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  1. Article ; Online: Microglial G

    Merlini, Mario / Rafalski, Victoria A / Ma, Keran / Kim, Keun-Young / Bushong, Eric A / Rios Coronado, Pamela E / Yan, Zhaoqi / Mendiola, Andrew S / Sozmen, Elif G / Ryu, Jae Kyu / Haberl, Matthias G / Madany, Matthew / Sampson, Daniel Naranjo / Petersen, Mark A / Bardehle, Sophia / Tognatta, Reshmi / Dean, Terry / Acevedo, Rosa Meza / Cabriga, Belinda /
    Thomas, Reuben / Coughlin, Shaun R / Ellisman, Mark H / Palop, Jorge J / Akassoglou, Katerina

    Nature neuroscience

    2020  Volume 24, Issue 1, Page(s) 19–23

    Abstract: Microglial surveillance is a key feature of brain physiology and disease. Here, we found that G ...

    Abstract Microglial surveillance is a key feature of brain physiology and disease. Here, we found that G
    MeSH term(s) Animals ; Calcium Signaling ; Cell Movement ; Convulsants ; Electroencephalography ; G-Protein-Coupled Receptor Kinase 1/physiology ; Immunologic Surveillance ; Mice ; Microglia/enzymology ; Microglia/physiology ; Microglia/ultrastructure ; Nerve Net/physiology ; Nervous System Diseases/physiopathology ; Nervous System Physiological Phenomena ; Pilocarpine ; Seizures/physiopathology ; Signal Transduction ; rho GTP-Binding Proteins/metabolism
    Chemical Substances Convulsants ; Pilocarpine (01MI4Q9DI3) ; G-Protein-Coupled Receptor Kinase 1 (EC 2.7.11.14) ; Grk1 protein, mouse (EC 2.7.11.14) ; rho GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2020-12-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1420596-8
    ISSN 1546-1726 ; 1097-6256
    ISSN (online) 1546-1726
    ISSN 1097-6256
    DOI 10.1038/s41593-020-00756-7
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    Zs.A 4891: Show issues Location:
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  2. Article ; Online: A Step Forward in Solving Amyloidosis.

    Merlini, Giampaolo

    The New England journal of medicine

    2023  Volume 389, Issue 17, Page(s) 1615–1617

    MeSH term(s) Humans ; Amyloidosis/diagnosis
    Language English
    Publishing date 2023-10-27
    Publishing country United States
    Document type Editorial
    ZDB-ID 207154-x
    ISSN 1533-4406 ; 0028-4793
    ISSN (online) 1533-4406
    ISSN 0028-4793
    DOI 10.1056/NEJMe2309308
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  3. Article ; Online: Active vaccination with ankyrin G reduces β-amyloid pathology in APP transgenic mice.

    Santuccione, A C / Merlini, M / Shetty, A / Tackenberg, C / Bali, J / Ferretti, M T / McAfoose, J / Kulic, L / Bernreuther, C / Welt, T / Grimm, J / Glatzel, M / Rajendran, L / Hock, C / Nitsch, R M

    Molecular psychiatry

    2013  Volume 18, Issue 3, Page(s) 358–368

    Abstract: ... the neuronal cytoskeletal protein ankyrin G (ankG); these correlated with slower rates of cognitive decline ...

    Abstract Serum antibodies against amyloid-β peptide (Aβ) in humans with or without diagnosis of Alzheimer's disease (AD) indicate the possibility of immune responses against brain antigens. In an unbiased screening for antibodies directed against brain proteins, we found in AD patients high serum levels of antibodies against the neuronal cytoskeletal protein ankyrin G (ankG); these correlated with slower rates of cognitive decline. Neuronal expression of ankG was higher in AD brains than in nondemented age-matched healthy control subjects. AnkG was present in exosomal vesicles, and it accumulated in β-amyloid plaques. Active immunization with ankG of arcAβ transgenic mice reduced brain β-amyloid pathology and increased brain levels of soluble Aβ(42). AnkG immunization induced a reduction in β-amyloid pathology, also in Swedish transgenic mice(.) Anti-ankG monoclonal antibodies reduced Aβ-induced loss of dendritic spines in hippocampal ArcAβ organotypic cultures. Together, these data established a role for ankG in the human adaptive immune response against resident brain proteins, and they show that ankG immunization reduces brain β-amyloid and its related neuropathology.
    MeSH term(s) Alzheimer Disease/blood ; Alzheimer Disease/immunology ; Alzheimer Disease/pathology ; Alzheimer Disease/prevention & control ; Amyloid beta-Peptides/antagonists & inhibitors ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Peptides/toxicity ; Animals ; Ankyrins/immunology ; Ankyrins/metabolism ; Antibodies/blood ; Antibodies, Monoclonal/pharmacology ; Brain/metabolism ; Brain/pathology ; Cells, Cultured ; Hippocampus/cytology ; Hippocampus/drug effects ; Humans ; Mice ; Mice, Transgenic ; Neurons/cytology ; Peptide Fragments/metabolism ; Plaque, Amyloid/metabolism ; Vaccination
    Chemical Substances ANK3 protein, human ; Amyloid beta-Peptides ; Ankyrins ; Antibodies ; Antibodies, Monoclonal ; Peptide Fragments ; amyloid beta-protein (1-42)
    Language English
    Publishing date 2013-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1330655-8
    ISSN 1476-5578 ; 1359-4184
    ISSN (online) 1476-5578
    ISSN 1359-4184
    DOI 10.1038/mp.2012.70
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    Zs.A 4812: Show issues Location:
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  4. Article ; Online: Introduction.

    Merlini, Giampaolo

    Hematology/oncology clinics of North America

    2020  Volume 34, Issue 6, Page(s) xv–xvi

    MeSH term(s) History, 19th Century ; History, 20th Century ; History, 21st Century ; Humans ; Immunoglobulin Light-chain Amyloidosis/history ; Immunoglobulin Light-chain Amyloidosis/therapy
    Language English
    Publishing date 2020-10-06
    Publishing country United States
    Document type Editorial ; Historical Article ; Introductory Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 93115-9
    ISSN 1558-1977 ; 0889-8588
    ISSN (online) 1558-1977
    ISSN 0889-8588
    DOI 10.1016/j.hoc.2020.08.008
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  5. Article ; Online: 'Standing on the Shoulders of the Giants': Dr. Giampaolo Merlini.

    Mohty, Mohamad / Merlini, Giampaolo

    Clinical hematology international

    2023  Volume 5, Issue 2-3, Page(s) 139–142

    Language English
    Publishing date 2023-03-20
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 2590-0048
    ISSN (online) 2590-0048
    DOI 10.1007/s44228-023-00039-5
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  6. Article ; Online: Mining the amyloid-plaque proteome to uncover disease mechanisms in renal amyloidoses.

    Nuvolone, Mario / Merlini, Giampaolo

    Kidney international

    2023  Volume 105, Issue 3, Page(s) 427–429

    Abstract: Beyond typing amyloid deposits and discovering new forms of amyloidosis, laser microdissection and mass spectrometry enable the analysis of the amyloid-plaque proteome constituents-amyloid fibrillar proteins, matrix and cellular components, and absorbed ... ...

    Abstract Beyond typing amyloid deposits and discovering new forms of amyloidosis, laser microdissection and mass spectrometry enable the analysis of the amyloid-plaque proteome constituents-amyloid fibrillar proteins, matrix and cellular components, and absorbed blood-borne proteins. Charalampous et al. analyzed the amyloid-plaque proteomes of the 7 most common renal amyloidoses to gain preliminary mechanistic insights on cellular and molecular perturbations elicited during gradual amyloid deposition and potential tissue repair or damage mechanisms. Clinical correlations identified a prognostic pattern.
    MeSH term(s) Humans ; Plaque, Amyloid ; Proteome ; Amyloidosis ; Amyloid/metabolism ; Mass Spectrometry
    Chemical Substances Proteome ; Amyloid
    Language English
    Publishing date 2023-08-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 120573-0
    ISSN 1523-1755 ; 0085-2538
    ISSN (online) 1523-1755
    ISSN 0085-2538
    DOI 10.1016/j.kint.2023.12.013
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  7. Article ; Online: Démolition controversée, entre revendication et droit d’auteur

    Chiara Merlini

    Les Cahiers de la Recherche Architecturale, Urbaine et Paysagère (2021)

    2021  

    Abstract: The discourse on demolition is generally characterized by emotional tones and conflicts. This is particularly evident in the debate on social housing districts. A debate that is particularly influenced by stigmatizing images and on which symbolic ... ...

    Abstract The discourse on demolition is generally characterized by emotional tones and conflicts. This is particularly evident in the debate on social housing districts. A debate that is particularly influenced by stigmatizing images and on which symbolic investments are particularly high, both for residents and for public institutions. In the case of a « signed » architecture, the controversy may be even more intense, because the conflict between different values is explicit. On one side, the values of comfort and habitability, supported mainly by the inhabitants. On the other side, the cultural value that recognizes an artefact as a collective heritage, supported above all by intellectual elites. This is what emerges from the case examined: a demolition hypothesis concerning a housing complex built in Bollate, near Milan, by the architect Guido Canella between 1974 and 1980. The architect’s mobilization, which replaces the lack of collective recognition with the claim of a “copyright”, is an interesting specificity of this story.
    Keywords Urban Project ; Social Housing ; Demolition ; Conservation Of Modern Architecture ; Copyright ; Architecture ; NA1-9428 ; Geography. Anthropology. Recreation ; G
    Subject code 720
    Language French
    Publishing date 2021-02-01T00:00:00Z
    Publisher Ministère de la culture
    Document type Article ; Online
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  8. Article ; Online: Two-hit strategy for treating AL amyloidosis?

    Merlini, Giampaolo / Palladini, Giovanni

    Blood

    2022  Volume 138, Issue 25, Page(s) 2596–2598

    MeSH term(s) Amyloidosis/therapy ; Humans ; Immunoglobulin Light Chains ; Immunoglobulin Light-chain Amyloidosis/drug therapy
    Chemical Substances Immunoglobulin Light Chains
    Language English
    Publishing date 2022-01-20
    Publishing country United States
    Document type Editorial ; Comment
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood.2021013817
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  9. Article ; Online: AL amyloidosis: from molecular mechanisms to targeted therapies.

    Merlini, Giampaolo

    Hematology. American Society of Hematology. Education Program

    2017  Volume 2017, Issue 1, Page(s) 1–12

    Abstract: Systemic amyloidosis is caused by misfolding and extracellular deposition of circulating proteins as amyloid fibrils, resulting in the dysfunction of vital organs. The most common systemic amyloidosis, light-chain (AL) amyloidosis, is caused by misfolded ...

    Abstract Systemic amyloidosis is caused by misfolding and extracellular deposition of circulating proteins as amyloid fibrils, resulting in the dysfunction of vital organs. The most common systemic amyloidosis, light-chain (AL) amyloidosis, is caused by misfolded light chains produced by a small, dangerous B-cell clone. The process of amyloid formation, organ targeting, and damage is multifaceted and, after disease initiation, the complexity of the downstream pathogenic cascade increases, rendering its control a challenge. Because of the progressive nature of the disease, early diagnosis to prevent end-stage organ damage is vital. Improving awareness and systematic use of biomarkers of organ damage in screening populations at risk may improve the still unsatisfactory diagnostic process. Amyloid imaging is now emerging as an important companion of biomarkers in formulating the diagnosis and prognosis and monitoring the effects of therapy. An accurate diagnosis is the basis for appropriate therapy that is risk-adapted and response-tailored. Effective treatments targeting the clone and rapidly and profoundly reducing the amyloid light chains have produced marked improvements in overall survival, making AL amyloidosis the most successful model of all amyloidoses. New therapies targeting the amyloid deposits are now under development, together with novel agents modulating light chain aggregation and proteotoxicity. The future of AL amyloidosis treatment is combination therapy and will require an innovative collaborative model for a rapid translation from bench to bedside with the ultimate aim of achieving a cure for this complex disease.
    MeSH term(s) B-Lymphocytes/metabolism ; B-Lymphocytes/pathology ; Biomarkers/blood ; Disease-Free Survival ; Humans ; Immunoglobulin Light-chain Amyloidosis/blood ; Immunoglobulin Light-chain Amyloidosis/mortality ; Immunoglobulin Light-chain Amyloidosis/therapy ; Protein Folding ; Survival Rate
    Chemical Substances Biomarkers
    Language English
    Publishing date 2017-12-01
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2084287-9
    ISSN 1520-4383 ; 1520-4391
    ISSN (online) 1520-4383
    ISSN 1520-4391
    DOI 10.1182/asheducation-2017.1.1
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  10. Article ; Online: How I treat AL amyloidosis.

    Palladini, Giovanni / Merlini, Giampaolo

    Blood

    2021  Volume 139, Issue 19, Page(s) 2918–2930

    Abstract: The treatment of patients with systemic light chain (AL) amyloidosis is a challenge to hematologists. Despite its generally small size, the underlying clone causes a rapidly progressing, often devastating multiorgan dysfunction through the toxic light ... ...

    Abstract The treatment of patients with systemic light chain (AL) amyloidosis is a challenge to hematologists. Despite its generally small size, the underlying clone causes a rapidly progressing, often devastating multiorgan dysfunction through the toxic light chains that form amyloid deposits. Clinical manifestations are deceitful and too often recognized at an irreversible stage. However, hematologists are in the unique position to diagnose AL amyloidosis at a presymptomatic stage, checking biomarkers of amyloid organ involvement in patients with monoclonal gammopathies at higher risk to develop the disease. Adequate technology and expertise are needed for a prompt and correct diagnosis, particularly for ruling out non-AL amyloidoses that are now also treatable. Therapy should be carefully tailored based on severity of organ involvement and clonal characteristics, and early and continual monitoring of response is critical. Three recent randomized clinical trials moved AL amyloidosis to evidence-based era. Above all, the daratumumab-bortezomib combination is a new standard-of-care for newly diagnosed patients, inducing rapid and deep responses that translate into high rates of organ response. The availability of new effective drugs allows to better personalize the therapy, reduce toxicity, and improve outcomes. Patients should be treated within clinical trials whenever possible.
    MeSH term(s) Amyloidosis/drug therapy ; Amyloidosis/therapy ; Bortezomib/therapeutic use ; Humans ; Immunoglobulin Light-chain Amyloidosis/drug therapy ; Immunoglobulin Light-chain Amyloidosis/therapy ; Immunotherapy ; Paraproteinemias/drug therapy
    Chemical Substances Bortezomib (69G8BD63PP)
    Language English
    Publishing date 2021-09-11
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood.2020008737
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