[97] Carab Amhed M., Skaanning L.K., Jussupow A., Newcombe E.A., Kragelund B.B., Camilloni C., Langkilde A.E., and Lindorff-Larsen K. (submitted) Refinement of α-synuclein ensembles against SAXS data: Comparison of force fields and methods. [bioRxiv]plumID:21.003

[96] Löhr T., Kohlhoff K., Heller G.T., Camilloni C., and Vendruscolo M. (2021) A kinetic ensemble of the Alzheimer’s Aβ peptide. NAT. COMPUT. SCI. 1: 71-78 [bioRxiv]

[95] Mangiagalli M., Lapi M., Maione S., Orlando M., Brocca S., Pesce A., Barbiroli A., Camilloni C., Pucciarelli S., Lotti M., and Nardini M. (2021) The co-existence of cold activity and thermal stability in an Antarctic GH42 β-galactosidase relies on its hexametric quaternary arrangement. FEBS J. 288: 546-565 [PDB: 6Y2K]


[94] Heller G.T., Aprile F.A., Michaels T.C.T., Limbocker R., Perni M., Ruggeri F.S., Mannini B., Löhr T., Bonomi M., Camilloni C., De Simone A., Felli I.C., Pierattelli R., Knowles T.P.J., Dobson C.M., and Vendruscolo M. (2020) Small molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer’s disease. SCI. ADV. 6: eabb5924 [bioRxiv]plumID:20.014

[93] Karlsson E., Paissoni C., Erkelens A.M., Tehranizadeh Z.A., Sorgenfrei F.A., Andersson E., Ye W., Camilloni C, and Jemth P. (2020) Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins. J. BIOL. CHEM. 295: 17698-17712 [bioRxiv]plumID:20.021

[92] Nardone V., Chaves-Sanjuan A., Lapi M., Airoldi C., Saponaro A., Pasqualato S., Dolfini D., Camilloni C., Bernardini A., Gnesutta N., Mantovani R., and Nardini M. (2020) Structural Basis of Inhibition of the Pioneer Transcription Factor NF-Y by Suramin. CELLS 9: 2370 [PDB: 7AH8]

[91] Jussupow A., Messias A.C., Stehle R., Geerlof A., Solbak S.M.Ø., Paissoni C., Bach A., Sattler M., and Camilloni C. (2020) The dynamics of linear polyubiquitin. SCI. ADV. 6: eabc3786 [bioRxiv] plumID:20.009

[90] Sala B.M., Le Marchand T., Pintacuda G., Camilloni C., Natalello A., and Ricagno S. (2020) Conformational stability and dynamics in crystals recapitulate protein behaviour in solution. BIOPHYS. J. 119: 978-988 [bioRxiv]plumID:20.001

[89] Paissoni C., Jussupow A., and Camilloni C. (2020) Determination of Protein Structural Ensembles by Hybrid-Resolution SAXS Restrained Molecular Dynamics. J. CHEM. THEORY COMPUT. 16: 2825-2834 [ChemRxiv]plumID:19.057

[88] Niu Z., Prade E., Malideli E., Hille K., Jussupow A., Mideksa Y.G., Yan L., Qian C., Fleisch M., Messias A.C, Sarkar R., Sattler M., Lamb D.C, Feige M.J, Camilloni C., Kapurniotu A., and Reif B. (2020) Structural insight into IAPP-derived amyloid inhibitors and their mechanism of action. ANGEW. CHEM. 59: 5771-5781

[87] Achour A., Broggini L., Han X., Sun R., Santambrogio C., Buratto J., Visentin C., Barbiroli A., De Luca C.M.G., Sormanni P., Moda F., De Simone A., Sandalova T., Grandori R., Camilloni C., and Ricagno S. (2020) Biochemical and biophysical comparison of human and mouse beta‐2 microglobulin reveals the molecular determinants of low amyloid propensity. FEBS J. 287: 546-560 plumID:19.038 [PDB: 6I8C]


[86] Swuec P., Chaves-Sanjuan A., Camilloni C., Vanoni M.A., and Bolognesi M. (2019) Cryo-EM structures of Azospirillum brasilense glutamate synthase in its oligomeric assemblies. J. MOL. BIOL. 431: 4523-4526

[85a] Bonomi M., and Camilloni C. (2019) Biomolecular Simulations. METHODS MOL. BIOL. 2022

[85b] Löhr T., Camilloni C., Bonomi M., and Vendruscolo M. (2019) A practical guide to the simultaneous determination of protein structure and dynamics using metainference.  In: Bonomi M., Camilloni C. (eds) Biomolecular Simulations. METHODS MOL. BIOL. 2022: 313-340 [arXiv]

[84] The PLUMED consortium. (2019) Promoting transparency and reproducibility in enhanced molecular simulations. NAT. METHODS 16: 670–673

[83] Paissoni C., Jussupow A., and Camilloni C. (2019) Martini bead form factors for nucleic-acids and their application in the refinement of protein/nucleic-acid complexes against SAXS data. J. APPL. CRYST. 52: 394-402 [bioRxiv]plumID:19.012

[82] Swuec P., Lavatelli F., Tasaki M., Paissoni C., Rognoni P., Maritan M., Brambilla F., Milani P., Mauri P., Camilloni C., Palladini G., Merlini G., Ricagno S., and Bolognesi M. (2019) Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain (AL) amyloidosis patient. NAT. COMMUN. 10: 1269 [bioRxiv]

[81] da Silva Neto A.M., Silva S.R., Vendruscolo M., Camilloni C., and Montalvo R.W. (2019) A superposition free method for protein conformational ensemble analyses and local clustering based on a differential geometry representation of backbone. PROTEINS 87: 302-312

[80] Karlsson E., Andersson E., Dogan J., Gianni S., Jemth P., and Camilloni C. (2019) A structurally heterogeneous transition state underlies coupled binding and folding of disordered proteins. J. BIOL. CHEM. 294: 1230-1239


[79] Troilo F., Bonetti D., Camilloni C., Toto A., Longhi S., Brunori M., and Gianni S. (2018) The Folding Mechanism of the SH3 Domain from Grb2. J. PHYS. CHEM. B 122: 11166-11173

[78] Weber B., Hora M., Kazman P., Göbl C., Camilloni C., Reif B., and Buchner J. (2018) The antibody light chain linker regulates domain orientation and amyloidogenicity. J. MOL. BIOL. 430: 4925-4940 plumID:19.010

[77] Possenti A., Vendruscolo M., Camilloni C., and Tiana G. (2018)  A method for partitioning the information contained in a protein sequence between its structure and function. PROTEINS 86: 956-964 [arXiv]

[76] Camilloni C. and Pietrucci F. (2018) Advanced simulation techniques for the thermodynamic and kinetic characterization of biological systems. ADV. PHYS. X 3, 1477531

[75] Waudby C.A., Wlodarski T., Karyadi M., Cassaignau A.M.E., Chan S.H.S., Wentink A.S., Schmidt-Engler J.M., Camilloni C., Vendruscolo M., Cabrita L.D., and Christodoulou J. (2018) Systematic mapping of free energy landscapes of a growing filamin domain during biosynthesis. PROC. NATL. ACAD. SCI. U.S.A. 115: 9744-9749 [bioRxiv]

[74] Tomba G., Camilloni C., and Vendruscolo M. (2018) Determination of the conformational states of strychnine using NMR residual dipolar couplings in a tensor-free approach. METHODS 148: 4-8

[73] Papaleo E., Camilloni C., Teilum K., Vendruscolo M., and Lindorff-Larsen K. (2018) Molecular dynamics ensemble refinement of the heterogeneous native state of NCBD using chemical shifts and NOEs. PEERJ 6: e5125 [bioRxiv]

[72] Kooshapur H., Choudhury N.R., Simon B., Mühlbauer M., Jussupow A., Fernandez N., Jones A.N., Dallmann A., Gabel F., Camilloni C., Michlewski G., Caceres J.F., and Sattler M. (2018) Structural basis for terminal loop recognition and stimulation of pri-miRNA-18a processing by hnRNP A1. NAT. COMMUN. 9: 2479 [bioRxiv]

[71] Capelli R., Tiana G., and Camilloni C. (2018) An implementation of the maximum-caliber principle by replica-averaged time-resolved restrained simulations. J. CHEM. PHYS. 148: 184114 [arXiv]

[70] Le Marchand T., De Rosa M., Salvi N., Sala B.M., Andreas L., Sormanni P., Barbiroli A., Porcari R., Mota C.S., De Sanctis D., Bolognesi M., Emsley L., Bellotti V., Blackledge M., Camilloni C., Pintacuda G., and Ricagno S. (2018) Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity. NAT. COMMUN. 9: 1658

[69] Piovesan D., Tabaro F., Paladin L., Necci M., Mičetić I., Camilloni C., Davey N., Dosztány Z., Meszaros B., Monzon A.M., Parisi G., Schad E., Sormanni P., Tompa P., Vendruscolo M., Vranken W.F. and Tosatto S.C.E. (2018) MobiDB 3.0: More annotations for intrinsic disorder, conformational diversity and interactions in proteins. NUCLEIC ACIDS RES. 46: D471–D476


[68] Bonomi M., and Camilloni C. (2017) Integrative Structural and Dynamical Biology with PLUMED-ISDB. BIOINFORMATICS 24: 3999-4000

[67] Rodriguez Camargo D.C., Korshavn K.J., Jussupow A., Raltchev K., Goricanec D., Fleisch M., Sarkar R., Xue K., Aichler M., Mettenleiter G., Walch A.K., Camilloni C., Hagn F., Reif B., and Ramamoorthy A. (2017) Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate. eLIFE 6: e31226

[66] Popolo L., Degani G., Camilloni C., and Fonzi W.A. (2017) The PHR Family: The Role of Extracellular Transglycosylases in Shaping Candida albicans Cells. J. FUNGI 3, 59

[65] Heller G.T., Aprile F.A., Bonomi M., Camilloni C., De Simone A., and Vendruscolo M. (2017) Sequence Specificity in the Entropy-Driven Binding of a Small Molecule and a Disordered Peptide. J. MOL. BIOL. 429: 2772-2779plumID:19.005

[64] Löhr T., Jussupow A., and Camilloni C. (2017) Metadynamic Metainference: convergence towards force field independent structural ensembles of a disordered peptide. J. CHEM. PHYS. 146: 165102plumID:19.025

[63] Kukic P., Pustovalova Y., Camilloni C., Gianni S., Korzhnev D., and Vendruscolo M. (2017) Structural characterization of the early events in the nucleation-condensation mechanism in a protein folding process. J. AM. CHEM. SOC. 139: 6899-6910

[62] Hultqvist G., Åberg E., Camilloni C., Sundell G.N., Andersson E., Dogan J., Chi C.N., Vendruscolo M., and Jemth P. (2017) Emergence and evolution of an interaction between intrinsically disordered proteins. eLIFE 6: e16059

[61] Sormanni P., Piovesan D., Heller G.T., Bonomi M., Kukic P., Camilloni C., Fuxreiter M., Dosztanyi Z., Pappu R., Babu M.M., Longhi S., Tompa P., Dunker A.K., Uversky V.N., Tosatto S.C.E., and Vendruscolo M. (2017) Simultaneous quantification of order and disorder in proteins. NAT. CHEM. BIOL. 13: 339-342

[60] Holliday M.J., Camilloni C., Armstrong G.S., Vendruscolo M., and Eisenmesser E.Z. (2017) Networks of Dynamic Allostery Regulate Enzyme Function. STRUCTURE 25: 276-286

[59] Borkar A.N., Vallurupalli P., Camilloni C., Kay L.E., and Vendruscolo M. (2017) Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop. PHYS. CHEM. CHEM. PHYS. 19: 2797-2804

[58] Bonomi M., Heller G.T., Camilloni C., and Vendruscolo M. (2017) Principles of protein structural ensemble determination. CURR. OPIN. STRUCT. BIOL. 42: 106-116


[57] Meloni R., Camilloni C., and Tiana G. (2016) Properties of low-dimensional collective variables in the molecular dynamics of biopolymers. PHYS. REV. E 94: 052406

[56] Bonomi M., Camilloni C., and Vendruscolo M. (2016) Metadynamic metainference: Enhanced sampling of the metainference ensemble using metadynamics. SCI. REP. 6: 31232

[55] Camilloni C., Bonetti D., Morrone A., Giri R., Dobson C.M., Brunori M., Gianni S., and Vendruscolo M.(2016) Towards a structural biology of the hydrophobic effect in protein folding. SCI. REP. 6, 28285

[54] Borkar A.N., Bardaro M.F., Camilloni C., Aprile F.A., Varani G. and Vendruscolo M. (2016) Structure of a low-population binding intermediate in protein-RNA recognition. PROC. NATL. ACAD. SCI. U.S.A. 113: 7171-7176

[53] Camilloni C., Sala B.M., Sormanni P., Porcari R., Corazza A., De Rosa M., Zanini S., Barbiroli A., Esposito G., Bolognesi M., Bellotti V., Vendruscolo M. and Ricagno S. (2016) Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability. SCI. REP. 6: 2555

[52] Bonetti D., Camilloni C., Visconti L., Longhi S., Brunori M., Vendruscolo M., and Gianni S. (2016) Identification and structural characterization of an intermediate in the folding of the measles virus X domain. J. BIOL. CHEM. 291: 10886-10892

[51] Deckert A., Waudby C.A., Wlodarski T., Wentink A.S., Wang X., Kirkpatrick J., Paton J.F.S., Camilloni C., Kukic P., Dobson C.M., Vendruscolo M., Cabrita L.D., Christodoulou J. (2016) Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor. PROC. NATL. ACAD. SCI. U.S.A. 113: 5012-5017

[50] Toto A., Camilloni C., Giri R., Brunori M., Vendruscolo M. and Gianni S. (2016) Molecular recognition by templated folding of an intrinsically disordered protein. SCI. REP. 6: 21994

[49] Cabrita L.D., Cassaignau A.M.E., Launay H.M.M., Waudby C.A., Camilloni C., Roberston A.L., Wang X., Wlodarski T., Wentik A.S., Woolhead C.A., Vendruscolo M., Dobson C.M., and Christodoulou J. (2016) A structural ensemble of a ribosome-nascent chain complex during in vivo co-translational protein folding. NAT. STRUCT. MOL. BIOL. 23: 278–285

[48] Bonomi M., Camilloni C., Cavalli A., Vendruscolo M. (2016) Metainference: A Bayesian inference method for heterogeneous systems. SCI. ADV. 2: e1501177 plumID:19.004

[47] Kukic P., Lundström P., Camilloni C., Evenäs J., Akke M., Vendruscolo M. (2016) Structural insights into the calcium-mediated allosteric transition in the C-terminal domain of calmodulin from NMR measurements. BIOCHEMISTRY 55: 19-28


[46] Camilloni C., Vendruscolo M. (2015) Using pseudocontact shifts and residual dipolar couplings as exact NMR restraints for the determination of protein structural ensembles. BIOCHEMISTRY 54: 7470–7476

[45] Kukic P., Kannan A., Dijkstra M.J.J., Abeln S., Camilloni C., Vendruscolo M. (2015) Mapping the protein fold universe using the CamTube force field in molecular dynamics simulations. PLOS COMP. BIOL. 11: e1004435

[44] Granata D., Baftizadeh F., Habchi J., Galvagnion C., De Simone A., Camilloni C., Laio A., Vendruscolo M. (2015) The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments. SCI. REP. 5: 15449

[43] Brewer K.D., Bacaj T., Cavalli A., Camilloni C., Swarbrick J.D., Liu J., Zhou A., Zhou P., Barlow N., Xu J., Seven A.B., Prinslow E.A., Voleti R., Haussinger D., Bonvin A.M.J.J., Tomchick D.R., Vendruscolo M., Graham B., Sudhof T.C., Rizo J. (2015) Dynamic Binding Mode of a Synaptotagmin-1-SNARE Complex in Solution. NAT. STRUCT. MOL. BIOL. 22: 555–564

[42] Camilloni C., Vendruscolo M. (2015) Reply to Comment on “A Tensor-Free Method for the Structural and Dynamical refinement of Proteins using Residual Dipolar Coupling. J. PHYS. CHEM. B 19: 8225-8226

[41] Holliday M.J., Camilloni C., Armstrong G.S., Isern N.G., Zhang F., Vendruscolo M., Eisenmesser E.Z. (2015) Structure and dynamics of GeoCyp: a thermophilic cyclophilin with a novel substrate binding mechanism that functions efficiently at low temperatures. BIOCHEMISTRY 54: 3207-3217

[40] Kukic P., Leung H.T.A., Bemporad F., Aprile F.A., Kumita J.R., De Simone A., Camilloni C., Vendruscolo M. (2015) Structure and Dynamics of the Integrin LFA-1 I-Domain in the Inactive State Underlie its Inside-Out/Outside-In Signaling and Allosteric Mechanisms. STRUCTURE 23: 745-753

[39] Sormanni P., Camilloni C., Fariselli P., Vendruscolo M. (2015) The s2D method: Simultaneous sequence-based prediction of secondary structure populations and intrinsic disorder of proteins. J. MOL. BIOL. 427: 982-996

[38] Porcari R., Proukakis C., Waudby C.A., Bolognesi B., Mangione P.P., Paton J.F.S., Mullin S., Cabrita L.D., Penco A., Relini A., Verona G., Vendruscolo M. Stoppini M., Tartaglia G.G., Camilloni C., Christodoulou J., Schapira A.H.V., Bellotti V. (2015) The H50Q mutation induces a tenfold decrease in the solubility of alpha-synuclein. J. BIOL. CHEM. 290: 2395-2404

[37] Camilloni C., Vendruscolo M. (2015) A Tensor-Free Method for the Structural and Dynamical Refinement of Proteins using Residual Dipolar Couplings. J. PHYS. CHEM. B 119: 653-661


[36] Leung H.T.A., Kukic P., Camilloni C., Bemporad F., De Simone A., Aprile F.A., Kumita J.R., Vendruscolo M. (2014) NMR characterisation of the conformational fluctuations of the human lymphocyte function associated antigen-1 I domain. PROTEIN SCIENCE 23: 1596-1606

[35] Gianni S., Camilloni C., Giri R., Toto A., Bonetti D., Morrone A., Sormanni P., Brunori M., Vendruscolo M. (2014) Understanding the frustration arising from the competition between function, misfolding and aggregation in a globular protein. PROC. NATL. ACAD. SCI. U.S.A. 111: 14141-14146

[34] Camilloni C., Sahakyan A.B., Holliday M., Isern N.G., Zhan F., Eisenmesser E.Z., Vendruscolo M. (2014) Cyclophilin A catalyses proline isomerization by an electrostatic handle mechanism. PROC. NATL. ACAD. SCI. U.S.A. 111: 10203–10208

[33] Camilloni C., Vendruscolo M. (2014) Statistical mechanics of the denatured state of a protein using replica-averaged metadynamics. J. AM. CHEM. SOC. 136: 8982-8991

[32] Blombach F., Launay H., Snijders A.P.L., Zorraquino V., Wu H., De Koning B., Brouns S.J.J., Ettema T., Camilloni C., Cavalli A., Vendruscolo M., Dickman M.J., Cabrita L.D., La Teana A., Benelli D., Londei P., Christodoulou J., Van Der Oost J. (2014) Archaeal MBF1 binds to 30S and 70S ribosomes via its helix-turn-helix domain. BIOCHEM. J. 462: 373-384

[31] Krieger J.R., Fusco G., Lewitzky M., Simister P.C., Marchant J., Camilloni C., Feller S.M., De Simone A. (2014) Conformational Recognition of an Intrinsically Disordered Protein. BIOPHYS. J. 106: 1771-1779

[30] Fu B., Sahakyan A.B., Camilloni C., Tartaglia G.G., Paci E., Caflisch A., Vendruscolo M., Cavalli A. (2014) ALMOST: An all atom molecular simulation toolkit for protein structure determination. J. COMPUT. CHEM. 35: 1101-1105

[29] Kukic P., Camilloni C., Cavalli A., Vendruscolo M. (2014) Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts. J. MOL. BIOL. 426: 1826-1838

[28] Kendrick A.A., Holliday M.J., Isern N.G., Zhang F., Camilloni C., Huyhn C., Vendruscolo M., Armstrong G., Eisenmesser E.Z. (2014) The dynamics of interleukin-8 and its interaction with human CXC receptor I peptide. PROTEIN SCIENCE 23: 464-480

[27] Kannan A., Camilloni C., Sahakyan A.B., Cavalli A., Vendruscolo M. (2014) A conformational ensemble derived using NMR methyl chemical shifts reveals a mechanical clamping transition that gates the binding of the HU protein to DNA. J. AM. CHEM. SOC. 136: 2204–2207

[26] Meloni R., Camilloni C., Tiana G. (2014) Sampling the denatured state of polypeptides in water, urea and guanidine chloride to strict equilibrium conditions with the help of massively parallel computers. J. CHEM. THEORY COMPUT. 10: 846-854

[25] Montalvao R., Camilloni C., De Simone A., Vendruscolo M. (2014) New opportunities for tensor-free calculations of residual dipolar couplings for the study of protein dynamics. J. BIOMOL. NMR 4: 233-238

[24] Tribello G.A., Bonomi M., Branduardi D., Camilloni C., Bussi G. (2014) PLUMED2: New feathers for an old bird. COMP. PHYS. COMM. 185: 604-613


[23] Camilloni C., Cavalli A., Vendruscolo M. (2013) Replica Averaged Metadynamics. J. CHEM. THEORY COMPUT. 9: 5610-5617

[22] Camilloni C., Vendruscolo M. (2013) A Relationship Between the Aggregation Rates of α-Synuclein Variants and the β-Sheet Populations in Their Monomeric Forms. J. PHYS. CHEM. B 117: 10737–10741

[21] Waudby C.A., Camilloni C., Fitzpatrick A.W.P., Cabrita L., Dobson C.M., Vendruscolo M., Christodoulou J. (2013) In-cell NMR characterization of the secondary structure populations of a disordered conformation of alpha-synuclein within E. coli cells. PLOS ONE 8: e72286

[20] Granata D., Camilloni C., Vendruscolo M., Laio A. (2013) Characterization of the free energy landscapes of proteins by NMR-guided metadynamics. PROC. NATL. ACAD. SCI. U.S.A. 110: 6817-6822

[19] Cavalli A., Camilloni C., Vendruscolo M. (2013) Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles that satisfy the maximum entropy principle. J. CHEM. PHYS. 138: 094112

[18] Camilloni C., Cavalli A., Vendruscolo M. (2013) Assessment of the Use of NMR Chemical Shifts as Replica-Averaged Structural Restraints in Molecular Dynamics Simulations to Characterise the Dynamics of Proteins. J. PHYS. CHEM. B 117: 1838-1843


[17] Tiana G., Camilloni C. (2012) Ratcheted molecular-dynamics simulations identify efficiently the transition state of protein folding. J. CHEM. PHYS. 137: 235101

[16] Heidarsson P., Valpapuram I., Camilloni C., Imparato A., Tiana G., Poulsen F., Kragelund B., Cecconi C. (2012) A Highly Compliant Protein Native State with a Spontaneous-like Mechanical Unfolding Pathway. J. AM. CHEM. SOC. 134: 17068–17075

[15] Sutto L., Camilloni C. (2012) From A to B: a ride in the free energy surfaces of Protein G domains suggests how new folds arise. J. CHEM. PHYS. 136: 185101

[14] Camilloni C., De Simone A., Vranken W., Vendruscolo M. (2012) Determination of Secondary Structure Populations in Disordered States of Proteins using NMR Chemical Shifts. BIOCHEMISTRY 51: 2224-2231

[13] Camilloni C., Robustelli P., De Simone A., Cavalli A., Vendruscolo M. (2012) Characterisation of the conformational equilibrium between the two major substates of RNase A using NMR chemical shifts. J. AM. CHEM. SOC. 134: 3968–3971

[12] Camilloni C., Schaal D., Schweimer K., Schwarzinger S., De Simone A. (2012) Energy Landscape of the Prion Protein Helix H1 Probed by Metadynamics and NMR. BIOPHYS. J. 102:158-167


[11] Camilloni C., Broglia R.A., Tiana G. (2011) Hierarchy of folding and unfolding events of protein G, CI2 and ACBP from explicit–solvent simulations. J. CHEM. PHYS. 134: 045105


[10] Caldarini M., Sutto L., Camilloni C., Vasile F., Broglia R.A., Tiana G. (2010) Identification of the folding inhibitors of hen-egg lysozyme: gathering the right tools. EUR. BIOPHYS. J. 39:911-919


[9] Camilloni C., Sutto L. (2009) Lymphotactin: how a protein can adopt two folds. J. CHEM. PHYS. 131: 245105

[8] Bonomi M., Branduardi D., Bussi G., Camilloni C., Provasi D., Raiteri P., Donadio D., Marinelli F., Pietrucci F., Broglia R.A., Parrinello M. (2009) PLUMED a Portable Plug-in for Free Energy Calculation with Molecular Dynamics. COMP. PHYS. COMM. 180: 1961-1970


[7] Calosci N., Chi C.N., Ritcher B., Camilloni C., Engström A., Eklund L., Travaglini-Allocatelli C., Gianni S., Vendruscolo M., Jemth P. (2008) Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins. PROC. NAT. ACAD. SCI. U.S.A 105: 19240-19245

[6] Verkhivker G.M., Tiana G., Camilloni C., Provasi D., Broglia R.A. (2008) Atomistic simulations of the HIV-1 protease folding inhibition. BIOPHYS. J. 95: 550-562

[5] Camilloni C., Sutto L., Provasi D., Tiana G., Broglia R.A. (2008) Early events in protein folding: is there something more than hydrophobic burst? PROTEIN SCIENCE 17: 1424-1433

[4] Marini F., Camilloni C., Provasi D., Broglia R.A., Tiana G. (2008) Metadynamic sampling of the free energy landscapes of proteins coupled with a Monte Carlo algorithm. GENE 422: 37-42

[3] Camilloni C., Guerini Rocco A., Eberini I., Gianazza E., Broglia R.A., Tiana G. (2008) Urea and guanidinium chloride denature Protein L in different ways in molecular dynamics simulations. BIOPHYS. J. 94: 4654-4661

[2] Camilloni C., Provasi D., Tiana G., Broglia R.A. (2008) Exploring the Protein G Helix Free Energy Surface by Solute Tempering Metadynamics. PROTEINS 71: 1647-1654


[1] Camilloni C., Provasi D., Tiana G., Broglia R.A. (2007) Optical absorption of a Green Fluorescent Protein variant: environment effects in a density functional study. J. PHYS. CHEM. B 111: 10807-10812