Protein–protein interaction networks: how can a hub protein bind so many different partners?

Emergence of Scaling in Random Networks

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Finishing the euchromatic sequence of the human genome

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Functional organization of the yeast proteome by systematic analysis of protein complexes

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A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae

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Network pharmacology: the next paradigm in drug discovery

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Global landscape of protein complexes in the yeast Saccharomyces cerevisiae

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A "Silent" Polymorphism in the MDR 1 Gene Changes Substrate Specificity

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Evidence for dynamically organized modularity in the yeast protein–protein interaction network

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Flexible nets: The roles of intrinsic disorder in protein interaction networks

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Recognition Dynamics Up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution

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Structure and dynamics of molecular networks: A novel paradigm of drug discovery

Csermely, P., Korcsmáros, T., Kiss, H., London, G., & Nussinov, R. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.01.016 · Cited by 911

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

iLoc-Hum: using the accumulation-label scale to predict subcellular locations of human proteins with both single and multiple sites

Chou, K., Wu, Z., & Xiao, X. (2011) · Molecular BioSystems · doi:10.1039/c1mb05420a · Cited by 334

Nonspecific Binding—Fundamental Concepts and Consequences for Biosensing Applications

Frutiger, A., Tanno, A., Hwu, S., Tiefenauer, R. F., Vörös, J., & Nakatsuka, N. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00044 · Cited by 287

The Ribosome as a Hub for Protein Quality Control

Pechmann, S., Willmund, F., & Frydman, J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.020 · Cited by 278

Protein binding specificity versus promiscuity

Schreiber, G., & Keating, A. E. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.10.002 · Cited by 268

Allosteric post-translational modification codes

Nussinov, R., Tsai, C.-J., Xin, F., & Radivojac, P. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.07.001 · Cited by 211

Identifying protein complexes and functional modules--from static PPI networks to dynamic PPI networks

Chen, B., Fan, W. Y., Liu, J., & Wu, F. (2013) · Briefings in Bioinformatics · doi:10.1093/bib/bbt039 · Cited by 179

Expanding the proteome: disordered and alternatively folded proteins

Dyson, H. J. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583511000060 · Cited by 181

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

Hub Promiscuity in Protein-Protein Interaction Networks

Patil, A., Kinoshita, K., & Nakamura, H. (2010) · International Journal of Molecular Sciences · doi:10.3390/ijms11041930 · Cited by 162

Rational Design of Peptide-Based Inhibitors Disrupting Protein-Protein Interactions

Wang, X., Ni, D., Liu, Y., & Lu, S. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.682675 · Cited by 162

Cross talk between stimulated NF-κB and the tumor suppressor p53

Schneider, G., Henrich, A., Greiner, G., Wolf, V, Lovas, A., Wieczorek, M., Wagner, T., Reichardt, S., von Werder, A., Schmid, R. M., et al. (2010) · Oncogene · doi:10.1038/onc.2010.46 · Cited by 149

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

New Force Field on Modeling Intrinsically Disordered Proteins

Wang, W., Ye, W., Jiang, C., Luo, R., & Chen, H. (2014) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12314 · Cited by 127

Quantitative proteomics in lung cancer

Cheung, C. H. Y., & Juan, H. (2017) · Journal of Biomedical Science · doi:10.1186/s12929-017-0343-y · Cited by 117

Targeting Intrinsically Disordered Transcription Factors: Changing the Paradigm

Tsafou, K., Tiwari, P. B., Forman-Kay, J. D., Metallo, S. J., & Toretsky, J. A. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.04.008 · Cited by 113

Topology of molecular interaction networks

Winterbach, W., Mieghem, P. V., Reinders, M. J. T., Wang, H., & de Ridder, D. (2013) · BMC Systems Biology · doi:10.1186/1752-0509-7-90 · Cited by 109

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

Hub Protein Controversy: Taking a Closer Look at Plant Stress Response Hubs

Vandereyken, K., Leene, J. V., Coninck, B. D., & Cammue, B. P. A. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.00694 · Cited by 99

PTEN proteoforms in biology and disease

Malaney, P., Uversky, V. N., & Davé, V. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2500-6 · Cited by 85

ff14IDPs force field improving the conformation sampling of intrinsically disordered proteins

Song, D., Wang, W., Ye, W., Ji, D., Luo, R., & Chen, H. (2016) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12832 · Cited by 85

Test and Evaluation of ff99IDPs Force Field for Intrinsically Disordered Proteins

Ye, W., Ji, D., Wang, W., Luo, R., & Chen, H. (2015) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00043 · Cited by 80

Local and global anatomy of antibody‐protein antigen recognition

Wang, M., Zhu, D. S., Zhu, J., Nussinov, R., & Ma, B. (2017) · Journal of Molecular Recognition · doi:10.1002/jmr.2693 · Cited by 76

Antigen binding allosterically promotes Fc receptor recognition

Zhao, J., Nussinov, R., & Ma, B. (2018) · mAbs · doi:10.1080/19420862.2018.1522178 · Cited by 79

Ferroptosis – An iron- and disorder-dependent programmed cell death

Djulbegovic, M. B., & Uversky, V. N. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.05.221 · Cited by 79

Non-Redundant Unique Interface Structures as Templates for Modeling Protein Interactions

Cukuroglu, E., Gürsoy, A., Nussinov, R., & Keskin, Ö. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086738 · Cited by 76

Disparate Degrees of Hypervariable Loop Flexibility Control T-Cell Receptor Cross-Reactivity, Specificity, and Binding Mechanism

Scott, D. R., Borbulevych, O. Y., Piepenbrink, K. H., Corcelli, S. A., & Baker, B. M. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.10.006 · Cited by 77

A Novel Co-immunoprecipitation Protocol Based on Protoplast Transient Gene Expression for Studying Protein–protein Interactions in Rice

Yang, J., Fu, J. X., Li, J., Cheng, X. L., Feng, L., Dong, J. F., Liu, Z. L., & Zhuang, C. X. (2013) · Plant Molecular Biology Reporter · doi:10.1007/s11105-013-0633-9 · Cited by 76

One hundred thousand mouse clicks down the road: selected online resources supporting drug discovery collected over a decade

Villoutreix, B. O., Lagorce, D., Labbé, C. M., Spérandio, O., & Miteva, M. A. (2013) · Drug Discovery Today · doi:10.1016/j.drudis.2013.06.013 · Cited by 75

MultitaskProtDB: a database of multitasking proteins

Hernández, S., Ferragut, G., Amela, I., Perez-Pons, J. A., Piñol, J., Mozo-Villarias, Á., Cedano, J. A., & Querol, E. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1153 · Cited by 72

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

Scale invariance in natural and artificial collective systems: a review

Khaluf, Y., Ferrante, E., Simoens, P., & Huepe, C. (2017) · Journal of The Royal Society Interface · doi:10.1098/rsif.2017.0662 · Cited by 73

Pathogen mimicry of host protein-protein interfaces modulates immunity

Guven‐Maiorov, E., Tsai, C., & Nussinov, R. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.06.004 · Cited by 72

AptaNet as a deep learning approach for aptamer–protein interaction prediction

Emami, N., & Ferdousi, R. (2021) · Scientific Reports · doi:10.1038/s41598-021-85629-0 · Cited by 68

Constructing structural networks of signaling pathways on the proteome scale

Kuzu, G., Keskin, Ö., Gürsoy, A., & Nussinov, R. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.04.004 · Cited by 64

Established and Emerging Trends in Computational Drug Discovery in the Structural Genomics Era

Taboureau, O., Baell, J. B., Fernández‐Recio, J., & Villoutreix, B. O. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.12.007 · Cited by 63

Heat Shock Partially Dissociates the Overlapping Modules of the Yeast Protein-Protein Interaction Network: A Systems Level Model of Adaptation

Mihalik, Á., & Csermely, P. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002187 · Cited by 61

Cell growth and cell cycle in Saccharomyces cerevisiae: Basic regulatory design and protein–protein interaction network

Alberghina, L., Mavelli, G., Drovandi, G., Palumbo, P. J., Pessina, S., Tripodi, F., Coccetti, P., & Vanoni, M. (2011) · Biotechnology Advances · doi:10.1016/j.biotechadv.2011.07.010 · Cited by 64

Domain distribution and intrinsic disorder in hubs in the human protein–protein interaction network

Patil, A., Kinoshita, K., & Nakamura, H. (2010) · Protein Science · doi:10.1002/pro.425 · Cited by 62

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

How yeast can be used as a genetic platform to explore virus–host interactions: from ‘omics’ to functional studies

Nagy, P. D., Pogany, J., & Lin, J.-Y. (2014) · Trends in Microbiology · doi:10.1016/j.tim.2014.02.003 · Cited by 55

The spatial structure of cell signaling systems

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

Multispecific Recognition: Mechanism, Evolution, and Design

Erijman, A., Aizner, Y., & Shifman, J. M. (2011) · Biochemistry · doi:10.1021/bi101563v · Cited by 47

DNA-binding protects p53 from interactions with cofactors involved in transcription-independent functions

Lambrughi, M., GIOIA, L. D., Gervasio, F. L., Lindorff‐Larsen, K., Nussinov, R., Urani, C., Bruschi, M., & Papaleo, E. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw770 · Cited by 42

Analysis of Hot Region Organization in Hub Proteins

Cukuroglu, E., Gürsoy, A., & Keskin, Ö. (2010) · Annals of Biomedical Engineering · doi:10.1007/s10439-010-0048-9 · Cited by 41

Specialized Dynamical Properties of Promiscuous Residues Revealed by Simulated Conformational Ensembles

Fornili, A., Pandini, A., Lu, H., & Fraternali, F. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct400486p · Cited by 38

Computational Alanine Scanning Mutagenesis—An Improved Methodological Approach for Protein–DNA Complexes

Ramos, R. M., & Moreira, I. S. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct400387r · Cited by 39

Cause-effect relationships in medicine: a protein network perspective

Fliri, A. F. J., Loging, W., & Volkmann, R. A. (2010) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.07.005 · Cited by 38

Connectedness of PPI network neighborhoods identifies regulatory hub proteins

Fox, A. D., Hescott, B. J., Blumer, A. C., & Slonim, D. K. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr099 · Cited by 37

Dissecting allosteric effects of activator–coactivator complexes using a covalent small molecule ligand

Wang, N., Lodge, J. M., Fierke, C. A., & Mapp, A. K. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1406033111 · Cited by 36

Structural Instability Tuning as a Regulatory Mechanism in Protein-Protein Interactions

Chen, L., Balabanidou, V., Remeta, D. P., Minetti, C. A. S. A., Portaliou, A. G., Economou, A., & Kalodimos, C. G. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.022 · Cited by 36

Multiple-Localization and Hub Proteins

Ota, M., Gonja, H., Koike, R., & Fukuchi, S. (2016) · PLoS ONE · doi:10.1371/journal.pone.0156455 · Cited by 32

Systems Biology and Bioinformatics approach to Identify blood based signatures molecules and drug targets of patient with COVID-19

Hasan, M. I., Rahman, M. H., Islam, M. B., Islam, M. Z., Hossain, M. A., & Moni, M. A. (2021) · Informatics in Medicine Unlocked · doi:10.1016/j.imu.2021.100840 · Cited by 36

Interplay between Chaperones and Protein Disorder Promotes the Evolution of Protein Networks

Pechmann, S., & Frydman, J. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003674 · Cited by 41

Construction and Application of a Protein Interaction Map for White Spot Syndrome Virus (WSSV)

Sangsuriya, P., Huang, J., Chu, Y., Phiwsaiya, K., Leekitcharoenphon, P., Meemetta, W., Senapin, S., Huang, W., Withyachumnarnkul, B., Flegel, T. W., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.029199 · Cited by 36

TRAF3 signaling: Competitive binding and evolvability of adaptive viral molecular mimicry

Guven‐Maiorov, E., Keskin, Ö., Gürsoy, A., Waes, C. V., Chen, Z., Tsai, C., & Nussinov, R. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.05.021 · Cited by 34

GIT2 Acts as a Systems-Level Coordinator of Neurometabolic Activity and Pathophysiological Aging

Martin, B., Chadwick, W., Janssens, J., Premont, R. T., Schmalzigaug, R., Becker, K. G., Lehrmann, E., Wood, W. H., Zhang, Y., Siddiqui, S., et al. (2016) · Frontiers in Endocrinology · doi:10.3389/fendo.2015.00191 · Cited by 34

Binding interface prediction by combining protein-protein docking results

Hwang, H., Vreven, T., & Weng, Z. (2013) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24354 · Cited by 32

Discovery of multiple interacting partners of gankyrin, a proteasomal chaperone and an oncoprotein—Evidence for a common hot spot site at the interface and its functional relevance

Nanaware, P. P., Ramteke, M. P., Somavarapu, A. K., & Venkatraman, P. (2013) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24494 · Cited by 31

Cooperative binding of transcription factors in the human genome

Nie, Y., Shu, C., & Sun, X. S. (2020) · Genomics · doi:10.1016/j.ygeno.2020.06.029 · Cited by 30

AlphaScreen selectivity assay for β-catenin/B-cell lymphoma 9 inhibitors

Zhang, M., Wisniewski, J. A., & Ji, H. (2014) · Analytical Biochemistry · doi:10.1016/j.ab.2014.09.018 · Cited by 28

Why Does Binding of Proteins to DNA or Proteins to Proteins Not Necessarily Spell Function?

Ma, B., Tsai, C., Pan, Y., & Nussinov, R. (2010) · ACS Chemical Biology · doi:10.1021/cb900293a · Cited by 28

Tombusvirus-yeast interactions identify conserved cell-intrinsic viral restriction factors

Sasvári, Z., González, P. A., & Nagy, P. D. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00383 · Cited by 27

OsHrd3 is necessary for maintaining the quality of endoplasmic reticulum-derived protein bodies in rice endosperm

Ohta, M., & Takaiwa, F. (2015) · Journal of Experimental Botany · doi:10.1093/jxb/erv229 · Cited by 25

Kinase signaling cascades: an updated mechanistic landscape

Nussinov, R., Regev, C., & Jang, H. (2025) · Chemical Science · doi:10.1039/d5sc04657b · Cited by 28

Spatial range, temporal span, and promiscuity of CLE-RLK signaling

Narasimhan, M., & Simon, R. G. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.906087 · Cited by 24

Biochemical Reduction of the Topology of the Diverse WDR76 Protein Interactome

Dayebgadoh, G., Sardiu, M. E., Florens, L. A., & Washburn, M. P. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00373 · Cited by 22

Interaction of myelin basic protein with cytoskeletal and signaling proteins in cultured primary oligodendrocytes and N19 oligodendroglial cells

Boggs, J. M., Homchaudhuri, L., Ranagaraj, G., Liu, Y., Smith, G. S. T., & Harauz, G. (2014) · BMC Research Notes · doi:10.1186/1756-0500-7-387 · Cited by 22

Predicting the Binding Patterns of Hub Proteins: A Study Using Yeast Protein Interaction Networks

Andorf, C. M., Honavar, V., & Sen, T. Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056833 · Cited by 24

Enriching Traditional Protein-protein Interaction Networks with Alternative Conformations of Proteins

Halakou, F., Sen-Kilic, E., Cukuroglu, E., Keskin, Ö., & Gürsoy, A. (2017) · Scientific Reports · doi:10.1038/s41598-017-07351-0 · Cited by 21

Surveying the Side-Chain Network Approach to Protein Structure and Dynamics: The SARS-CoV-2 Spike Protein as an Illustrative Case

Halder, A., Anto, A., Subramanyan, V., Bhattacharyya, M., Vishveshwara, S., & Vishveshwara, S. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.596945 · Cited by 21

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

Do Moonlighting Proteins Belong to the Intrinsically Disordered Protein Class?

Hernández, S. (2012) · Journal of Proteomics & Bioinformatics · doi:10.4172/jpb.1000247 · Cited by 20

Community Structure Detection for Overlapping Modules through Mathematical Programming in Protein Interaction Networks

Bennett, L., Kittas, A., Liu, S., Papageorgiou, L. G., & Tsoka, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0112821 · Cited by 21

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

Developments in integrative modeling with dynamical interfaces

Ozdemir, E. S., Nussinov, R., Gursoy, A., & Keskin, O. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.10.007 · Cited by 17

Hubs and Bottlenecks in Protein-Protein Interaction Networks

Nithya, C., Kiran, M., & Nagarajaram, H. A. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3461-5_13 · Cited by 18

Mutations in Protein-Binding Hot-Spots on the Hub Protein Smad3 Differentially Affect Its Protein Interactions and Smad3-Regulated Gene Expression

Schiro, M. M., Stauber, S. E., Peterson, T. L., Krueger, C., Darnell, S. J., Satyshur, K. A., Drinkwater, N. R., Newton, M. A., & Hoffmann, F. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025021 · Cited by 16

Network Re-Wiring During Allostery and Protein-Protein Interactions: A Graph Spectral Approach

Gadiyaram, V., Dighe, A., Ghosh, S., & Vishveshwara, S. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-1154-8_7 · Cited by 14

Scale-Free Behaviour of Amino Acid Pair Interactions in Folded Proteins

Petersen, S. B., Neves‐Petersen, M. T., Henriksen, S. B., Mortensen, R. J., & Geertz‐Hansen, H. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041322 · Cited by 14

Human genes with a greater number of transcript variants tend to show biological features of housekeeping and essential genes

Ryu, J. Y., Kim, H. U., & Lee, S. Y. (2015) · Molecular BioSystems · doi:10.1039/c5mb00322a · Cited by 13

Effect of Alternative Splicing on the Degree Centrality of Nodes in Protein–Protein Interaction Networks of Homo sapiens

Sinha, A., & Nagarajaram, H. A. (2013) · Journal of Proteome Research · doi:10.1021/pr4000812 · Cited by 13

Alterations in Immune-Related Defensin Alpha 4 (DEFA4) Gene Expression in Health and Disease

Basingab, F. S., Alsaiary, A. H., Almontashri, S., Alrofaidi, A., Alharbi, M. G., Azhari, S. A., Algothmi, K. M., & Alhazmi, S. (2022) · International Journal of Inflammation · doi:10.1155/2022/9099136 · Cited by 12

Dipeptide analysis of p53 mutations and evolution of p53 family proteins

Huang, Q., Yu, L., Levine, A. J., Nussinov, R., & Ma, B. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.04.002 · Cited by 11

Allosteric Modulation of Intrinsically Disordered Proteins

Rehman, A. U., Rahman, M. U., Arshad, T., & Chen, H. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-8719-7_14 · Cited by 12

A structural network associated with the kallikrein-kinin and renin-angiotensin systems

Stoka, V., & Türk, V. (2010) · Biological Chemistry · doi:10.1515/bc.2010.046 · Cited by 12

Comparative Analysis of Techniques Oriented on the Recognition of Ligand Binding Area in Proteins

Alejster, P., Banach, M., Jurkowski, W., Marchewka, D., & Roterman‐Konieczna, I. (2012) · Focus on structural biology · doi:10.1007/978-94-007-5285-6_4 · Cited by 11

Toponome imaging system: multiplex biomarkers in oncology

Evans, R. G., Naidu, B. V., Rajpoot, N., Epstein, D. B. A., & Khan, M. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.10.003 · Cited by 11

Tutorial on biological networks

Vital-Lopez, F. G., Memišević, V., & Dutta, B. (2012) · Wiley Interdisciplinary Reviews Data Mining and Knowledge Discovery · doi:10.1002/widm.1061 · Cited by 11

Programmed Trade-offs in Protein Folding Networks

Pechmann, S. (2020) · Structure · doi:10.1016/j.str.2020.09.009 · Cited by 11

A Selection Fit Mechanism in BMP Receptor IA as a Possible Source for BMP Ligand-Receptor Promiscuity

Harth, S., Kotzsch, A., Hu, J., Sebald, W., & Mueller, T. D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013049 · Cited by 11

Promiscuous domains: facilitating stability of the yeast protein–protein interaction network

Pang, E., Tan, T., & Lin, K. (2011) · Molecular BioSystems · doi:10.1039/c1mb05364g · Cited by 9

Identification of hub proteins from sequence

Latha, A. B., Nair, A. S., Sivasankaran, A., & Dhar, P. K. (2011) · Bioinformation · doi:10.6026/97320630007163 · Cited by 8

Differential Network Analysis via the Lasso Penalized D-Trace LossPreprint

Yuan, H., Xi, R., Chen, C., & Deng, M. (2015) · arXiv (Cornell University) · doi:10.48550/arxiv.1511.09188 · Cited by 8

DNA-Bound p53-DNA-Binding Domain Interconverts between Multiple Conformations: Implications for Partner Protein Recognition

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Elliptic geometry-based kernel matrix for improved biological sequence classification

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Viral species, viral genomes and HIV vaccine design: is the rational design of biological complexity a utopia?

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Deciphering novel common gene signatures for rheumatoid arthritis and systemic lupus erythematosus by integrative analysis of transcriptomic profiles

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Protein folding by ‘levels of separation’: A hypothesis

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Hub Promiscuity in Protein-Protein Interaction Networks

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Structural properties of hub proteins

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Similar Binding Sites and Different Partners: Implications to Shared Proteins in Cellular Pathways

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The Role Of Dynamics On Binding Specificity And Promiscuity

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What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae?

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