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  1. Article: Tom Paine

    Gallagher, Buell G / Paine, Tom

    Great American liberals , p. 1-13

    1971  , Page(s) 1–13

    Author's details Buell G. Gallagher
    Publisher Books for Libraries Press
    Publishing place Freeport, New York
    Document type Article
    Database ECONomics Information System

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  2. Book: Guide to the psychiatry of old age

    Ames, David / Gallagher, Damien / Loi, Samantha / Russ, Tom

    2022  

    Abstract: What is the psychiatry of old age and why do we need it? -- Assessment of the elderly psychiatric patient -- Differential diagnosis - the 3 Ds -- The dementias -- Behavioural and psychological symptoms of dementia -- Delirium -- Mood disorders in late ... ...

    Author's details David Ames (University of Melbourne), Damien Gallagher (University of Toronto), Samantha Loi (Royal Melbourne Hospital), Tom Russ (University of Edinburgh & NHS Lothian)
    Abstract What is the psychiatry of old age and why do we need it? -- Assessment of the elderly psychiatric patient -- Differential diagnosis - the 3 Ds -- The dementias -- Behavioural and psychological symptoms of dementia -- Delirium -- Mood disorders in late life -- Schizophrenia and related disorders in late life -- Neurotic and personality disorders -- Substance abuse and iatrogenesis in late life -- Services for older patients with psychiatric disorders -- The future of the psychiatry of old age.

    "Emeritus Professor of Psychiatry, University of Melbourne Academic Unit for Psychiatry of Old Age and National Ageing Research Institute, Parkville and consultant psychiatrist for Royal Melbourne, St George's and Epworth Camberwell Hospitals, all in Melbourne. David Ames is an experienced old age psychiatrist who has worked both clinically and academically in the field for 31 years. He has edited/written over 20 books, over 250 peer reviewed research papers and led the first edition of this book. is an old age psychiatrist in Sunnybrook Health Sciences Centre, Toronto, Canada and assistant professor with the University of Toronto. His clinical and research interests include the neurobiology of depression in later life and associated cognitive dysfunction. In his work he has explored modifiable risk factors for cognitive decline and is now engaged in interventional studies to improve treatment outcomes for older adults with behavioural and neurocognitive disorders in later life. Samantha Loi is an old age psychiatrist working at the Royal Melbourne Hospital, Australia in the Neuropsychiatry Unit since 2015. She is also a senior lecturer at the University of Melbourne Academic Unit for Psychiatry of Old Age and recently received her PhD qualification. She has extensive clinical experience and her research interests include carer well-being and the use of modern technology to improve quality of life of older adults. Intermediate Clinical Fellow at the Centre for Dementia Prevention and Alzheimer Scotland Dementia Research Centre, both at the University of Edinburgh, and an Honorary Consultant Psychiatrist for NHS Lothian"--
    Keywords Mental Disorders ; Aged ; Geriatric Psychiatry / methods ; Geriatrie ; Psychiatrie
    Subject Seelenheilkunde ; Altersmedizin ; Altersheilkunde
    Language English
    Size xvi, 125 Seiten, Illustrationen
    Edition Second edition
    Publisher Cambridge University Press
    Publishing place Cambridge
    Publishing country Great Britain
    Document type Book
    Note "... revised second edition ... The new edition is updated to incorporate new developments in assessment, investigation, classification, treatment and care since the publication of the first edition, including the ICD-11 and DSM-5.". - Rückumschlag ; Includes bibliographical references and index
    HBZ-ID HT021401133
    ISBN 978-1-108-40715-1 ; 9781108290173 ; 1-108-40715-3 ; 1108290175
    Database Catalogue ZB MED Medicine, Health

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  3. Article ; Online: Many Keys Unlock the Doors for Virus Entry.

    Gallagher, Tom

    mBio

    2022  Volume 13, Issue 3, Page(s) e0044522

    Abstract: To successfully infect, viruses must respond to cues that promote their genome delivery into host cells. These keys to virus entry frequently reside inside endocytic vesicles. In a recent mBio article, Poston et al. (D. Poston, Y. Weisblum, A. Hobbs, and ...

    Abstract To successfully infect, viruses must respond to cues that promote their genome delivery into host cells. These keys to virus entry frequently reside inside endocytic vesicles. In a recent mBio article, Poston et al. (D. Poston, Y. Weisblum, A. Hobbs, and P. D. Bieniasz, mBio 13:e0300221, 2022, https://doi.org/10.1128/mbio.03002-21) identified and characterized protein complexes generating endocytic environments favorable for virus entry. These included retromer-associated vacuolar protein sorting 29 (VPS29) proteins. Without VPS29, endosomes lacked cathepsin activities, making them incapable of supporting those viruses in which endosomal proteolysis triggers entry. These protease-dependent viruses encompass several zoonotic filoviruses and coronaviruses, including recent SARS-CoV-2 variants of concern. The valuable findings of Poston et al. reveal retromer complexes as master keys for select endosomal virus entry processes and raise the possibility that threatening coronaviruses might be resisted through targeted inactivation of components controlling endosome structure and function.
    MeSH term(s) COVID-19 ; Endosomes/metabolism ; Humans ; SARS-CoV-2 ; Virus Internalization
    Language English
    Publishing date 2022-05-17
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mbio.00445-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: COVID19 therapeutics: Expanding the antiviral arsenal.

    Gallagher, Tom

    EBioMedicine

    2021  Volume 66, Page(s) 103289

    MeSH term(s) Antiviral Agents/therapeutic use ; COVID-19 ; Humans ; SARS-CoV-2
    Chemical Substances Antiviral Agents
    Language English
    Publishing date 2021-03-19
    Publishing country Netherlands
    Document type Journal Article ; Comment
    ZDB-ID 2851331-9
    ISSN 2352-3964
    ISSN (online) 2352-3964
    DOI 10.1016/j.ebiom.2021.103289
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: COVID19 therapeutics

    Tom Gallagher

    EBioMedicine, Vol 66, Iss , Pp 103289- (2021)

    Expanding the antiviral arsenal

    2021  

    Keywords Medicine ; R ; Medicine (General) ; R5-920
    Language English
    Publishing date 2021-04-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: Opportunity in a Crisis: We Can Do Better.

    Gallagher, Tom K

    Transplantation

    2020  Volume 105, Issue 10, Page(s) 2140–2141

    Language English
    Publishing date 2020-09-10
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 208424-7
    ISSN 1534-6080 ; 0041-1337
    ISSN (online) 1534-6080
    ISSN 0041-1337
    DOI 10.1097/TP.0000000000003492
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Adaptive variations in SARS-CoV-2 spike proteins: effects on distinct virus-cell entry stages.

    Qing, Enya / Gallagher, Tom

    mBio

    2023  Volume 14, Issue 4, Page(s) e0017123

    Abstract: Evolved SARS-CoV-2 variants of concern (VOCs) spread through human populations in succession. Major virus variations are in the entry-facilitating viral spike (S) proteins; Omicron VOCs have 29-40 S mutations relative to ancestral D614G viruses. The ... ...

    Abstract Evolved SARS-CoV-2 variants of concern (VOCs) spread through human populations in succession. Major virus variations are in the entry-facilitating viral spike (S) proteins; Omicron VOCs have 29-40 S mutations relative to ancestral D614G viruses. The impacts of this Omicron divergence on S protein structure, antigenicity, cell entry pathways, and pathogenicity have been extensively evaluated, yet gaps remain in correlating specific alterations with S protein functions. In this study, we compared the functions of ancestral D614G and Omicron VOCs using cell-free assays that can reveal differences in several distinct steps of the S-directed virus entry process. Relative to ancestral D614G, Omicron BA.1 S proteins were hypersensitized to receptor activation, to conversion into intermediate conformational states, and to membrane fusion-activating proteases. We identified mutations conferring these changes in S protein character by evaluating domain-exchanged D614G/Omicron recombinants in the cell-free assays. Each of the three functional alterations was mapped to specific S protein domains, with the recombinants providing insights on inter-domain interactions that fine-tune S-directed virus entry. Our results provide a structure-function atlas of the S protein variations that may promote the transmissibility and infectivity of current and future SARS-CoV-2 VOCs. IMPORTANCE Continuous SARS-CoV-2 adaptations generate increasingly transmissible variants. These succeeding variants show ever-increasing evasion of suppressive antibodies and host factors, as well as increasing invasion of susceptible host cells. Here, we evaluated the adaptations enhancing invasion. We used reductionist cell-free assays to compare the entry steps of ancestral (D614G) and Omicron (BA.1) variants. Relative to D614G, Omicron entry was distinguished by heightened responsiveness to entry-facilitating receptors and proteases and by enhanced formation of intermediate states that execute virus-cell membrane fusion. We found that these Omicron-specific characteristics arose from mutations in specific S protein domains and subdomains. The results reveal the inter-domain networks controlling S protein dynamics and efficiencies of entry steps, and they offer insights on the evolution of SARS-CoV-2 variants that arise and ultimately dominate infections worldwide.
    MeSH term(s) Humans ; COVID-19 ; SARS-CoV-2/genetics ; Spike Glycoprotein, Coronavirus/genetics ; Virus Internalization ; Endopeptidases
    Chemical Substances spike protein, SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Endopeptidases (EC 3.4.-)
    Language English
    Publishing date 2023-06-29
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mbio.00171-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Dynamic association of the intramembrane proteases SPPL2a/b and their substrates with tetraspanin-enriched microdomains.

    Leinung, Nadja / Mentrup, Torben / Patel, Mehul / Gallagher, Tom / Schröder, Bernd

    iScience

    2023  Volume 26, Issue 10, Page(s) 107819

    Abstract: Signal peptide peptidase-like 2a and b (SPPL2a/b) are aspartyl intramembrane proteases and cleave tail-anchored proteins as well as N-terminal fragments (NTFs) derived from type II-oriented transmembrane proteins. How these proteases recruit substrates ... ...

    Abstract Signal peptide peptidase-like 2a and b (SPPL2a/b) are aspartyl intramembrane proteases and cleave tail-anchored proteins as well as N-terminal fragments (NTFs) derived from type II-oriented transmembrane proteins. How these proteases recruit substrates and cleavage is regulated, is still incompletely understood. We found that SPPL2a/b localize to detergent-resistant membrane (DRM) domains with the characteristics of tetraspanin-enriched microdomains (TEMs). Based on this, association with several tetraspanins was evaluated. We demonstrate that not only SPPL2a/b but also their substrates tumor necrosis factor (TNF) and CD74 associate with tetraspanins like CD9, CD81, and CD82 and/or TEMs and analyze the stability of these complexes in different detergents. CD9 and CD81 deficiency has protease- and substrate-selective effects on SPPL2a/b function. Our findings suggest that reciprocal interactions with tetraspanins may assist protease-substrate encounters of SPPL2a/b within the membrane. Beyond SPP/SPPL proteases, this supports previous concepts that tetraspanins facilitate membrane-embedded proteolytic processes.
    Language English
    Publishing date 2023-09-04
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2023.107819
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: SARS Coronavirus Redux.

    Qing, Enya / Gallagher, Tom

    Trends in immunology

    2020  Volume 41, Issue 4, Page(s) 271–273

    Abstract: As an atypical pneumonia began to appear in December 2019, Zhou et al. worked with remarkable speed to identify the associated virus, determine its relationship to animal viruses, and evaluate factors conferring infection susceptibility and resistance. ... ...

    Abstract As an atypical pneumonia began to appear in December 2019, Zhou et al. worked with remarkable speed to identify the associated virus, determine its relationship to animal viruses, and evaluate factors conferring infection susceptibility and resistance. These foundational results are being advanced to control the current worldwide human coronavirus epidemic.
    MeSH term(s) Animals ; Betacoronavirus ; Chiroptera ; Coronavirus ; Disease Outbreaks ; Humans ; Pneumonia, Viral/epidemiology ; SARS Virus
    Keywords covid19
    Language English
    Publishing date 2020-03-12
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 2036831-8
    ISSN 1471-4981 ; 1471-4906
    ISSN (online) 1471-4981
    ISSN 1471-4906
    DOI 10.1016/j.it.2020.02.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Book: Injury prevention and public health

    Christoffel, Tom / Gallagher, Susan Scavo

    practical knowledge, skills, and strategies

    2006  

    Author's details Tom Christoffel and Susan Scavo Gallagher
    Keywords Wounds and Injuries / prevention & control ; Accident Prevention ; Wounds and injuries/Prevention ; Accidents/Prevention ; Personal injuries/Prevention
    Subject code 617.1
    Language English
    Size XXX, 495 S., 24cm
    Edition 2. ed.
    Publisher Jones and Bartlett
    Publishing place Sudbury, Mass. u.a.
    Publishing country United States
    Document type Book
    Note Includes bibliographical references and index. - Formerly CIP
    HBZ-ID HT015351426
    ISBN 0-7637-3392-X ; 978-0-7637-3392-6
    Database Catalogue ZB MED Medicine, Health

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