin histochemistry to defining functionality of glycans by pairing with endogenous lectins

Kaltner, H., Caballero, G. G., Ludwig, A., Manning, J. C., & Gabius, H. (2018) · Histochemistry and Cell Biology · doi:10.1007/s00418-018-1676-7 · Cited by 44

Identification of Enriched PTM Crosstalk Motifs from Large-Scale Experimental Data Sets

Peng, M., Scholten, A., Heck, A. J. R., & van Breukelen, B. (2013) · Journal of Proteome Research · doi:10.1021/pr4005579 · Cited by 42

A Reduction of Transcriptional Regulation in Aquatic Oligotrophic Microorganisms Enhances Fitness in Nutrient-Poor Environments

Noell, S. E., Hellweger, F. L., Temperton, B., & Giovannoni, S. J. (2023) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00124-22 · Cited by 40

Systematic Characterization and Prediction of Post-Translational Modification Cross-Talk *

Huang, Y., Xu, B., Zhou, X., Li, Y., Lü, M., Jiang, R., & Li, T. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.037994 · Cited by 40

How to gather useful and valuable information from protein binding measurements using Langmuir lipid monolayers

Boisselier, É., Demers, É., Cantin, L., & Salesse, C. (2017) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2017.03.004 · Cited by 40

Characterization of intact sialylated glycopeptides and phosphorylated glycopeptides from IMAC enriched samples by EThcD fragmentation: Toward combining phosphoproteomics and glycoproteomics

Glover, M. S., Yu, Q., Chen, Z., Shi, X., Kent, K. C., & Li, L. (2017) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2017.09.002 · Cited by 41

Small Molecules Govern Thiol Redox Switches

Knuesting, J., & Scheibe, R. (2018) · Trends in Plant Science · doi:10.1016/j.tplants.2018.06.007 · Cited by 40

Allosteric perspective on the mutability and druggability of the SARS-CoV-2 Spike protein

Tan, Z. W., Tee, W.-V., Samsudin, F., Guarnera, E., Bond, P. J., & Berezovsky, I. N. (2022) · Structure · doi:10.1016/j.str.2021.12.011 · Cited by 38

A methylated lysine is a switch point for conformational communication in the chaperone Hsp90

Rehn, A., Lawatscheck, J., Jokisch, M.-L., Mader, S. L., Luo, Q., Tippel, F., Blank, B., Richter, K., Lang, K., Kaila, V. R. I., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15048-8 · Cited by 38

Allosteric Control of a Plant Receptor Kinase through S-Glutathionylation

Moffett, A. S., Bender, K. W., Huber, S. C., & Shukla, D. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.08.059 · Cited by 37

Dynamic multiprotein assemblies shape the spatial structure of cell signaling

Nussinov, R., & Jang, H. (2014) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2014.07.002 · Cited by 38

PRMT5-Mediated Methylation of NF-κB p65 at Arg174 Is Required for Endothelial CXCL11 Gene Induction in Response to TNF-α and IFN-γ Costimulation

Harris, D. P., Chandrasekharan, U. M., Bandyopadhyay, S., Willard, B. B., & DiCorleto, P. E. (2016) · PLoS ONE · doi:10.1371/journal.pone.0148905 · Cited by 38

PINE: An Automation Tool to Extract and Visualize Protein-Centric Functional Networks

Sundararaman, N., Go, J. L., Robinson, A., Mato, J. M., Lu, S. C.-L., Eyk, J. E. V., & Venkatraman, V. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00032 · Cited by 33

The role of allostery in the ubiquitin–proteasome system

Liu, J., & Nussinov, R. (2012) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2012.742856 · Cited by 34

Engineering an Allosteric Control of Protein Function

Vishweshwaraiah, Y. L., Chen, J., & Dokholyan, N. V. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c11640 · Cited by 33

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

Ruegenberg, S., Mayr, F. A. M. C., Atanassov, I., Baumann, U., & Denzel, M. S. (2021) · Nature Communications · doi:10.1038/s41467-021-22320-y · Cited by 35

ISG15 promotes esophageal squamous cell carcinoma tumorigenesis via c-MET/Fyn/β-catenin signaling pathway

Yuan, H., Zhou, W., Yang, Y., Xue, L., Liu, L., & Song, Y. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.03.017 · Cited by 34

Selective Modulation of Dynamic Protein Complexes

Garlick, J. M., & Mapp, A. K. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.07.019 · Cited by 39

PRMT5 K240lac confers ferroptosis resistance via ALKBH5/SLC7A11 axis in colorectal cancer

Qu, S., Feng, B., Xing, M., Qiu, Y.-Y., Ma, L., Yang, Z., Ji, Y., Huang, F., Wang, Y., Zhou, J., et al. (2025) · Oncogene · doi:10.1038/s41388-025-03457-2 · Cited by 35

Allosteric inhibitors of the STAT3 signaling pathway

Qin, J., Shen, X., Zhang, J., & Jia, D. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112122 · Cited by 33

Regulation of the EphA2 receptor intracellular region by phosphomimetic negative charges in the kinase-SAM linker

Lechtenberg, B. C., Gehring, M. P., Light, T. P., Horne, C. R., Matsumoto, M. W., Hristova, K. A., & Pasquale, E. B. (2021) · Nature Communications · doi:10.1038/s41467-021-27343-z · Cited by 33

Global Profiling of 2-Hydroxyisobutyrylome in Common Wheat

Zhang, N., Zhang, L., Li, L., Geng, J., Zhao, L., Ren, Y. N., Dong, Z., & Chen, F. (2021) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2020.06.008 · Cited by 31

Trypanosoma brucei histones are heavily modified with combinatorial post-translational modifications and mark Pol II transcription start regions with hyperacetylated H2A

Maree, J. P., Tvardovskiy, A., Ravnsborg, T., Jensen, O. N., Rudenko, G., & Patterton, H. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac759 · Cited by 29

Cell phenotypes can be predicted from propensities of protein conformations

Nussinov, R., Liu, Y., Zhang, W., & Jang, H. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102722 · Cited by 30

TRIM-NHL as RNA Binding Ubiquitin E3 Ligase (RBUL): Implication in development and disease pathogenesis

Goyani, S., Roy, M., & Singh, R. K. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.166066 · Cited by 29

Mechanism of activation and the rewired network: New drug design concepts

Nussinov, R., Zhang, M., Maloney, R., Tsai, C., Yavuz, B. R., Tunçbağ, N., & Jang, H. (2021) · Medicinal Research Reviews · doi:10.1002/med.21863 · Cited by 30

The value of protein allostery in rational anticancer drug design: an update

Nussinov, R., & Jang, H. (2024) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2024.2384467 · Cited by 29

Investigation of the impact of PTMs on the protein backbone conformation

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From The Editors

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