Annalisa Pastore

Distinguished Scientist at Elettraphoto

Contact information

Email: , - Mob. +39 340 7983293
Elettra - Sincrotrone Trieste S.C.p.A., SS 14 - km 163,5 - AREA Science Park, 34149 Basovizza, Trieste ITALY

Higher Education

Master Degree in Chemistry, University Federico II Napoli
PhD in Chemistry, Department of Chimica, Universita’ Federico II, Napoli

Appointments

2024 – present Visiting Scientist at King’s College London and Distinguished Scientist at Elettra Sincrotrone Trieste affiliated also Imperial College London
2022 – 2023 Director for Life Science and Chemistry at the European Synchrotron Radiation Facility, Grenoble, France
2013 – 2021 Professor, King’s College London (full time Oct 2013-Apr 2015 and Apr 2019 to 2021, part time 2015-2019) and member of Dementia Research Institute
Oct 2018 – Apr 2019 Professor, Scuola Normale of Pisa (part time)
2015 – 2018 Professor, University of Pavia (part time)
1997 – 2013 Team Leader, MRC NIMR, Mill Hill, London
1991 – 1997 Group leader at EMBL Heidelberg, Germany, in the Structures Program
1988 – 1991 Staff scientist position at EMBL Heidelberg, Germany, in the Biocomputing Program.
1986 – 1987 Postdoctoral fellow at the Department of Biochemistry, University of Oxford, UK
 
Honours
2015 Honorary Fellow at the Technical University of Munich (TUM-IAS)
2017 Proclamed “Top Italian Women Scientists-TIWS” by the    Italian Osservatorio Salute Donna Onda
2013 Included in AcademiaNet, a database of outstanding   Women Scientists which can be accessed only upon   nomination of an Institution. Nominated by EMBO.
2013 Elected Member of the Academia Europaea
2003-2013 Honorary professor of London University
2001 Elected EMBO Member
 
 

Awards and fellowships

Apr 2015 August Wilhelm Scheer Visiting Professor at the Technical University of Munich (TUM-IAS)
May 2015 Winner of an Italian National competition for a position of Director of the CNR IBIM in Palermo (suspended position because of a pending appeal)
Mar 2009-Feb 2012 Honorary Visiting Scientist (part-time) at INRA, Jouy-en-Josas, France supported by a Grant from the French Government (4 years)
Oct 2011 Invited visiting scientist at University of Baleari Islands (Mallorca)
Oct 2010 Invited visiting scientist at EPFL, in Lausanne.
Jul 2010 Invited visiting scientist to University of Baleari Islands (Palma de Mallorca)
Dec 2007 Selected (‘ternata’) in an Italian National competition for a position of Director of the CNR Institute of Biochemistry in Naples (the Italian equivalent of a Max Planck Director)
Jun 2006 Winner of an ICREA competition in Catalunya (only 15% of the International applicants were selected).
Mar 2004 – May 2004 Invited visiting scientist at MPI in Dortmund
Oct 2003 – Sep 2005 Invited visiting Professor (‘Ritorno dei cervelli’ scheme) at SISSA, Trieste, Italy
Mar 2002 –  May 2002 Invited visiting scientist at EMBL
Sep 2000 – Feb 2001 Invited visiting Professor (Poste Rouge) at the University of Strasbourg, France
Jan 1997 – Sep 1997 Invited visiting Professor (Poste Rouge) at the University of Rouen, France
Oct 1984 – Jul 1985 Italian/Swiss exchange grant to work in the Nobel Laureate Prof. R.R. Ernst’s group in the Physical Chemistry Dept. of ETH, Zurich, Switzerland
Jun 1982 – Jul 1983 NIH grant in Prof. W.A. Gibbons’ group, at the Department of Biochemistry, Wisconsin University, USA

Management

During my entire career as a principal investigator/ university professor (1991-2022), I have supervised more than 80 students (master and PhD), 150 postdocs and 20 visiting scientists.

Teaching

Academic qualifications and recognitions:
May 2000-2004 ‘Qualification’ for teaching in French Universities.
Sep 2002 Guest of Honour (‘Marraine de Promo’) at the end-of- the-course Ceremony of the University of Strasbourg ESBS (at the end of a 3 years undergraduate course, the students invite the person who meant most for   their formation)
May 2003-2013 Honorary Professor at University College London, UK
May 2005-2009 ‘Qualification’ for teaching in French Universities.
May 2013 My CV was recognized as the equivalent of an habilitation in Molecular Biology and Biochemistry in Italy
October 2013-2021 Full professor at King’s College London
 
Mentoring highlights
1992-2024 Supervisor of >20 PhD students
1992-2024 Supervision (as a first or second supervisor) of >58 PhD students.
2020-2024 Instructor of the Kings iGEM team who won a Silver Medal in 2020 and a Gold Medal in 2021.
 
Teaching experience
2013-2021 Lecturer in three Modules at King’s (Neurobiology, Biochemistry and Advanced methodologies)
2015-2018 Course of Immunology at University of Pavia
2012-2017 Invited lecturer at Scuola Normale di Pisa in Bioinformatics and Structural Biology
Feb 2007-2012 Invited lecturer at King’s College (London)(undergraduate course)
July 2004 Invited lecturer for an undergraduate course at University of Pisa (Pisa, Italy).
Oct 2000 – Feb 2001 undergraduate course on Structural Biology (1st year students) and Bioinformatics at the ESBS, Strasbourg (France).
1992-1997 Lectures and practicals in the EMBL Predoc Program
 

Other recognitions

  • Invited to write a biography of the Nobel Prize Rita Levi Montalcini by Enciclopedia Treccani (Italian equivalent of Encyclopaedia Britannica) (2024)
  • Panel member of the FCT-Tenure selection for Natural Sciences to select the new key academic positions for the Portuguese Ministery of Culture (2024)
  • Elected Member of the Editorial Board of Current Opinions in Structural Biology (2024)
  • SAB member for the ALBA Spanish synchrotron (2022-present)
  • Chair person for the Italian Ministerial Grants in the sector LS1 (2022-2023)
  • Elected committee member of Novo Nordisk Foundation (2023-2027)
  • Elected member of the Ampere NMR committee (2022-2027)
  • Committee Member of the Biochemistry & Molecular Biology Section of Academia Europeae for the selection of new members (2020-2024)
  • Committee Member of the F.R.S.-FNRS (Belgium) international panels for Grants and Fellowships (2020-2023)
  • Panel member of the Remedy Institute in Warsaw (2019-2024)
  • Member of the Scientific Advisory board of CERIC (C-European Research Infrastructure Consortium) (2011 - present)
  • Panel member for the evaluation of Lund University (Chemistry panel) (2020)
  • Panel member of the European Research Council (2016-2017)
  • Panel member of the Scientific Advisory Board of University Autonoma Catalunya (2016-present)
  • Panel member of the grant selection committee for the French Ministry of Research and Education ANR (2016-2017)
  • Panel member of the grant selection committee for the German DFG Funding Agency (2016)
  • Panel member of the grant selection committee for the Swedish Ministry of Research and Education (2014 and 2015)
  • Chairperson in the evaluation of the Life Sciences panel for the Research Projects of National Interest (PRIN) grants for the Italian Ministry of University and Research (MIUR) (2012-2013)
  • Reviewer of European Research Council grants
  • Member of an International panel for the assessment of University of Zurich (January 2013)
  • International Member (OCSE) of a panel for the Habilitation process (Molecular Biology sector) organized by the Italian Ministry (2013-2014)
  • Panel member of DFG assessments of applications for high field (1.2 GHz) NMR spectrometers in Germany (August 2012, February 2013 and February 2014).
  • Panel member of the Scientific Advisory Board of Biotechnology Institute in Helsinki, Finland (2011-2018)
  • Co-chairperson in the annual grant evaluation for the Portuguese Science Ministry (July 2009, 2010)
  • Panel member of the Roadmap Working Group of Experts for Biological and Medical Sciences (Systems Biology sub-group) (EU grants) (January 2008)
  • Panel member in a quinquennial evaluation of the Forth, Eraklion and Fleming Institutes, Athens (Greece) (September 2007), in the Institute for Molecular Medicine in Munich (Germany) (January 2005) and at the University of Ivry (France) (March 2006)
  • Chairperson of the CCPN committee (2004-2007)
  • Reviewer for the evaluation of National Grants in Czech Republic, Sweden, Italy (MURST, MIUR, PRIN), Belgium, France (Pasteur Institute, BLANC), UK (Wellcome, MRC, BBSRC), Swiss National Science Foundation, Israel, Portugal, Spain (ICREA) and Russia.
  • Chief Editor of the Open Systems Biology Journal (2006-2010)
  • Chief Editor of Frontiers in Biosciences (EPFL) (2013-2022)
  • Editorial board member of International Journal of Molecular Sciences (Molecular Biophysics Section). J. Biol. Chem., J. of Biol. Inorg. Chem., BBA: Proteins and Proteomics, PlosOne, Medicinal Chemistry, Prion, ScienceJet, PeerJ, The Open Biochemistry Journal and The Open Spectroscopy Journal

Patents and other translational work:

Non-anaphylactic forms of grass pollen Ph1 p6 allergen and their use. (00975093.6-2405-SE0002062)
The use of RNA aptamers in the visualization of TDP-43 aggregates.Patentapplication IT 102022000009500 (ref IIT PT210613/ref KCL IP501/2890)
 

Current Funding

2020 - 2025 Grant from ARUK (ARUK-PG2019B-020) Understanding the role of pathological cleavage in TDP-43 phase-separation ARUK 577,777
2022 - 2027 Pathfinder EU Grant £360,000
 

Research

The Pastore’s group has always followed two main interconnected lines: one more directly connected with main metabolic pathways (e.g. iron-sulfur cluster biogenesis, the role of RNA in protein aggregation) and human disease, the second related to more physico-chemical themes such as the forces that determine protein folding and stability. In the following some of the main aspects of both themes are given.
 
RNA in protein aggregation and disease
Increasing evidence has suggested that RNA plays an active dual role in neurodegeneration, either directly through sequestration of RNA binding proteins (RBPs) in foci or indirectly through aberrant RNA processing caused by the aggregation of RBPs as observed in myotonic dystrophy, multiple ataxias and Huntington’s disease (Gotor et al., 2020). At the same time, RBPs are implicated in the formation of physiologic membrane-less organelles suggesting that RNA may also be a beneficial component. A dual role of RNA in normal function and disease well agrees with the concept that aggregation is a competing pathway between physiologic and aberrant functions, as we observed in 2011 for polyglutamine proteins responsible for spinocerebellar ataxias (Masino et al., 2011). One of the most striking examples of a link between RNA and neurodegeneration are the frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) diseases. These are clinically distinct neurodegenerative diseases that share overlapping pathologies and genetic origins. Aggregates containing the RNA-binding proteins (RBPs) TDP-43 or FUS are observed in a predominant number (95%) of tau-negative FTD and ALS patients. Both knock-down and overexpression of the two proteins are neurotoxic. TDP-43 and FUS are involved in regulating RNA transcription, splicing, stabilization, transport and translation. They are modular proteins containing globular domains, intrinsically disordered regions and prion-like motifs. Until recently, the precise role of nucleic acids in the aggregation of TDP-43 and FUS had remained controversial even though increasing evidence seemed to link these proteins with liquid-liquid phase separation (LLPS), RNA-mediated protein condensation and prion-like behaviour (Louka et al., 2020). We centred our program of the last five years on the study of how RNA affects aggregation of these proteins and how this knowledge may be exploited for designing molecules able to compete specifically protein aggregation or used for diagnostic purposes. More recently, we have also initiated research on annexin A11 (ANXA11), another protein added to the causes of ALS/FTD (Smith et al., 2017).
Our research is organised in four interlinked objectives aiming at understanding the mechanisms that lead to disease and translating the knowledge into potential therapeutic approaches to prevent or alleviate neurodegeneration: 1. What is the link between RBPs, LLPS and prion-like aggregation? 2. Can we understand the determinants of protein-RNA recognition? 3. Can RNA be used as a specific aggregation inhibitor of RBDs and/or as a means to visualise protein aggregates? 4. How do Post-Translational Modifications (PTM) affect RNA-binding and aggregation? We are structural biologists who aim at dissecting the mechanisms that lead to neurodegeneration through biophysical and structural tools. In this attempt, we study the structure, fold stability, and function of proteins involved in diseases using different but complementary biophysical, biochemical and systems biology approaches. Our approach is that of understanding the processes leading to alterations in function through studying the responsible proteins both in their pathologic and normal states.

Iron-sulfur clusters and disease
FeS clusters are inorganic cofactors thought to be present already in the protocell and to have provided the most ancient response to the problem of storing the toxic and yet essential iron and sulfur elements in living cells. In proteins, they are usually coordinated by cysteine and/or histidine residues. Thanks to their favourable redox potential, FeS cluster proteins cover also in the modern cell essential functions in catalysis, electron transfer, and regulation of gene expression. FeS clusters also act as sulfur donors in biotin and lipoic acid cofactor biosynthesis. Synthesis and assembly of FeS into the target proteins is a complex and tightly regulated process under the control of evolutionary conserved machines, which were all discovered around year 2000. The importance of the FeS cluster assembly machine for human life and the urgency of dedicating research to its study are urged by the number of diseases which increasingly appear to be linked to impairment of FeS proteins and their maturation process, with defects in >12 genes linked to human disease having been identified so far in a very few years. Many of these diseases are lethal also very early on in life and are associated with a deficiency in the respiratory chain and alterations of the iron metabolism.Examples include pathologies associated with neurodegeneration, myopathies and haematology. Our group has been working for 25 years (e.g. since the identification of the responsible gene) on Friedreich’s ataxia (FRDA) making considerable progresses in the understanding of the disease mechanism. This is an autosomal recessive neurodegenerative disease with occurrence in 1:50000 and onset usually before 25 years of age. Because of our previous work in FRDA and in the ISC machine we are in a unique position to take on the challenge of studying the ISC machine and its relationship to disease with the final goal to define the molecular mechanism of FeS biogenesis in the eukaryotic cell. This information will provide a fundamental contribution to i) our knowledge of an essential metabolic pathway which plays a crucial role in several metabolic functions, iron homeostasis and gene expression, ii) our comprehension of the causes of diseases associated with defects in FeS proteins and iii) suggesting new therapeutic approaches much needed in the field.

The forces that determine protein folding
This project aims at understanding the mechanism of cold denaturation of proteins, an important and yet understudied phenomenon which is in principle common to all proteins. It is now well established that denaturation of proteins at low temperature is not a rare event but all globular proteins undergo cold denaturation in addition to the heat promoted transition. Understanding the structural determinants which allow the cold transition is thus a fundamental problem of protein biophysics that would allow a better understanding of the basic atomic forces and the effect of solvation. The reason why cold denaturation is observed only very rarely is solely due to the fact that most mesophilic proteins have their cold melting point at temperatures well below the freezing point of water. The thermodynamic expert P. Privalov suggested in the’90s that an essential aspect which plays a role in cold denaturation is solvation of residues of the hydrophobic core but up today no proof has been given to this fascinating hypothesis mostly due to the difficulty of studying the phenomenon.
To circumvent the problem of examining protein behaviour at sub-zero temperatures, proteins are often artificially destabilized by chemical or physical means and/or mutated, but these approaches may hinder the true causes of cold denaturation. We have found instead a system uniquely suited for the purpose, namely the yeast protein Yfh1 which we have exploited in the past for a number of purposes. This small full-length protein belongs to a large family of proteins, in human called frataxin, conserved from bacteria to primates. Yfh1 has its cold and heat denaturation, in the absence of salts, around 5 and 35°C, making the system convenient to study these transitions. Recently, we showed that we can, by introducing carefully chosen single mutations, stabilize selectively only the cold transition while retaining a low heat transition. We explained this asymmetric behaviour by showing that, in Yfh1, electrostatic repulsion between spatially close residues of Yfh1 directly affects the cold denaturation transition.
Now we would like to prove that this concept is not only applicable to the specific and somewhat special case of Yfh1 but is a fundamental phenomenon accessible to all proteins. We thus want to induce cold denaturation in otherwise stable proteins unrelated to Yfh1. If true, our hypothesis has important consequences for our understanding of cold denaturation and of the nature of the atomic forces which govern protein folding.

Recent publications

H-factor 81, citations 21769 according to Google-scholar
Selected from 291 primary articles over the period 2018-2024
(291) Spence H, Waldron FM, Saleeb RS, Brown AL, Rifai OM, Gilodi M, Read F, Roberts K, Milne G, Wilkinson D, O'Shaughnessy J, Pastore A, Fratta P, Shneider N, Tartaglia GG, Zacco E, Horrocks MH, Gregory JM. RNA aptamer reveals nuclear TDP-43 pathology is an early aggregation event that coincides with STMN-2 cryptic splicing and precedes clinical manifestation in ALS. Acta Neuropathol. 2024 Mar 5;147(1):50. doi: 10.1007/s00401-024-02705-1.
(289) Trajkovski, M., Pastore, A. and Plavec, J. (2024) Dimeric structures of DNA ATTTC repeats promoted by divalent cations. Nucleic Acids Res. 2024 Jan 31:gkae052. doi: 10.1093/nar/gkae052
(288) Dudas, E.F., Tully, M., Foldes, T., Kelly, G., Tartaglia, G.G., Pastore, A. (2024) The structural properties of full-length annexin A11. Frontiers in Mol. Biosci. 11:1347741. doi: 10.3389/fmolb.2024.1347741
(286) Chappard, A., Leighton, C., Saleeb, R.S., Jeacock, K.,Ball, S.R., Morris, K., Kantelberg, O., Lee, J., Zacco, E., Pastore, A., Sunde, M., Clarke, D.J., Downey, P., Kunath, T., Horrocks, M.H. (2023) Single-Molecule Two-Color Coincidence Detection of Unlabeled alpha-Synuclein Aggregates. Angew Chem Int Ed Engl. 2023 Apr 3;62(15):e202216771. doi: 10.1002/anie.202216771.
(285) Bennett SP, Crack JC, Puglisi R, Pastore A, Le Brun NE. (2022) Native mass spectrometric studies of IscSU reveal a concerted, sulfur-initiated mechanism of iron-sulfur cluster assembly. Chem Sci. 4(1):78-95. doi: 10.1039/d2sc04169c. 
(283) Morando MA, Venturella F, Sollazzo M, Monaca E, Sabbatella R, Vetri V, Passantino R, Pastore A, Alfano C. Solution structure of recombinant Pvfp-5βreveals insights into mussel adhesion. Commun Biol. 2022 Jul 25;5(1):739. doi: 10.1038/s42003-022-03699-w. 
(282) Zacco E, Kantelberg O, Milanetti E, Armaos A, Panei FP, Gregory J, Jeacock K, Clarke DJ, Chandran S, Ruocco G, Gustincich S, Horrocks MH, Pastore A*, Tartaglia GG*. (2022) Probing TDP-43 condensation using an in silico designed aptamer. Nat Commun. 13(1):3306. doi: 10.1038/s41467-022-30944-x (*co-corresponding author).
(280) Bitonti, A., Puglisi, R., Meli, M., Martin, S.R., Colombo, G.,Temussi, P.A., Pastore, A. (2022) Recipes for inducing cold denaturation in an otherwise stable protein. J Am Chem Soc. 144(16):7198-7207. doi: 10.1021/jacs.1c13355.
(279) Puglisi, R., Cioni, P., Gabellieri, E., Presciuttini, G.,Pastore, A.*, Temussi, P.A.* (2022) Heat and cold denaturation of Yeast frataxin: the effect of pressure. Biophys J. 2022 Apr 19;121(8):1502-1511. doi: 10.1016/j.bpj.2022.03.010  (*co-corresponding author).
(277) Louka, A., Bagnoli, S. Rupert, J., Esapa, B., Tartaglia, G.G., Cellerino, A., Pastore, A.*, Terzibasi Tozzini, E.*(2021) New lessons on TDP-43 from old N. furzeri killifish. Aging Cell e13517. https://doi.org/10.1111/acel.13517 (*co-corresponding author).
(276) Gilodi, M., Lisi, S., Dudás, E.F., Fantini, M., Puglisi, R., Louka, A., Marcatili, P., Cattaneo, A., Pastore, A. (2021) Selection and modelling of a new single-domain intrabody against TDP-43. Research Topic: A Journey Through 50 Years of Structural Bioinformatics in Memoriam of Cyrus Chothia, Frontiers in Molecular Biosciences, 8, 773234,
(275) Lyu, C., Da Vela, S., Al-Hilaly, Y., Marshall, Karen., Thorogate, R., Svergun, D., Serpell, L.C., Pastore, A., Hanger, D. (2021) The disease associated Tau35 fragment has an increased propensity to aggregate compared to full-length tau.Frontiers in Molecular Biosciences, Front Mol Biosci. 8:779240. doi: 10.3389/fmolb.2021.779240.
(274) Vannocci, T., Quaroni, L., de Riso, A., Milordini,G., Wolna, M., Cinque, G., Pastore, A. (2021) Label-free, real-time measurement of metabolism of adherent and suspended single cells by in-cell Fourier Transform Infrared Microspectroscopy. Int J Mol Sci. 2021 Oct 4;22(19):10742. doi: 10.3390/ijms221910742.
(272) Puglisi, R., Karunanithy, G., Hansen, D.F., Pastore, A.*, Temussi, P.A.* The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy. Commun Chem 4,127 (2021). https://doi.org/10.1038/s42004-021-00566-3 (*co-corresponding author).
(271) Monti, M., Armaos, A., Fantini, M., Pastore, A., Tartaglia, G.G. (2021) Aggregation is a context dependent constraint on protein evolution. Front. In Mol. Biosci. 8:678115. doi: 10.3389/fmolb.2021.678115
(270) Dudás, E.F., Puglisi, R., Korn, S.M., Alfano, C., Bellone, M.L., Dal Piaz, F., Kelly, G., Monaca, E., Schlundt, A., Schwalbe, H., Pastore, A. (2021). Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9. Biomolecular NMR Assignments, 23:1-7. doi: 10.1007/s12104-021-10011-0.
(269) Sicorello, A., Rozycki, Konarev, P., Svergun, D., Pastore, A. (2021) Capturing the conformational ensemble of the mixed foldedpolyglutamine .protein ataxin-3. Structure. 29(1):70-81.e5.doi: 10.1016/j.str.2020.09.010.
(267) Puglisi, R., Brilsky, O., Alfano, C., Martin, S.R., Pastore, A., Temussi, P.A. (2020) Thermodynamics of protein unfolding in complex environments: using 2D NMR to measure protein stability curves. Comm. Chem. https://doi.org/10.1038/s42004-020-00358-1.
(266) Pinto, M.F., Baici, A., Barbosa Pereira, P.J., Macedo-Ribeiro, S., Pastore, A., Rocha, F., Martins, P.M. (2020) InterferENZY: a web-based tool for enzymatic assay validation and standardized kinetic analysis. J. Mol. Biol. S0022-2836(20)30482-4. doi: 10.1016/j.jmb.2020.07.025.
(264) Millana Fañanás E, Todesca S, Sicorello A, Masino L, Pompach P, Magnani F, Pastore A*, Mattevi A*.  (2020) On the mechanism of calcium-dependent activation of NADPH oxidase 5 (NOX5). FEBS J 287:2486-2503.doi: 10.1111/febs.15160  (*co-corresponding author).
(263) Milordini,G.,Zacco,E.,Percival,M.,Puglisi,R.,Dal Piaz,F.,Temussi,P.A.,Pastore, A.(2020) The role of glycation on the aggregation properties of IAPP. Front. Mol. Biosci. 3;7:104. doi: 10.3389/fmolb.2020.00104.
(262) Fantini M, Lisi S, De Los Rios P, Cattaneo A, Pastore A. (2020) Protein Structural Information and Evolutionary Landscape by In Vitro Evolution. Mol Biol Evol. 37, 1179-1192. doi: 10.1093/molbev/msz256.
(260) Vannocci, T., Dinarelli, S., Pastore*, A., Longo*, A. (co-correpsonding author) (2019) A new tool to determine the cellular metabolic landscape: nanotechnology to the study of Friedreich’s ataxia. Sci Rep. 9, 19282. doi: 10.1038/s41598-019-55799-z.
(259) Yalinca,H., Gehin,C.J.C., Oleinikovas,V., Lashuel,H.A., Gervasio,F.L., Pastore, A. (2019) Therole of post-translational modifications on the energy landscape of Huntingtin N-terminus. Frontiers in Mol. Biosci. 6:95. doi: 10.3389/fmolb.2019.00095. eCollection 2019.
(257) Santonocito, R., Venturella, F., Dal Piaz, F., Morando, M.A., Provenzano, A., Rao, E., Costa, M.A.,  Bulone, D., San Biagio, P.L., Giacomazza, D., Sicorello, A., Alfano, C., Passantino, R., Pastore, A.(2019) Recombinant mussel protein Pvfp-5β: a potential tissue bioadhesive. JBC 294(34):12826-12835. doi: 10.1074/jbc.RA119.009531
(254)  Zacco, E., Graña-Montes, R., Martin, S., Sanchez de Groot, N., Alfano, C., Tartaglia, G., Pastore, A. (2019) RNA as a key factor in driving or preventing self-assembly of the TAR DNA-binding protein 43. J. Mol. Biol. 431(8):1671-1688. doi: 10.1016/j.jmb.2019.01.028.
(253) Rasheed, M.Jamshidiha, M., Puglisi, R., Yan, R., Cota, E., Pastore, A. (2019) A structural and functional characterization of a frataxin from a thermophile organism. Febs J. 286(3):495-506. doi: 10.1111/febs.14750. 
(251) Ramaswamy, S., Rasheed, M., Morelli, C., Calvio, C., Sutton, B., Pastore, A. (2018) The structure of PghL hydrolase bound to its substrate poly-γ-glutamate. Febs J. Nov. 2 doi: 10.1111/febs.
(250) Zacco, E., Martin, S.R., Thorogate, R., Pastore, A. (2018) The RNA-recognition motifs of TAR DNA-binding protein 43 may play a role in the aberrant self-assembly of the protein. Frontiers in Molecular Neuroscience 11, 372.
(249) Yan, R., Yalinca, H., Paoletti, F., Gobbo, F., Marchetti, L, Kuzmanic, A., Lamba, D., Gervasio, F.L., Konarev, P.V.,Cattaneo, A., Pastore, A. (2018)The structure of the Pro-domain of mouse proNGF in contact with the NGF domain. Structure 27(1):78-89.e3. doi: 10.1016/j.str.2018.09.013
(247) Emendato, A., Milordini, G., Zacco, E., Sicorello, A., Dal Piaz, F., Guerrini, R, Thorogate, R., Picone, D., Pastore, A. (2018) Glycation affects fibril formation of Aβpeptides. J Biol Chem. 293(34):13100-13111 doi: 10.1074/jbc.RA118.002275.
(246) Sicorello, A., Kelly, G., Oregioni, A., Nováček, J., Sklenář, V., Pastore, A. (2018) The structural properties in solution of the intrinsically mixed folded protein ataxin-3. Biophys. J. 115(1):59-71. doi: 10.1016/j.bpj.2018.05.029.
(245) Vannocci, T., Notario Manzano, R., Beccalli, O., Bettegazzi, B., Grohovaz, F., Cinque, G., de Riso, A., Quaroni, L., Codazzi, F., Pastore, A. (2018)Adding a temporal dimension to the study of Friedreich’s ataxia:the effect of frataxin overexpression in a human cell model. Dis Model Mech. 11, 6. doi: 10.1242/dmm.032706.
(244) Yan, R., De Los Rios, P., Pastore, A., Temussi, P. A. (2018) The Cold Denaturation of Iscu Highlights Structure-Function Dualism in Marginally Stable Proteins. Communications Chemistry 1, 13 doi:10.1038/s42004-018-0015-1
(243) Adinolfi, S., Puglisi, R., Crack, J. C., Iannuzzi, C., Dal Piaz, F., Konarev, P. V., Svergun, D. I., Martin, S., Le Brun, N. E. and Pastore, A. (2018) The molecular bases of the dual regulation of bacterial iron sulfur cluster biogenesis by CyaY and IscX.  Front. Mol. Biosci. 4:97 doi: 10.3389/fmolb.2017.00097.
 
Selected from 67 reviews, commentaries and book chapters over the period 2018-2024
(67) Pastore, A., Rivas Caballero, G., Temussi, P.A. (2024) Molecular crowding. Editorial of the Special Issue. Chemical Reviews. Accepted.
(66) Zacco, E., Broglia, L., Kurihara, M., Monti, M., Gustincich, S., Pastore, A., Plath, K., Nakagawa, S., Cerase, A., Sanchez de Groot, N., Tartaglia, G.G. (2024) RNA: The Unsuspected Conductor in the Orchestra of Macromolecular Crowding. Chemical review accepted.
(65) Grassmann, G., Miotto, M., Desantis, F., di Rienzo, L., Tartaglia, G.G., Pastore, A., Ruocco, G., Monti, M., Milanetti, E. (2024) Computational approaches to predict protein-protein interactions in crowded cellular environments. Chem Rev. 2024 Mar 27. doi: 10.1021/acs.chemrev.3c00550. 
(64) Alfano, C, Fichou, Y, Huber, K, Weiss, M., Spruijt, E, Ebbinghaus, S, De Luca, G., Morando, M. A., Vetri, V., Temussi, P.A., Pastore, A. (2024) Molecular crowding: the history and development of a scientific paradigm. Chem Rev. 2024 Mar 27;124(6):3186-3219. doi: 10.1021/acs.chemrev.3c00615. 
(62) Pastore, A., Shakhnovitch, E. (2023) From sequence to structure to mechanism to phenotype: The new frontiers of structural biology. Curr. Op. in Struct. Biol. 82, 102714.
(61) Pastore, A., Temussi, P.A. (2023) Unfolding under pressure: an NMR perspective. ChemBioChem. 2023 May 8;e202300164. doi: 10.1002/cbic.202300164.
(58) Alfano C, Pastore A, Temussi PA. (2022) Editorial: Insights in Structural Biology: 2021. Front Mol Biosci. 9:1020473. doi: 10.3389/fmolb.2022.1020473.
(57) Pastore A, Temussi PA. (2022) The Protein Unfolded State: One, No One and One Hundred Thousand. J Am Chem Soc. 144(49):22352-22357. doi: 10.1021/jacs.2c07696. 
(55) Pastore A, Temussi PA. (2022) Crowding revisited: Open questions and future perspectives. Trends Biochem Sci. S0968-0004(22)00140-2. doi: 10.1016/j.tibs.2022.05.007.
(54) Aprile, F., Temussi, P.A. A. (2021) Man does not live by intrinsically unstructured proteins alone: The role of structured regions in aggregation. Bioessays. Bioessays 43(11):e2100178. doi: 10.1002/bies.202100178.
(52) Temussi, P.A., Tartaglia, G.G., Pastore, A. (2021) The seesaw between normal function and protein aggregation: How functional interactions may increase protein solubility. Bioessays 43(6):e2100031. doi: 10.1002/bies.202100031.
(49) Louka, A., Zacco, E., Temussi, P.A., Tartaglia, G.G., Pastore, A. (2020) RNA as the Stone Guest of protein aggregation. Nucleic Acid Research, Oct 2020,gkaa822,https://doi.org/10.1093/nar/gkaa822
(48) Astoricchio, E., Alfano, C., Rajendran, L., Temussi, P.A., Pastore, A. (2020) The wide world of coacervates: from the sea to neurodegeneration. Trends Biochem Sci. 2020 May 13:S0968-0004(20)30109-2. doi: 10.1016/j.tibs.2020.04.006.
(47) Pastore A, Raimondi F, Rajendran L, Temussi PA. Why does the Aβ peptide of Alzheimer share structural similarity with antimicrobial peptides? Commun Biol. 2020 Mar 19;3(1):135. doi: 10.1038/s42003-020-0865-9.
(44) Pastore, A., Martin, S., Temussi, P.A. (2018) A generalized view of protein folding: In medio stat virtus. J. Am. Chem. Soc. 141(6):2194-2200. doi: 10.1021/jacs.8b10779
 
 
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