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  1. Article ; Online: V(D)J recombination and the evolution of the adaptive immune system.

    Market, Eleonora / Papavasiliou, F Nina

    PLoS biology

    2003  Volume 1, Issue 1, Page(s) E16

    MeSH term(s) Animals ; DNA Repair ; DNA-Binding Proteins ; Evolution, Molecular ; Gene Rearrangement ; Humans ; Immune System/physiology ; Mice ; Mice, SCID ; Mice, Transgenic ; Models, Biological ; Nuclear Proteins ; Nucleic Acid Conformation ; Receptors, Antigen, B-Cell/physiology ; Receptors, Antigen, T-Cell/physiology ; Recombination, Genetic ; Translocation, Genetic ; VDJ Recombinases/metabolism ; VDJ Recombinases/physiology
    Chemical Substances DNA-Binding Proteins ; Nuclear Proteins ; Receptors, Antigen, B-Cell ; Receptors, Antigen, T-Cell ; VDJ Recombinases (EC 2.7.7.-)
    Language English
    Publishing date 2003-10
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2126776-5
    ISSN 1545-7885 ; 1544-9173
    ISSN (online) 1545-7885
    ISSN 1544-9173
    DOI 10.1371/journal.pbio.0000016
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6193: Show issues Location:
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  2. Article: Intramolecular Diels-Alder reactions of N-substituted oxazolones.

    Fearnley, Stephen Philip / Market, Eleonora

    Chemical communications (Cambridge, England)

    2002  , Issue 5, Page(s) 438–439

    Abstract: The first intramolecular Diels-Alder reactions of simple trienes featuring an N-substituted oxazolone as the dienophilic component have been investigated and are reported herein. ...

    Abstract The first intramolecular Diels-Alder reactions of simple trienes featuring an N-substituted oxazolone as the dienophilic component have been investigated and are reported herein.
    MeSH term(s) Alkaloids/chemical synthesis ; Cyclization ; Oxazolone/analogs & derivatives ; Oxazolone/chemical synthesis ; Stereoisomerism
    Chemical Substances Alkaloids ; Oxazolone (15646-46-5)
    Language English
    Publishing date 2002-07-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/b110992h
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: V(D)J recombination and the evolution of the adaptive immune system.

    Eleonora Market / F Nina Papavasiliou

    PLoS Biology, Vol 1, Iss 1, p E

    2003  Volume 16

    Keywords Biology (General) ; QH301-705.5
    Language English
    Publishing date 2003-10-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article: The transcription elongation complex directs activation-induced cytidine deaminase-mediated DNA deamination.

    Besmer, Eva / Market, Eleonora / Papavasiliou, F Nina

    Molecular and cellular biology

    2006  Volume 26, Issue 11, Page(s) 4378–4385

    Abstract: Activation-induced cytidine deaminase (AID) is a single-stranded DNA deaminase required for somatic hypermutation of immunoglobulin (Ig) genes, a key process in the development of adaptive immunity. Transcription provides a single-stranded DNA substrate ... ...

    Abstract Activation-induced cytidine deaminase (AID) is a single-stranded DNA deaminase required for somatic hypermutation of immunoglobulin (Ig) genes, a key process in the development of adaptive immunity. Transcription provides a single-stranded DNA substrate for AID, both in vivo and in vitro. We present here an assay which can faithfully replicate all of the molecular features of the initiation of hypermutation of Ig genes in vivo. In this assay, which detects AID-mediated deamination in the context of transcription by Escherichia coli RNA polymerase, deamination targets either strand and declines in efficiency as the distance from the promoter increases. We show that AID binds DNA exposed by the transcribing polymerase, implicating the polymerase itself as the vehicle which distributes AID on DNA as it moves away from the promoter.
    MeSH term(s) Base Sequence ; Cytidine Deaminase/genetics ; Cytidine Deaminase/metabolism ; DNA/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Deamination ; Escherichia coli/enzymology ; Humans ; Molecular Sequence Data ; Plasmids/genetics ; Promoter Regions, Genetic/genetics ; Protein Binding ; Transcription, Genetic
    Chemical Substances DNA (9007-49-2) ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; AICDA (activation-induced cytidine deaminase) (EC 3.5.4.-) ; Cytidine Deaminase (EC 3.5.4.5)
    Language English
    Publishing date 2006-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.02375-05
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1666: Show issues Location:
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  5. Article: Intramolecular Diels–Alder reactions of N-substituted oxazolones

    Fearnley, Stephen Philip / Market, Eleonora

    Chemical communications. 2002 Feb. 28, , no. 5

    2002  

    Abstract: The first intramolecular Diels–Alder reactions of simple trienes featuring an N-substituted oxazolone as the dienophilic component have been investigated and are reported herein. ...

    Abstract The first intramolecular Diels–Alder reactions of simple trienes featuring an N-substituted oxazolone as the dienophilic component have been investigated and are reported herein.
    Keywords cycloaddition reactions ; oxazoles ; reaction mechanisms
    Language English
    Dates of publication 2002-0228
    Size p. 438-439.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/b110992h
    Database NAL-Catalogue (AGRICOLA)

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  6. Article: AID mediates hypermutation by deaminating single stranded DNA.

    Dickerson, Sarah K / Market, Eleonora / Besmer, Eva / Papavasiliou, F Nina

    The Journal of experimental medicine

    2003  Volume 197, Issue 10, Page(s) 1291–1296

    Abstract: Activation-induced deaminase (AID) is a protein indispensable for the diversification of immunoglobulin (Ig) genes by somatic hypermutation (SHM), class switch recombination (CSR), and gene conversion. To date, the precise role of AID in these processes ... ...

    Abstract Activation-induced deaminase (AID) is a protein indispensable for the diversification of immunoglobulin (Ig) genes by somatic hypermutation (SHM), class switch recombination (CSR), and gene conversion. To date, the precise role of AID in these processes has not been determined. Here we demonstrate that purified, tetrameric AID can deaminate cytidine residues in DNA, but not in RNA. Furthermore, we show that AID will bind and deaminate only single-stranded DNA, which implies a direct, functional link between hypermutation and transcription. Finally, AID does not target mutational hotspots, thus mutational targeting to specific residues must be attributed to different factors.
    MeSH term(s) APOBEC-1 Deaminase ; Cytidine Deaminase/physiology ; DNA, Single-Stranded/metabolism ; Deamination ; Humans ; RNA/metabolism ; Somatic Hypermutation, Immunoglobulin
    Chemical Substances DNA, Single-Stranded ; RNA (63231-63-0) ; AICDA (activation-induced cytidine deaminase) (EC 3.5.4.-) ; APOBEC-1 Deaminase (EC 3.5.4.36) ; APOBEC1 protein, human (EC 3.5.4.36) ; Cytidine Deaminase (EC 3.5.4.5)
    Language English
    Publishing date 2003-05-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218343-2
    ISSN 1540-9538 ; 0022-1007
    ISSN (online) 1540-9538
    ISSN 0022-1007
    DOI 10.1084/jem.20030481
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ua VI Zs.107: Show issues Location:
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