Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

Collective dynamics of ‘small-world’ networks

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Computational Prediction of Protein Complexes from Protein Interaction Networks

Srihari, S., Yong, C. H., & Wong, L. (2017) · doi:10.1145/3064650 · Cited by 17

Actinous enigma or enigmatic actin

Povarova, O. I., Uversky, V. N., Kuznetsova, I. М., & Константинович, Т. К. (2014) · Intrinsically Disordered Proteins · doi:10.4161/idp.34500 · Cited by 17

Prevalence of intrinsic disorder in the hepatitis C virus ARFP/Core+1/S protein

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NOT THAT RIGID MIDGETS AND NOT SO FLEXIBLE GIANTS: ON THE ABUNDANCE AND ROLES OF INTRINSIC DISORDER IN SHORT AND LONG PROTEINS

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Alzheimer’s-disease-associated conformation of intrinsically disordered tau protein studied by intrinsically disordered protein liquid-phase competitive enzyme-linked immunosorbent assay

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Functional dissection of an intrinsically disordered protein: Understanding the roles of different domains of Knr4 protein in protein–protein interactions

Dagkessamanskaia, A., Durand, F., Uversky, V. N., Binda, M., Lopez, F., Azzouzi, K. E., François, J., & Martin‐Yken, H. (2010) · Protein Science · doi:10.1002/pro.418 · Cited by 17

Structural Disorder within the Nucleoprotein and Phosphoprotein from Measles, Nipah, and Hendra Viruses

Habchi, J., Mamelli, L., & Longhi, S. (2011) · doi:10.1002/9781118135570.ch3 · Cited by 17

Visualizing RNA Structures by SAXS-Driven MD Simulations

He, W., Henning‐Knechtel, A., & Kırmızıaltın, S. (2022) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2022.781949 · Cited by 16

Prediction of protein-protein interaction sites in intrinsically disordered proteins

Chen, R., Li, X., Yang, Y., Song, X., Wang, C., & Qiao, D. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.985022 · Cited by 15

Analyzing a potential drug target N-myristoyltransferase of Plasmodium falciparum through in silico approaches

Murty, U., Banerjee, A. K., & Arora, N. (2012) · Journal of Global Infectious Diseases · doi:10.4103/0974-777x.93761 · Cited by 16

An Overview of the Importance of Conformational Flexibility in Gene Regulation by the Transcription Factors

Khan, S. H., & Kumar, R. (2009) · Journal of Biophysics · doi:10.1155/2009/210485 · Cited by 15

Hydrophobic Moments, Shape, and Packing in Disordered Proteins

Rawat, N., & Biswas, P. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp3016529 · Cited by 16

The effect of phosphorylation on the salt-tolerance-related functions of the soybean protein PM18, a member of the group-3 LEA protein family

Liu, Y., Yang, M., Cheng, H., Sun, N., Liu, S., Li, S., Wang, Y., Zheng, Y., & Uversky, V. N. (2017) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2017.08.020 · Cited by 16

Ubiquitin-independent protein degradation in proteasomes

Бунеева, О. А., & Medvedev, A. E. (2018) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20186402134 · Cited by 17

The Role of HSP90 Chaperones in Stability and Plasticity of Ontogenesis of Plants under Normal and Stressful Conditions (Arabidopsis thaliana)

Kozeko, L. (2019) · Cytology and Genetics · doi:10.3103/s0095452719020063 · Cited by 16

Physical Chemistry of the Protein Backbone: Enabling the Mechanisms of Intrinsic Protein Disorder

Drake, J. A., & Pettitt, B. M. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c02489 · Cited by 16

Multifunctionality and intrinsic disorder of royal jelly proteome

Uversky, V., Albar, A., Khan, R. H., & Redwan, E. (2021) · Proteomics · doi:10.1002/pmic.202000237 · Cited by 15

Characterization of Weak Protein Domain Structure by Spin-Label Distance Distributions

Ritsch, I., Hofer, L. E., Lehmann, E., Emmanouilidis, L., Yulikov, M., Allain, F. H. ‐., & Jeschke, G. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.636599 · Cited by 16

Insights into the evolutionary forces that shape the codon usage in the viral genome segments encoding intrinsically disordered protein regions

Kumar, N., Kaushik, R., Tennakoon, C., Uversky, V. N., Longhi, S., Zhang, K. Y. J., & Bhatia, S. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab145 · Cited by 16

Conformation of the EPEC Tir Protein in Solution: Investigating the Impact of Serine Phosphorylation at Positions 434/463

Race, P. R., Solovyova, A. S., & Banfield, M. J. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.101766 · Cited by 16

3.9 Intrinsically Disordered Proteins

Uversky, V. N., & Dunker, A. K. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-374920-8.00312-x · Cited by 17

Solvent interaction analysis of intrinsically disordered proteins in aqueous two-phase systems

Breydo, L., Mikheeva, L. M., Madeira, P. P., Zaslavsky, B. Y., & Uversky, V. N. (2013) · Molecular BioSystems · doi:10.1039/c3mb70329k · Cited by 15

Soft disorder modulates the assembly path of protein complexes

Seoane, B., & Carbone, A. (2022) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1010713 · Cited by 15

The Disordered Amino-Terminus of SIMPL Interacts with Members of the 70-kDa Heat-Shock Protein Family

Breese, E. H., Uversky, V. N., Georgiadis, M. M., & Harrington, M. A. (2006) · DNA and Cell Biology · doi:10.1089/dna.2006.25.704 · Cited by 15

Investigating the structural stability of the Tup1‐interaction domain of Ssn6: Evidence for a conformational change on the complex

Palaiomylitou, M., Tartas, A., Vlachakis, D., Tzamarias, D., & Vlassi, M. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21489 · Cited by 15

Allosteric Communication between cAMP Binding Sites in the RI Subunit of Protein Kinase A Revealed by NMR

Byeon, I. L., Dao, K. K., Jung, J., Keen, T. J., Leiros, I., Døskeland, S. O., Martı́nez, A., & Gronenborn, A. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.106666 · Cited by 15

Chicken cathelicidins as potent intrinsically disordered biocides with antimicrobial activity against infectious pathogens

yacoub, H. A., Elazzazy, A. M., Mahmoud, M. M., Baeshen, M. N., Almaghrabi, O. A., Alkarim, S., Ahmed, E. S., Almehdar, H. A., & Uversky, V. N. (2016) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2016.06.012 · Cited by 15

Dynamics of the BH3-Only Protein Binding Interface of Bcl-xL

Liu, X., Beugelsdijk, A., & Chen, J. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.07.043 · Cited by 16

Chaotic aging: intrinsically disordered proteins in aging-related processes

Manyilov, V. D., Ilyinsky, N. S., Nesterov, S. V., Saqr, B. M. G. A., Dayhoff, G. W., Zinovev, E. V., Matrenok, S. S., Fonin, A. V., Kuznetsova, I. M., Turoverov, K. K., et al. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04897-3 · Cited by 14

CoMemMoRFPred: Sequence-based Prediction of MemMoRFs by Combining Predictors of Intrinsic Disorder, MoRFs and Disordered Lipid-binding Regions

Basu, S., Hegedűs, T., & Kurgan, L. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168272 · Cited by 14

Order and Disorder in the Replicative Complex of Paramyxoviruses

Erales, J., Blocquel, D., Habchi, J., Beltrandi, M., Gruet, A., Dosnon, M., Bignon, C., & Longhi, S. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-20164-1_12 · Cited by 14

Ordered Disorder of the Astrocytic Dystrophin-Associated Protein Complex in the Norm and Pathology

Na, I., Redmon, D., Kopa, M., Qin, Y., Xue, B., & Uversky, V. N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073476 · Cited by 15

Prediction of Disordered Regions and Their Roles in the Anti-Pathogenic and Immunomodulatory Functions of Butyrophilins

Redwan, E. M. M. M., Al-Hejin, A. M., Almehdar, H. A., Elsaway, A., & Uversky, V. N. (2018) · Molecules · doi:10.3390/molecules23020328 · Cited by 16

A comparative proteomic approach to analyse structure, function and evolution of rice chitinases: a step towards increasing plant fungal resistance

Sarma, K., Dehury, B., Sahu, J., Sarmah, R., Sahoo, S., Sahu, M., Sen, P., Modi, M. K., & Barooah, M. (2012) · Journal of Molecular Modeling · doi:10.1007/s00894-012-1470-8 · Cited by 14

Dendritic peptide-conjugated polymeric nanovectors for non-toxic delivery of plasmid DNA and enhanced non-viral transfection of immune cells

Yi, S., Kim, S., Vincent, M. P., Yuk, S. A., Bobbala, S. K. R., Du, F., & Scott, E. A. (2022) · iScience · doi:10.1016/j.isci.2022.104555 · Cited by 13

Antibody Responses to a Novel Plasmodium falciparum Merozoite Surface Protein Vaccine Correlate with Protection against Experimental Malaria Infection in Aotus Monkeys

Cavanagh, D. R., Kocken, C. H. M., White, J. H., Cowan, G. J. M., Samuel, K., Dubbeld, M. A., der Wel, A. V.-V., Thomas, A. W., McBride, J. S., & Arnot, D. E. (2014) · PLoS ONE · doi:10.1371/journal.pone.0083704 · Cited by 14

Integration of Nanometer-Range Label-to-Label Distances and Their Distributions into Modelling Approaches

Jeschke, G. (2022) · Biomolecules · doi:10.3390/biom12101369 · Cited by 13

Protein Misfolding in Lipid-Mimetic Environments

Uversky, V. N. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-17344-3_2 · Cited by 13

Solution structure and dynamics of the chimeric SH3 domains, SHH- and SHA-“Bergeracs”

Kutyshenko, V. P., Prokhorov, D. A., Timchenko, M., Kudrevatykh, Y., Gushchina, L. V., Khristoforov, V. S., Filimonov, V. V., & Uversky, V. N. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.08.021 · Cited by 13

Knr4 N‐terminal domain controls its localization and function during sexual differentiation and vegetative growth

Dagkessamanskaia, A., Azzouzi, K. E., Kikuchi, Y., Timmers, T., Ohya, Y., François, J., & Martin‐Yken, H. (2010) · Yeast · doi:10.1002/yea.1804 · Cited by 13

14-3-3 protein and ATRAP bind to the soluble class IIB phosphatidylinositol transfer protein RdgBβ at distinct sites

Cockcroft, S., & Garner, K. (2012) · Biochemical Society Transactions · doi:10.1042/bst20110770 · Cited by 13

Abundance and functional roles of intrinsic disorder in the antimicrobial peptides of the NK-lysin family

yacoub, H. A., Almaghrabi, O. A., Ahmed, E. S., & Uversky, V. N. (2016) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2016.1164077 · Cited by 13

Intrinsically disordered caldesmon binds calmodulin via the “buttons on a string” mechanism

Permyakov, S. E., Permyakov, E. A., & Uversky, V. N. (2015) · PeerJ · doi:10.7717/peerj.1265 · Cited by 13

Environmental Pressure May Change the Composition Protein Disorder in Prokaryotes

Vicedo, E., Schlessinger, A., & Rost, B. (2015) · PLoS ONE · doi:10.1371/journal.pone.0133990 · Cited by 13

Defining Structural Domains of an Intrinsically Disordered Protein: Sic1, the Cyclin-Dependent Kinase Inhibitor of Saccharomyces cerevisiae

Brocca, S., Testa, L., Šamalíková, M., Grandori, R., & Lotti, M. (2010) · Molecular Biotechnology · doi:10.1007/s12033-010-9309-y · Cited by 13

HIV-1 mutants expressing B cell clonogenic matrix protein p17 variants are increasing their prevalence worldwide

Caccuri, F., Messali, S., Zani, A., Campisi, G., Giovanetti, M., Zanussi, S., Vaccher, E., Fabris, S., Bugatti, A., Focà, E., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2122050119 · Cited by 12

A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR

Goda, N., Shimizu, K., Kuwahara, Y., Tenno, T., Noguchi, T., Ikegami, T., Ota, M., & Hiroaki, H. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160715743 · Cited by 12

Fluorescence-based techniques for the detection of the oligomeric status of proteins: implication in amyloidogenic diseases

Mirdha, L., & Chakraborty, H. (2021) · European Biophysics Journal · doi:10.1007/s00249-021-01505-9 · Cited by 12

Heme‐dependent recognition of 5‐aminolevulinate synthase by the human mitochondrial molecular chaperone ClpX

Nomura, K., Kitagawa, Y., Aihara, M., Ohki, Y., Furuyama, K., & Hirokawa, T. (2021) · FEBS Letters · doi:10.1002/1873-3468.14214 · Cited by 12

The protein disorder cycle

Uversky, V. N. (2021) · Biophysical Reviews · doi:10.1007/s12551-021-00853-2 · Cited by 10

Co-opting disorder into order: Intrinsically disordered proteins and the early evolution of complex multicellularity

Kulkarni, P., Behal, A., Mohanty, A. R., Salgia, R., Nedelcu, A. M., & Uversky, V. N. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.12.182 · Cited by 12

Lighting up Nobel Prize-winning studies with protein intrinsic disorder

Piersimoni, L., el Malek, M. A., Bhatia, T., Bender, J., Brankatschk, C., Sánchez, J. C., Dayhoff, G. W., Ianni, A. D., Parra, J. O. F., Martínez, D. G., et al. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04468-y · Cited by 11

Molecular Recognition by the EWS Transcriptional Activation Domain

Lee, K. A. W. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-0659-4_7 · Cited by 12

Solvation Thermodynamics of Oligoglycine with Respect to Chain Length and Flexibility

Drake, J. A., Harris, R. C., & Pettitt, B. M. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.07.013 · Cited by 12

Investigating the Formation of a Repulsive Hydrogel of a Cationic 16mer Peptide at Low Ionic Strength in Water by Vibrational Spectroscopy and Rheology

DiGuiseppi, D. M., Kraus, J., Toal, S. E., Alvarez, N. J., & Schweitzer‐Stenner, R. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b07673 · Cited by 12

The PPII-to-α-helix transition of poly-l-lysine in methanol/water solvent mixtures accompanied by fibrillar self-aggregation: An influence of fluphenazine molecules

Cieślik-Boczula, K. (2017) · Biophysical Chemistry · doi:10.1016/j.bpc.2017.05.012 · Cited by 12

InSiDDe: A Server for Designing Artificial Disordered Proteins

Schramm, A., Lieutaud, P., Gianni, S., Longhi, S., & Bignon, C. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms19010091 · Cited by 12

Protein Regulation by Intrinsically Disordered Regions: A Role for Subdomains in the IDR of the HIV‐1 Rev Protein

Faust, O., Grunhaus, D., Tepper, O., Yavin, E., & Friedler, A. (2018) · ChemBioChem · doi:10.1002/cbic.201800192 · Cited by 12

Assessing Allostery in Intrinsically Disordered Proteins With Ensemble Allosteric Model

Li, J., & Hilser, V. J. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.09.004 · Cited by 11

Turncoat Polypeptides: We Adapt to Our Environment

Zamora‐Carreras, H., Maestro, B., Sanz, J. M., & Jiménez, M. A. (2019) · ChemBioChem · doi:10.1002/cbic.201900446 · Cited by 12

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

Discovery of 4-(3,5-dimethoxy-4-(((4-methoxyphenethyl)amino)methyl)phenoxy)-N-phenylaniline as a novel c-myc inhibitor against colorectal cancer in vitro and in vivo

Yang, J., Cao, C.-G., Luo, D., Lan, S., Luo, M., Shan, H., Ma, X., Liu, Y., Yu, S., Zhong, X.-X., et al. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112336 · Cited by 12

Disorder in the lifetime of a protein

Uversky, V. N. (2013) · Intrinsically Disordered Proteins · doi:10.4161/idp.26782 · Cited by 11

Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential

Sarma, K., Sen, P., Barooah, M., Choudhury, M. D., Roychoudhury, S., & Modi, M. K. (2014) · BioMed Research International · doi:10.1155/2014/583606 · Cited by 12

Intrinsic disorder in biomarkers of insulin resistance, hypoadiponectinemia, and endothelial dysfunction among the type 2 diabetic patients

Al-Jiffri, O. H., Al-Sharif, F. M., Jiffri, E. H., & Uversky, V. N. (2016) · Intrinsically Disordered Proteins · doi:10.1080/21690707.2016.1171278 · Cited by 11

DISOselect: Disorder predictor selection at the protein level

Katuwawala, A., Oldfield, C. J., & Kurgan, L. (2019) · Protein Science · doi:10.1002/pro.3756 · Cited by 11

The Phosphofurin Acidic Cluster Sorting Protein 2 (PACS-2) E209K Mutation Responsible for PACS-2 Syndrome Increases Susceptibility to Apoptosis

Zang, R. X., Mumby, M. J., & Dikeakos, J. D. (2022) · ACS Omega · doi:10.1021/acsomega.2c04014 · Cited by 11

Looking at the carcinogenicity of human insulin analogues via the intrinsic disorder prism

Redwan, E. M. M. M., Linjawi, M. H., & Uversky, V. N. (2016) · Scientific Reports · doi:10.1038/srep23320 · Cited by 11

Intrinsic Disorder and Semi-disorder Prediction by SPINE-D

Zhang, T., Faraggi, E., Li, Z., & Zhou, Y. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6406-2_12 · Cited by 11

Dynamics of Dystrophin’s Actin-Binding Domain

Fealey, M. E., Horn, B. T., Coffman, C., Miller, R. C., Lin, A. Y., Thompson, A. R., Schramel, J., Groth, E., Hinderliter, A. K., Cembran, A., et al. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.05.039 · Cited by 11

CATS: A Tool for Clustering the Ensemble of Intrinsically Disordered Peptides on a Flat Energy Landscape

Ezerski, J. C., & Cheung, M. S. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b08852 · Cited by 11

The Methods and Tools for Intrinsic Disorder Prediction and their Application to Systems Medicine

Kurgan, L., Li, M., & Li, Y. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.11320-0 · Cited by 11

Presence and structure‐activity relationship of intrinsically disordered regions across mucins

Carmicheal, J., Atri, P., Sharma, S., Sushil Kumar, K., Venkata, R. C., Kulkarni, P., Salgia, R., Ghersi, D., Kaur, S., & Batra, S. K. (2020) · The FASEB Journal · doi:10.1096/fj.201901898rr · Cited by 11

A novel mode of interaction between intrinsically disordered proteins

Hibino, E., & Hoshino, M. (2020) · Biophysics and Physicobiology · doi:10.2142/biophysico.bsj-2020012 · Cited by 11

Unraveling the nature of the segmentation clock: Intrinsic disorder of clock proteins and their interaction map

Roy, S., Schnell, S. D., & Predrag Radivojac, A. (2006) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2006.04.005 · Cited by 11

Intrinsically disordered tau protein in Alzheimer's tangles: a coincidence or a rule?

Škrabana, R., Skrabanova, M., Csokova, N. T., Sevcik, J., & Novák, M. (2006) · Bratislavské lekárske listy/Bratislava medical journal · doi:10.1007/bf03656853 · Cited by 11

Predicting Disordered Regions in Proteins Based on Decision Trees of Reduced Amino Acid Composition

Han, P., Zhang, X., Norton, R. S., & Feng, Z. (2006) · Journal of Computational Biology · doi:10.1089/cmb.2006.13.1723 · Cited by 11

Why are we Interested in the Unfolded Peptides and Proteins?

Uversky, V. N., & Dunker, A. K. (2012) · Wiley eBooks · doi:10.1002/9781118183373.ch1 · Cited by 11

Biological Regulation via Ankyrin Repeat Folding

Barrick, D. (2009) · ACS Chemical Biology · doi:10.1021/cb900003f · Cited by 11

Detecting Disordered Regions in Proteins by Limited Proteolysis

Fontana, A., de Laureto, P. P., Spolaore, B., Frare, E., & Zambonin, M. (2010) · doi:10.1002/9780470602614.ch20 · Cited by 11

Evolution of Intrinsic Disorder in Protein Loops

Mughal, F., & Caetano-Anollés, G. (2023) · Life · doi:10.3390/life13102055 · Cited by 7

Network-informed discovery of multidrug combinations for ERα+/HER2-/PI3Kα-mutant breast cancer

Hany, D., Zoetemelk, M., Bhattacharya, K., Nowak-Sliwinska, P. M., & Picard, D. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04730-x · Cited by 9

Current research on viral proteins that interact with fibrillarin

Decle-Carrasco, S., Rodríguez-Piña, A. L., Rodríguez‐Zapata, L. C., & Castaño, E. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08343-2 · Cited by 13

Chaperoned amyloid proteins for immune manipulation: α‐Synuclein/Hsp70 shifts immunity toward a modulatory phenotype

Labrador‐Garrido, A., Cejudo‐Guillén, M., Klippstein, R., Genst, E. D., Tomás‐Gallardo, L., Leal‐Lasarte, M., Villadiego, J., Toledo‐Aral, J. J., Dobson, C. M., Pozo, D., et al. (2014) · Immunity Inflammation and Disease · doi:10.1002/iid3.39 · Cited by 10

Detection of HIV-1 Matrix Protein p17 Quasispecies Variants in Plasma of Chronic HIV-1–Infected Patients by Ultra-Deep Pyrosequencing

Giombini, E., Dolcetti, R., Caccuri, F., Selleri, M., Rozera, G., Abbate, I., Bartolini, B., Martorelli, D., Faè, D. A., Fiorentini, S., et al. (2014) · JAIDS Journal of Acquired Immune Deficiency Syndromes · doi:10.1097/qai.0000000000000164 · Cited by 10

Yersinia pestis Caf1 Protein: Effect of Sequence Polymorphism on Intrinsic Disorder Propensity, Serological Cross-Reactivity and Cross-Protectivity of Isoforms

Kopylov, P. K., Platonov, М. E., Ablamunits, V. G., Kombarova, T. I., Иванов, С. А., Kadnikova, L. A., Somov, A. N., Dentovskaya, S. V., Uversky, V. N., & Anisimov, A. P. (2016) · PLoS ONE · doi:10.1371/journal.pone.0162308 · Cited by 10

Flexibility of the Sec13/31 cage is influenced by the Sec31 C-terminal disordered domain

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