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  1. Article ; Online: Surface ruptures database related to the 26 December 2018, M

    Villani, F / Pucci, S / Azzaro, R / Civico, R / Cinti, F R / Pizzimenti, L / Tarabusi, G / Branca, S / Brunori, C A / Caciagli, M / Cantarero, M / Cucci, L / D'Amico, S / De Beni, E / De Martini, P M / Mariucci, M T / Messina, A / Montone, P / Nappi, R /
    Nave, R / Pantosti, D / Ricci, T / Sapia, V / Smedile, A / Vallone, R / Venuti, A

    Scientific data

    2020  Volume 7, Issue 1, Page(s) 42

    Abstract: ... of displacement with an average slip of about 0.09 m and a maximum value of 0.35 m. We have parsed and organized ...

    Abstract We provide a database of the surface ruptures produced by the 26 December 2018 Mw 4.9 earthquake that struck the eastern flank of Mt. Etna volcano in Sicily (southern Italy). Despite its relatively small magnitude, this shallow earthquake caused about 8 km of surface faulting, along the trace of the NNW-trending active Fiandaca Fault. Detailed field surveys have been performed in the epicentral area to map the ruptures and to characterize their kinematics. The surface ruptures show a dominant right-oblique sense of displacement with an average slip of about 0.09 m and a maximum value of 0.35 m. We have parsed and organized all observations in a concise database, with 932 homogeneous georeferenced records. The Fiandaca Fault is part of the complex active Timpe faults system affecting the eastern flank of Etna, and its seismic history indicates a prominent surface-faulting potential. Therefore, this database is essential for unravelling the seismotectonics of shallow earthquakes in volcanic areas, and contributes updating empirical scaling regressions that relate magnitude and extent of surface faulting.
    Language English
    Publishing date 2020-02-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2775191-0
    ISSN 2052-4463 ; 2052-4463
    ISSN (online) 2052-4463
    ISSN 2052-4463
    DOI 10.1038/s41597-020-0383-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Book ; Online: The United Nations' Declaration on Peasants' Rights

    ALABRESE, Mariagrazia / Bessa, Adriana / Brunori, Margherita / GIUGGIOLI, PIER FILIPPO

    2022  

    Keywords Applied ecology ; Environmental management ; Treaties & other sources of international law ; Human rights ; Central government policies ; Environmental policy & protocols ; Environmental science, engineering & technology ; Ecology / Agriculture / Rural Studies
    Size 1 electronic resource (286 pages)
    Publisher Taylor and Francis
    Document type Book ; Online
    Note English ; Open Access
    HBZ-ID HT021289913
    ISBN 9781003139874 ; 1003139876
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  3. Book ; Online: La volonté Italie-France allers-retours

    Bassano, Marie / Brunori, Luisa / Ciancio, Cristina / Garnier, Florent

    (Études d'histoire du droit et des idées politiques)

    2022  

    Series title Études d'histoire du droit et des idées politiques
    Keywords Language: history & general works ; criminologie ; doctrine ; influence ; volonté
    Language fra
    Size 1 electronic resource (525 pages)
    Publisher Presses de l'Université Toulouse Capitole
    Publishing place Toulouse
    Document type Book ; Online
    Note French
    HBZ-ID HT030377715
    ISBN 9782361702502 ; 2361702509
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  4. Article ; Online: Eraldo Antonini Lectures, 1983-2019.

    Brunori, Maurizio

    Biology direct

    2022  Volume 17, Issue 1, Page(s) 18

    Abstract: Can order spring from Chaos?" is the title of an extensive Report on Italian science published by NATURE on 12 May 1983 and written by Robert Walgate, the Chief European Correspondent. It is a twenty pages complete paper touching all aspects of the ... ...

    Abstract "Can order spring from Chaos?" is the title of an extensive Report on Italian science published by NATURE on 12 May 1983 and written by Robert Walgate, the Chief European Correspondent. It is a twenty pages complete paper touching all aspects of the struggle of Italian scientists to work in the "curious amalgam of ingenuity and muddle, a reflection of the political system". (Nature, 1983; 303: 109-128). To read it after four decades is interesting but somewhat depressing since the main problems unfolded in the paper have not been solved, starting with the largely insufficient support of fundamental curiosity driven research. At page 114 you could find a item called: ITALY's TOP SCIENTISTS: Four in the top one thousand. The Author refers to the data reported by the ISI (Institute of Scientific Information) that took two years to scan 3,000 major journals over the period 1965-78 and covered 5 millions articles and 67 millions references. The four top Italian scientists working in Italy were: Eraldo Antonini (3127 citations), Enrico Clementi (4001), Silvio Garattini (2833), and Giorgio Giacomelli (2483); 3 out of four were 52 years old, and one 55. Antonini did not see the Report since he passed away on March 18, 1983. However the information leaked before the publication of Nature because I remember the Messaggero of Rome reporting a whole page with the ranking of the four Italians, and even a picture of Eraldo. The students of the first year Medical course, his Class, welcomed the Professor with a standing ovation. After a short time the Board of the SIB (Società Italiana di Biochimica) casted a unanimous vote in favour of the motion of President Noris Siliprandi to begin the annual Congress with an Antonini Lecture, forever. As reported below, the tradition began immediately at the Congress in Saint-Vicent, Italy, and is continuing. In this paper I report an account of the Eraldo Antonini Lectures that I attended over the years and until September 2019, a few months before the pandemics lock down.
    Language English
    Publishing date 2022-07-15
    Publishing country England
    Document type Letter
    ZDB-ID 2221028-3
    ISSN 1745-6150 ; 1745-6150
    ISSN (online) 1745-6150
    ISSN 1745-6150
    DOI 10.1186/s13062-022-00330-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Still quoted after half a century.

    Brunori, Maurizio

    Molecular aspects of medicine

    2021  Volume 84, Page(s) 100989

    MeSH term(s) Hemoglobins ; Humans ; Myoglobin
    Chemical Substances Hemoglobins ; Myoglobin
    Language English
    Publishing date 2021-06-28
    Publishing country England
    Document type Editorial
    ZDB-ID 197640-0
    ISSN 1872-9452 ; 0098-2997
    ISSN (online) 1872-9452
    ISSN 0098-2997
    DOI 10.1016/j.mam.2021.100989
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: From Kuru to Alzheimer: A personal outlook.

    Brunori, Maurizio

    Protein science : a publication of the Protein Society

    2021  Volume 30, Issue 9, Page(s) 1776–1792

    Abstract: Seventy years ago, we learned from Chris Anfinsen that the stereochemical code necessary to fold a protein is embedded into its amino acid sequence. In water, protein morphogenesis is a spontaneous reversible process leading from an ensemble of ... ...

    Abstract Seventy years ago, we learned from Chris Anfinsen that the stereochemical code necessary to fold a protein is embedded into its amino acid sequence. In water, protein morphogenesis is a spontaneous reversible process leading from an ensemble of disordered structures to the ordered functionally competent protein; conforming to Aristotle's definition of substance, the synolon of matter and form. The overall process of folding is generally consistent with a two state transition between the native and the denatured protein: not only the denatured state is an ensemble of several structures, but also the native protein populates distinct functionally relevant conformational (sub)states. This two-state view should be revised, given that any globular protein can populate a peculiar third state called amyloid, characterized by an overall architecture that at variance with the native state, is by-and-large independent of the primary structure. In a nut shell, we should accept that beside the folded and unfolded states, any protein can populate a third state called amyloid which gained center stage being the hallmark of incurable neurodegenerative disorders, such as Alzheimer's and Parkinson's diseases as well as others. These fatal diseases are characterized by clear-cut clinical differences, yet display some commonalities such as the presence in the brain of amyloid deposits constituted by one misfolded protein specific for each disease. Some aspects of this complex problem are summarized here as an excursus from the prion's fibrils observed in the brain of aborigines who died of Kuru to the amyloid detectable in the cortex of Alzheimer's patients.
    MeSH term(s) Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid/metabolism ; Amyloid/ultrastructure ; Amyloid beta-Protein Precursor/chemistry ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Brain/metabolism ; Brain/pathology ; Gene Expression ; Humans ; Kuru/genetics ; Kuru/metabolism ; Kuru/pathology ; Models, Molecular ; Parkinson Disease/genetics ; Parkinson Disease/metabolism ; Parkinson Disease/pathology ; PrPC Proteins/chemistry ; PrPC Proteins/genetics ; PrPC Proteins/metabolism ; PrPSc Proteins/chemistry ; PrPSc Proteins/genetics ; PrPSc Proteins/metabolism ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Denaturation ; Protein Folding ; Thermodynamics ; alpha-Synuclein/chemistry ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism ; tau Proteins/chemistry ; tau Proteins/genetics ; tau Proteins/metabolism
    Chemical Substances APP protein, human ; Amyloid ; Amyloid beta-Protein Precursor ; MAPT protein, human ; PrPC Proteins ; PrPSc Proteins ; alpha-Synuclein ; tau Proteins
    Language English
    Publishing date 2021-06-26
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1002/pro.4145
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Modulation of Allosteric Control and Evolution of Hemoglobin.

    Brunori, Maurizio / Miele, Adriana Erica

    Biomolecules

    2023  Volume 13, Issue 3

    Abstract: Allostery arises when a ligand-induced change in shape of a binding site of a protein is coupled to a tertiary/quaternary conformational change with a consequent modulation of functional properties. The two-state allosteric model of Monod, Wyman and ... ...

    Abstract Allostery arises when a ligand-induced change in shape of a binding site of a protein is coupled to a tertiary/quaternary conformational change with a consequent modulation of functional properties. The two-state allosteric model of Monod, Wyman and Changeux [J. Mol. Biol. 1965; 12, 88-118] is an elegant and effective theory to account for protein regulation and control. Tetrameric hemoglobin (Hb), the oxygen transporter of all vertebrates, has been for decades the ideal system to test for the validity of the MWC theory. The small ligands affecting Hb's behavior (organic phosphates, protons, bicarbonate) are produced by the red blood cell during metabolism. By binding to specific sites, these messengers make Hb sensing the environment and reacting consequently. HbI and HbIV from trout and human HbA are classical cooperative models, being similar yet different. They share many fundamental features, starting with the globin fold and the quaternary assembly, and reversible cooperative O
    MeSH term(s) Animals ; Humans ; Ligands ; Allosteric Regulation ; Models, Molecular ; Hemoglobins/metabolism ; Oxygen/metabolism
    Chemical Substances Ligands ; Hemoglobins ; Oxygen (S88TT14065)
    Language English
    Publishing date 2023-03-22
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom13030572
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Towards a new framework to assess agri-food value chains' sustainability - The case of chestnut value chain.

    Allali, Tarek / Colabianchi, Manola / Moretti, Michele / Brunori, Gianluca

    Heliyon

    2024  Volume 10, Issue 7, Page(s) e27836

    Abstract: Food systems rely on natural resources for production causing their depletion. Sustainability assessment can encourage farms and agri-food companies to improve sustainability performances. Sustainability assessment frameworks and tools differ in their ... ...

    Abstract Food systems rely on natural resources for production causing their depletion. Sustainability assessment can encourage farms and agri-food companies to improve sustainability performances. Sustainability assessment frameworks and tools differ in their purposes, scope, methods of application, and required time for execution; however, most of them do not fit with value chains, or they do not cover all sustainability dimensions. Our objective is to propose a holistic framework to assess sustainability at agri-food value chains level. The proposed framework combines the Sustainability Assessment of Food and Agriculture systems (SAFA) (El Hage, 2012) [1] and The Agri-food Evaluation Framework (TEEB) [2]. It incorporates the concepts of Socio-Ecological Systems, Assemblage, and Social Practices. It integrates system dynamics by emphasising human and natural capital stocks and their users. We explain in detail the methodological steps we followed to construct and to apply this new framework to two case studies in Italy and France. The new framework was applied to real-life case studies and has shown its effectiveness and demonstrates its potential for widespread use in similar scenarios.
    Language English
    Publishing date 2024-03-19
    Publishing country England
    Document type Journal Article
    ZDB-ID 2835763-2
    ISSN 2405-8440
    ISSN 2405-8440
    DOI 10.1016/j.heliyon.2024.e27836
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: A retrospective study of hydrocortisone continuous rate infusion compared with administration of dexamethasone boluses in dogs with adrenal crisis.

    Brunori, Lara / Walesby, Olivia X / Lewis, Daniel H / Boag, Alisdair M

    Journal of veterinary internal medicine

    2024  Volume 38, Issue 2, Page(s) 951–959

    Abstract: Background: Evidence indicating the optimal treatment protocol for dogs in adrenal crisis is lacking.: Objectives: Compare outcomes of dogs presented in adrenal crisis treated with either hydrocortisone (HC) continuous rate infusion (CRI) or ... ...

    Abstract Background: Evidence indicating the optimal treatment protocol for dogs in adrenal crisis is lacking.
    Objectives: Compare outcomes of dogs presented in adrenal crisis treated with either hydrocortisone (HC) continuous rate infusion (CRI) or intermittent dexamethasone (DEX) administration.
    Animals: Thirty-nine client-owned dogs.
    Methods: Multi-institutional retrospective observational study (July 2016-May 2022) including dogs diagnosed with adrenal crisis and with available sequential blood work during hospitalization. Dogs were excluded if already on treatment with exogenous corticosteroids. Outcomes assessed included duration of hospitalization, survival, number of repeat measurements of electrolyte concentrations, and time to normalization of electrolyte and acid-base status.
    Results: No significant difference was found between the groups for hospitalization time (P = .41; HC median [range] 48 h [19-105 h]; DEX 57 h [17-167 h]) nor case fatality rate 2/28 in the DEX group and 0/11 in the HC group (P = 1), nor in number of measurements of electrolyte concentrations (P = .90; HC 4 [2-10]; DEX 4.5 [2-15]). No significant differences were found between the 2 treatment groups in time to normalization of serum Na (P = .30; HC 33 h [7-66 h]; DEX 16 h [1.5-48 h]), K (P = .92; HC 17 h [4-48 h]; DEX 16 h [1.25-60 h]) or Na/K ratio (P = .08; HC 17 h [8-48 h]; DEX 26 h [1.5-60 h]).
    Conclusions: This study detected no difference in outcomes for dogs in adrenal crisis treated with either DEX boluses or HC CRIs.
    MeSH term(s) Animals ; Dogs ; Dexamethasone/therapeutic use ; Electrolytes ; Hydrocortisone/therapeutic use ; Retrospective Studies
    Chemical Substances Dexamethasone (7S5I7G3JQL) ; Electrolytes ; Hydrocortisone (WI4X0X7BPJ)
    Language English
    Publishing date 2024-02-14
    Publishing country United States
    Document type Journal Article ; Multicenter Study ; Observational Study, Veterinary
    ZDB-ID 92798-3
    ISSN 1939-1676 ; 0891-6640
    ISSN (online) 1939-1676
    ISSN 0891-6640
    DOI 10.1111/jvim.17017
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: An Outlook on the Complexity of Protein Morphogenesis in Health and Disease.

    Brunori, Maurizio / Gianni, Stefano

    Frontiers in molecular biosciences

    2022  Volume 9, Page(s) 909567

    Abstract: The study of the mechanisms whereby proteins achieve their native functionally competent conformation has been a key issue in molecular biosciences over the last 6 decades. Nevertheless, there are several debated issues and open problems concerning some ... ...

    Abstract The study of the mechanisms whereby proteins achieve their native functionally competent conformation has been a key issue in molecular biosciences over the last 6 decades. Nevertheless, there are several debated issues and open problems concerning some aspects of this fundamental problem. By considering the emerging complexity of the so-called "native state," we attempt hereby to propose a personal account on some of the key topics in the field, ranging from the relationships between misfolding and diseases to the significance of protein disorder. Finally, we briefly describe the recent and exciting advances in predicting protein structures from their amino acid sequence.
    Language English
    Publishing date 2022-06-13
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2814330-9
    ISSN 2296-889X
    ISSN 2296-889X
    DOI 10.3389/fmolb.2022.909567
    Database MEDical Literature Analysis and Retrieval System OnLINE

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