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  1. Article ; Online: The CRISPR-RNA World: An Interview with Martin Jínek.

    Davies, Kevin / Jínek, Martin

    The CRISPR journal

    2020  Volume 3, Issue 2, Page(s) 68–72

    Language English
    Publishing date 2020-05-13
    Publishing country United States
    Document type Interview
    ZDB-ID 3017891-5
    ISSN 2573-1602 ; 2573-1599
    ISSN (online) 2573-1602
    ISSN 2573-1599
    DOI 10.1089/crispr.2020.29091.mji
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 7195: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 119: Show issues

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  2. Article ; Online: Uncut but Primed for Change.

    Jínek, Martin

    The CRISPR journal

    2019  Volume 2, Issue 6, Page(s) 352–354

    MeSH term(s) Anastomosis, Roux-en-Y ; DNA ; Gastrectomy ; Gene Editing
    Chemical Substances DNA (9007-49-2)
    Language English
    Publishing date 2019-12-01
    Publishing country United States
    Document type Journal Article ; Comment
    ISSN 2573-1602
    ISSN (online) 2573-1602
    DOI 10.1089/crispr.2019.29079.mji
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  3. Book ; Conference proceedings: Festschrift

    Huys, Quentin J. M. / Jínek, Martin / Huys, Quentin J.M.

    aus Anlass der Verleihung des Georg-Friedrich-Götz-Preises 2016

    2017  

    Title translation Festschrift
    Event/congress Georg-Friedrich-Götz-Preis 2016 (2017, Zürich)
    Author's details Georg-Friedrich-Götz-Preis 2016
    Language German ; English
    Size 54 Seiten, Illustrationen, Diagramme
    Publisher Georg-Friedrich-Götz-Stiftung, Medizinische Fakultät der Universität Zürich
    Publishing place Zürich
    Publishing country Switzerland
    Document type Book ; Conference proceedings
    Note Der 2. Beitrag ist in englischer Sprache
    HBZ-ID HT019246826
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    2017 A 356 available for loan (reading room) Lesesaal EG

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  4. Book ; Online ; Conference proceedings: Festschrift

    Huys, Quentin J. M. / Jínek, Martin / Huys, Quentin J.M.

    aus Anlass der Verleihung des Georg-Friedrich-Götz-Preises 2016

    2017  

    Title translation Festschrift
    Event/congress Georg-Friedrich-Götz-Preis 2016 (2017, Zürich)
    Author's details Georg-Friedrich-Götz-Preis 2016
    Subject code 610
    Language German ; English
    Size 1 Online-Ressource (54 Seiten), Illustrationen, Diagramme
    Publisher Georg-Friedrich-Götz-Stiftung, Medizinische Fakultät der Universität Zürich
    Publishing place Zürich
    Publishing country Switzerland
    Document type Book ; Online ; Conference proceedings
    Note Der 2. Beitrag ist in englischer Sprache ; Götz-Preisverleihung vom 9. Februar 2017
    HBZ-ID HT019486131
    DOI 10.4126/FRL01-006405257
    Database Repository for Life Sciences

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  5. Article ; Online: Past, present, and future of CRISPR genome editing technologies.

    Pacesa, Martin / Pelea, Oana / Jinek, Martin

    Cell

    2024  Volume 187, Issue 5, Page(s) 1076–1100

    Abstract: Genome editing has been a transformative force in the life sciences and human medicine, offering unprecedented opportunities to dissect complex biological processes and treat the underlying causes of many genetic diseases. CRISPR-based technologies, with ...

    Abstract Genome editing has been a transformative force in the life sciences and human medicine, offering unprecedented opportunities to dissect complex biological processes and treat the underlying causes of many genetic diseases. CRISPR-based technologies, with their remarkable efficiency and easy programmability, stand at the forefront of this revolution. In this Review, we discuss the current state of CRISPR gene editing technologies in both research and therapy, highlighting limitations that constrain them and the technological innovations that have been developed in recent years to address them. Additionally, we examine and summarize the current landscape of gene editing applications in the context of human health and therapeutics. Finally, we outline potential future developments that could shape gene editing technologies and their applications in the coming years.
    MeSH term(s) Humans ; Biological Science Disciplines ; CRISPR-Cas Systems ; Gene Editing ; Genetic Therapy ; Technology
    Language English
    Publishing date 2024-02-27
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2024.01.042
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1167: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 58: Show issues

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  6. Article ; Online: Substrate selectivity and catalytic activation of the type III CRISPR ancillary nuclease Can2.

    Jungfer, Kenny / Sigg, Annina / Jinek, Martin

    Nucleic acids research

    2023  Volume 52, Issue 1, Page(s) 462–473

    Abstract: Type III CRISPR-Cas systems provide adaptive immunity against foreign mobile genetic elements through RNA-guided interference. Sequence-specific recognition of RNA targets by the type III effector complex triggers the generation of cyclic oligoadenylate ( ...

    Abstract Type III CRISPR-Cas systems provide adaptive immunity against foreign mobile genetic elements through RNA-guided interference. Sequence-specific recognition of RNA targets by the type III effector complex triggers the generation of cyclic oligoadenylate (cOA) second messengers that activate ancillary effector proteins, thus reinforcing the host immune response. The ancillary nuclease Can2 is activated by cyclic tetra-AMP (cA4); however, the mechanisms underlying cA4-mediated activation and substrate selectivity remain elusive. Here we report crystal structures of Thermoanaerobacter brockii Can2 (TbrCan2) in substrate- and product-bound complexes. We show that TbrCan2 is a single strand-selective DNase and RNase that binds substrates via a conserved SxTTS active site motif, and reveal molecular interactions underpinning its sequence preference for CA dinucleotides. Furthermore, we identify a molecular interaction relay linking the cA4 binding site and the nuclease catalytic site to enable divalent metal cation coordination and catalytic activation. These findings provide key insights into the molecular mechanisms of Can2 nucleases in type III CRISPR-Cas immunity and may guide their technological development for nucleic acid detection applications.
    MeSH term(s) Binding Sites ; CRISPR-Associated Proteins/metabolism ; CRISPR-Cas Systems ; Endonucleases/metabolism ; Endoribonucleases/metabolism ; RNA/metabolism ; Second Messenger Systems ; Thermoanaerobacter/enzymology ; Thermoanaerobacter/metabolism
    Chemical Substances CRISPR-Associated Proteins ; Endonucleases (EC 3.1.-) ; Endoribonucleases (EC 3.1.-) ; RNA (63231-63-0)
    Language English
    Publishing date 2023-11-28
    Publishing country England
    Document type Journal Article
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkad1102
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1067: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Article ; Online: Publisher Correction: R-loop formation and conformational activation mechanisms of Cas9.

    Pacesa, Martin / Loeff, Luuk / Querques, Irma / Muckenfuss, Lena M / Sawicka, Marta / Jinek, Martin

    Nature

    2023  Volume 623, Issue 7987, Page(s) E10

    Language English
    Publishing date 2023-11-17
    Publishing country England
    Document type Published Erratum
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-023-06779-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 26: Show issues Location:
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    Zs.MG 9: Show issues
    Zs.MO 244: Show issues

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  8. Article ; Online: Editorial overview: Protein-nucleic acid interactions - cryo-EM, what else?

    Allain, Frédéric H-T / Jinek, Martin

    Current opinion in structural biology

    2019  Volume 59, Page(s) vi–viii

    MeSH term(s) Cryoelectron Microscopy/methods ; Nucleic Acids/chemistry ; Nucleic Acids/metabolism ; Nucleic Acids/ultrastructure ; Protein Binding ; Proteins/chemistry ; Proteins/metabolism ; Proteins/ultrastructure ; Structure-Activity Relationship
    Chemical Substances Nucleic Acids ; Proteins
    Language English
    Publishing date 2019-10-18
    Publishing country England
    Document type Editorial ; Introductory Journal Article
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2019.09.005
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    Zs.A 3206: Show issues Location:
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  9. Article ; Online: An alpha-helical lid guides the target DNA toward catalysis in CRISPR-Cas12a.

    Saha, Aakash / Ahsan, Mohd / Arantes, Pablo R / Schmitz, Michael / Chanez, Christelle / Jinek, Martin / Palermo, Giulia

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 1473

    Abstract: CRISPR-Cas12a is a powerful RNA-guided genome-editing system that generates double-strand DNA breaks using its single RuvC nuclease domain by a sequential mechanism in which initial cleavage of the non-target strand is followed by target strand cleavage. ...

    Abstract CRISPR-Cas12a is a powerful RNA-guided genome-editing system that generates double-strand DNA breaks using its single RuvC nuclease domain by a sequential mechanism in which initial cleavage of the non-target strand is followed by target strand cleavage. How the spatially distant DNA target strand traverses toward the RuvC catalytic core is presently not understood. Here, continuous tens of microsecond-long molecular dynamics and free-energy simulations reveal that an α-helical lid, located within the RuvC domain, plays a pivotal role in the traversal of the DNA target strand by anchoring the crRNA:target strand duplex and guiding the target strand toward the RuvC core, as also corroborated by DNA cleavage experiments. In this mechanism, the REC2 domain pushes the crRNA:target strand duplex toward the core of the enzyme, while the Nuc domain aids the bending and accommodation of the target strand within the RuvC core by bending inward. Understanding of this critical process underlying Cas12a activity will enrich fundamental knowledge and facilitate further engineering strategies for genome editing.
    MeSH term(s) CRISPR-Cas Systems/genetics ; RNA, Guide, CRISPR-Cas Systems ; DNA/genetics ; Gene Editing ; Catalysis
    Chemical Substances RNA, Guide, CRISPR-Cas Systems ; DNA (9007-49-2)
    Language English
    Publishing date 2024-02-17
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-45762-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Target DNA-dependent activation mechanism of the prokaryotic immune system SPARTA.

    Finocchio, Giada / Koopal, Balwina / Potocnik, Ana / Heijstek, Clint / Westphal, Adrie H / Jinek, Martin / Swarts, Daan C

    Nucleic acids research

    2024  Volume 52, Issue 4, Page(s) 2012–2029

    Abstract: In both prokaryotic and eukaryotic innate immune systems, TIR domains function as NADases that degrade the key metabolite NAD+ or generate signaling molecules. Catalytic activation of TIR domains requires oligomerization, but how this is achieved varies ... ...

    Abstract In both prokaryotic and eukaryotic innate immune systems, TIR domains function as NADases that degrade the key metabolite NAD+ or generate signaling molecules. Catalytic activation of TIR domains requires oligomerization, but how this is achieved varies in distinct immune systems. In the Short prokaryotic Argonaute (pAgo)/TIR-APAZ (SPARTA) immune system, TIR NADase activity is triggered upon guide RNA-mediated recognition of invading DNA by an unknown mechanism. Here, we describe cryo-EM structures of SPARTA in the inactive monomeric and target DNA-activated tetrameric states. The monomeric SPARTA structure reveals that in the absence of target DNA, a C-terminal tail of TIR-APAZ occupies the nucleic acid binding cleft formed by the pAgo and TIR-APAZ subunits, inhibiting SPARTA activation. In the active tetrameric SPARTA complex, guide RNA-mediated target DNA binding displaces the C-terminal tail and induces conformational changes in pAgo that facilitate SPARTA-SPARTA dimerization. Concurrent release and rotation of one TIR domain allow it to form a composite NADase catalytic site with the other TIR domain within the dimer, and generate a self-complementary interface that mediates cooperative tetramerization. Combined, this study provides critical insights into the structural architecture of SPARTA and the molecular mechanism underlying target DNA-dependent oligomerization and catalytic activation.
    MeSH term(s) Immune System ; NAD+ Nucleosidase ; Prokaryotic Cells/immunology ; RNA, Guide, CRISPR-Cas Systems ; Signal Transduction ; Eukaryota/immunology ; Immunity, Innate
    Chemical Substances NAD+ Nucleosidase (EC 3.2.2.5) ; RNA, Guide, CRISPR-Cas Systems
    Language English
    Publishing date 2024-01-15
    Publishing country England
    Document type Journal Article
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkad1248
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1067: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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