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  1. Book ; Audio / Video: Leaders in American Medicine--Daniel Nathans

    DiMaio, Daniel

    (Leaders in American Medicine)

    1996  

    Abstract: Daniel Nathan was born and raised in Delaware where he attended the public schools and ...

    Title variant Daniel Nathans.
    Institution Alpha Omega Alpha.
    Johns Hopkins University. / School of Medicine
    Author's details [Johns Hopkins University School of Medicine in cooperation with Alpha Omega Alpha]
    Series title Leaders in American Medicine
    Abstract Daniel Nathan was born and raised in Delaware where he attended the public schools and the University of Delaware. In an environment where education was stressed, he went to the Washington University in St. Louis, MO and interned at Presbyterian Hospital in NY. From there, he went to the NIH for 2 years, the Rockefeller Institute for Medical Research for 3 years and then to The Johns Hopkins University School of Medicine in Baltimore, MD, where he taught in the department of microbiology for 37 years until his death in 1999. He also served as department chairman and interim president in 1994-95. In 1978, Dr. Nathan, along with Dr. Werner Arber and Dr. Hamilton O. Smith were co-recipients of the Nobel Prize in Medicine for the 'discovery of restriction enzymes and their application to problems of molecular genetics'.
    MeSH term(s) Biomedical Research/history ; Genetics ; History, 20th Century ; Melanoma/etiology ; Physicians ; Bacteriophages/genetics ; DNA, Recombinant/biosynthesis ; Virology/classification
    Keywords United States
    Language English
    Size 1 videocassette of 1 (U-Matic) (59 min.) :, sd., col. ;, 3/4 in. ; 1 videocassette of 1 (Betacam SP) (59 min.) :, sd., col. ;, 1/2 in. ; 1 videodisc of 1 (DVD) (59 min.) :, sd., col. ;, 4 3/4 in.
    Publisher Johns Hopkins University School of Medicine
    Publishing place Baltimore, MD
    Document type Book ; Audio / Video
    Note Last inspected: 200304
    Database Catalogue of the US National Library of Medicine (NLM)

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  2. Article: Daniel Nathans: October 30, 1928-November 16, 1999.

    Dimaio, D

    Biographical memoirs. National Academy of Sciences (U.S.)

    2001  Volume 79, Page(s) 262–279

    MeSH term(s) Genetics/history ; History, 20th Century ; Molecular Biology/history ; United States ; Virology/history
    Language English
    Publishing date 2001
    Publishing country United States
    Document type Biography ; Historical Article ; Journal Article ; Portrait
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Noncanonical Rab9a action supports endosomal exit of human papillomavirus during virus entry.

    Choi, Jeongjoon / DiMaio, Daniel

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Rab GTPases play key roles in controlling intracellular vesicular transport. GTP-bound Rab proteins support vesicle trafficking. Here, we report that, unlike cellular protein cargos, the delivery of human papillomaviruses (HPV) into the retrograde ... ...

    Abstract Rab GTPases play key roles in controlling intracellular vesicular transport. GTP-bound Rab proteins support vesicle trafficking. Here, we report that, unlike cellular protein cargos, the delivery of human papillomaviruses (HPV) into the retrograde transport pathway during virus entry is inhibited by Rab9a in its GTP-bound form. Knockdown of Rab9a hampers HPV entry by regulating the HPV-retromer interaction and impairing retromer-mediated endosome-to-Golgi transport of the incoming virus, resulting in the accumulation of HPV in the endosome. Rab9a is in proximity to HPV as early as 3.5 h post-infection, prior to the Rab7-HPV interaction. HPV displays increased association with retromer in Rab9a knockdown cells, even in the presence of dominant negative Rab7. Thus, Rab9a can regulate HPV-retromer association independently of Rab7. Surprisingly, excess GTP-Rab9a impairs HPV entry, whereas excess GDP-Rab9a stimulates entry. These findings reveal that HPV employs a trafficking mechanism distinct from that used by cellular proteins.
    Language English
    Publishing date 2023-05-01
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.05.01.538937
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry.

    Choi, Jeongjoon / DiMaio, Daniel

    PLoS pathogens

    2023  Volume 19, Issue 9, Page(s) e1011648

    Abstract: Rab GTPases play key roles in controlling intracellular vesicular transport. GTP-bound Rab proteins support vesicle trafficking. Here, we report that, unlike cellular protein cargos, retromer-mediated delivery of human papillomaviruses (HPV) into the ... ...

    Abstract Rab GTPases play key roles in controlling intracellular vesicular transport. GTP-bound Rab proteins support vesicle trafficking. Here, we report that, unlike cellular protein cargos, retromer-mediated delivery of human papillomaviruses (HPV) into the retrograde transport pathway during virus entry is inhibited by Rab9a in its GTP-bound form. Knockdown of Rab9a inhibits HPV entry by modulating the HPV-retromer interaction and impairing retromer-mediated endosome-to-Golgi transport of the incoming virus, resulting in the accumulation of HPV in the endosome. Rab9a is in proximity to HPV as early as 3.5 h post-infection, prior to the Rab7-HPV interaction, and HPV displays increased association with retromer in Rab9a knockdown cells, even in the presence of dominant negative Rab7. Thus, Rab9a can regulate HPV-retromer association independently of Rab7. Surprisingly, excess GTP-Rab9a impairs HPV entry, whereas excess GDP-Rab9a reduces association between L2 and Rab9a and stimulates entry. These findings reveal that HPV and cellular proteins utilize the Rab9a host trafficking machinery in distinct ways during intracellular trafficking.
    MeSH term(s) Humans ; Human Papillomavirus Viruses ; Virus Internalization ; Papillomavirus Infections/genetics ; Endosomes ; Guanosine Triphosphate
    Chemical Substances Guanosine Triphosphate (86-01-1)
    Language English
    Publishing date 2023-09-13
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1011648
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Human Papillomavirus L2 Capsid Protein Stabilizes γ-Secretase during Viral Infection.

    Crite, Mac / DiMaio, Daniel

    Viruses

    2022  Volume 14, Issue 4

    Abstract: Intracellular trafficking of human papillomavirus (HPV) during virus entry requires γ-secretase, a cellular protease consisting of a complex of four cellular transmembrane (TM) proteins. γ-secretase typically cleaves substrate proteins but it plays a non- ...

    Abstract Intracellular trafficking of human papillomavirus (HPV) during virus entry requires γ-secretase, a cellular protease consisting of a complex of four cellular transmembrane (TM) proteins. γ-secretase typically cleaves substrate proteins but it plays a non-canonical role during HPV entry. γ-secretase binds to the HPV minor capsid protein L2 and facilitates its insertion into the endosomal membrane. After insertion, L2 protrudes into the cytoplasm, which allows HPV to bind other cellular factors required for proper virus trafficking into the retrograde transport pathway. Here, we further characterize the interaction between γ-secretase and HPV L2. We show that γ-secretase is required for cytoplasmic protrusion of L2 and that L2 associates strongly with the PS1 catalytic subunit of γ-secretase and stabilizes the γ-secretase complex. Mutational studies revealed that a putative TM domain in HPV16 L2 cannot be replaced by a foreign TM domain, that infectivity of HPV TM mutants is tightly correlated with γ-secretase binding and stabilization, and that the L2 TM domain is required for protrusion of the L2 protein into the cytoplasm. These results provide new insight into the interaction between γ-secretase and L2 and highlight the importance of the native HPV L2 TM domain for proper virus trafficking during entry.
    MeSH term(s) Alphapapillomavirus/metabolism ; Amyloid Precursor Protein Secretases/metabolism ; Capsid Proteins/metabolism ; Humans ; Oncogene Proteins, Viral/metabolism ; Papillomaviridae/metabolism ; Papillomavirus Infections/metabolism
    Chemical Substances Capsid Proteins ; Oncogene Proteins, Viral ; Amyloid Precursor Protein Secretases (EC 3.4.-)
    Language English
    Publishing date 2022-04-13
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v14040804
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Traptamer screening: a new functional genomics approach to study virus entry and other cellular processes.

    Xie, Jian / DiMaio, Daniel

    The FEBS journal

    2021  Volume 289, Issue 2, Page(s) 355–362

    Abstract: Historically, the genetic analysis of mammalian cells entailed the isolation of randomly arising mutant cell lines with altered properties, followed by laborious genetic mapping experiments to identify the mutant gene responsible for the phenotype. In ... ...

    Abstract Historically, the genetic analysis of mammalian cells entailed the isolation of randomly arising mutant cell lines with altered properties, followed by laborious genetic mapping experiments to identify the mutant gene responsible for the phenotype. In recent years, somatic cell genetics has been revolutionized by functional genomics screens, in which expression of every protein-coding gene is systematically perturbed, and the phenotype of the perturbed cells is determined. We outline here a novel functional genomics screening strategy that differs fundamentally from commonly used approaches. In this strategy, we express libraries of artificial transmembrane proteins named traptamers and select rare cells with the desired phenotype because, by chance, a traptamer specifically perturbs the expression or activity of a target protein. Active traptamers are then recovered from the selected cells and can be used as tools to dissect the biological process under study. We also briefly describe how we have used this new strategy to provide insights into the complex process by which human papillomaviruses enter cells.
    MeSH term(s) Amino Acid Sequence/genetics ; Cell Line ; Cell Lineage/genetics ; Gene Expression Regulation/genetics ; Genomics ; Humans ; Mass Screening ; Membrane Proteins/genetics ; Protein Transport/genetics ; Virus Internalization
    Chemical Substances Membrane Proteins
    Language English
    Publishing date 2021-05-08
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.15775
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
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  7. Article ; Online: Small size, big impact: how studies of small DNA tumour viruses revolutionized biology.

    DiMaio, Daniel

    Philosophical transactions of the Royal Society of London. Series B, Biological sciences

    2019  Volume 374, Issue 1773, Page(s) 20180300

    Abstract: Intense study of three families of small tumour viruses with double-stranded DNA genomes, carried out over 50 years, has had a profound impact on biology. The polyomaviruses and papillomaviruses have circular DNA genomes of approximately 5000 and ... ...

    Abstract Intense study of three families of small tumour viruses with double-stranded DNA genomes, carried out over 50 years, has had a profound impact on biology. The polyomaviruses and papillomaviruses have circular DNA genomes of approximately 5000 and approximately 8000 base-pairs, respectively, and thus encode only a handful of proteins. Adenoviruses have a 32 000-base-pair linear DNA genome, still far smaller than the three billion-base-pair human genome. Members of all three virus families can transform cultured cells to tumorigenicity and cause tumours in experimental animals. Several human papillomaviruses (HPV) and at least one polyomavirus are oncogenic in humans. Early analysis of these viruses, particularly the polyomavirus SV40, led to the development of many powerful experimental tools, including restriction mapping, site-directed mutagenesis, gene transfer, genome-wide sequencing and recombinant DNA. These tools have since been refined and used to study cellular genes, revolutionizing our understanding of biology. These tools were also applied to the viruses themselves. Analysis of the virus life cycle and the effect of these viruses on cells yielded important new insights into many aspects of gene expression, DNA replication, cell biology and carcinogenesis. These studies have also led to vaccination strategies to prevent infection and cancer in humans. This article is part of the theme issue 'Silent cancer agents: multi-disciplinary modelling of human DNA oncoviruses'.
    MeSH term(s) Animals ; DNA Tumor Viruses/physiology ; Humans ; Tumor Virus Infections/virology
    Language English
    Publishing date 2019-04-29
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 208382-6
    ISSN 1471-2970 ; 0080-4622 ; 0264-3839 ; 0962-8436
    ISSN (online) 1471-2970
    ISSN 0080-4622 ; 0264-3839 ; 0962-8436
    DOI 10.1098/rstb.2018.0300
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Einzelsignatur: Show issues

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  8. Article ; Online: Introduction.

    Enquist, Lynn W / Dermody, Terence S / DiMaio, Daniel

    Annual review of virology

    2021  Volume 8, Issue 1, Page(s) i–ii

    Language English
    Publishing date 2021-09-29
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2764224-0
    ISSN 2327-0578 ; 2327-056X
    ISSN (online) 2327-0578
    ISSN 2327-056X
    DOI 10.1146/annurev-vi-08-072621-100001
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  9. Article ; Online: Recurring Revolutions in Virology.

    Enquist, Lynn W / DiMaio, Daniel / Dermody, Terence S

    Annual review of virology

    2021  Volume 8, Issue 1, Page(s) v–vii

    Language English
    Publishing date 2021-04-07
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2764224-0
    ISSN 2327-0578 ; 2327-056X
    ISSN (online) 2327-0578
    ISSN 2327-056X
    DOI 10.1146/annurev-vi-08-032921-100002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Is virology dead?

    Dimaio, Daniel

    mBio

    2014  Volume 5, Issue 2, Page(s) e01003–14

    MeSH term(s) History, 20th Century ; History, 21st Century ; Host-Pathogen Interactions ; Virology/history ; Virology/trends ; Virus Diseases/epidemiology ; Virus Diseases/virology ; Virus Physiological Phenomena ; Viruses/pathogenicity
    Keywords covid19
    Language English
    Publishing date 2014-03-25
    Publishing country United States
    Document type Editorial ; Historical 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.01003-14
    Database MEDical Literature Analysis and Retrieval System OnLINE

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