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  1. AU="Aziz, Masood"
  2. AU="Piovanello, Fabio"
  3. AU="Norman, Aurora"
  4. AU="Zoumpourlis, Vassilis"
  5. AU="Coleman-McCray, Joann D"
  6. AU="Carroll, Kaitlin M"
  7. AU="Zhu, Wen-Yi"
  8. AU="Bartolomé-Comas, Rosa"
  9. AU="Mathew, Josey"
  10. AU="Ali A. Shati"
  11. AU="Tavares, Guilherme M"
  12. AU="Deoni, Sean"
  13. AU="Byrne, Michael E"
  14. AU=Edwards Adrianne N.
  15. AU=Mehr Reyhaneh Niayesh
  16. AU="Par-Young, Jennefer"
  17. AU="Yon, Yongjie"
  18. AU="Laisi, Arttu"
  19. AU="Huang, Haibing"
  20. AU="Volk, Michelle"
  21. AU="Zijlstra, J. G."
  22. AU="Aditya Narayan"
  23. AU="Soliño, S. López"
  24. AU="Bervoets, Lieven"
  25. AU=Perween Reshma AU=Perween Reshma
  26. AU="Wang, Zhenduo"

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  1. Artikel ; Online: Talin and kindlin use integrin tail allostery and direct binding to activate integrins.

    Aretz, Jonas / Aziz, Masood / Strohmeyer, Nico / Sattler, Michael / Fässler, Reinhard

    Nature structural & molecular biology

    2023  Band 30, Heft 12, Seite(n) 1913–1924

    Abstract: Integrin affinity regulation, also termed integrin activation, is essential for metazoan life. Although talin and kindlin binding to the β-integrin cytoplasmic tail is indispensable for integrin activation, it is unknown how they achieve this function. ... ...

    Abstract Integrin affinity regulation, also termed integrin activation, is essential for metazoan life. Although talin and kindlin binding to the β-integrin cytoplasmic tail is indispensable for integrin activation, it is unknown how they achieve this function. By combining NMR, biochemistry and cell biology techniques, we found that talin and kindlin binding to the β-tail can induce a conformational change that increases talin affinity and decreases kindlin affinity toward it. We also discovered that this asymmetric affinity regulation is accompanied by a direct interaction between talin and kindlin, which promotes simultaneous binding of talin and kindlin to β-tails. Disrupting allosteric communication between the β-tail-binding sites of talin and kindlin or their direct interaction in cells severely compromised integrin functions. These data show how talin and kindlin cooperate to generate a small but critical population of ternary talin-β-integrin-kindlin complexes with high talin-integrin affinity and high dynamics.
    Mesh-Begriff(e) Animals ; Talin/chemistry ; Talin/metabolism ; Integrins/metabolism ; Binding Sites ; Protein Binding
    Chemische Substanzen Talin ; Integrins
    Sprache Englisch
    Erscheinungsdatum 2023-12-12
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-023-01139-9
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Kinetic FRET Assay to Measure Binding-Induced Conformational Changes of Nucleic Acids.

    Higuera-Rodriguez, R Anahi / De Pascali, Mareike C / Aziz, Masood / Sattler, Michael / Rant, Ulrich / Kaiser, Wolfgang

    ACS sensors

    2023  Band 8, Heft 12, Seite(n) 4597–4606

    Abstract: The interaction of small molecules or proteins with RNA or DNA often involves changes in the nucleic acid (NA) folding and structure. A biophysical characterization of these processes helps us to understand the underlying molecular mechanisms. Here, we ... ...

    Abstract The interaction of small molecules or proteins with RNA or DNA often involves changes in the nucleic acid (NA) folding and structure. A biophysical characterization of these processes helps us to understand the underlying molecular mechanisms. Here, we propose kinFRET (kinetics Förster resonance energy transfer), a real-time ensemble FRET methodology to measure binding and folding kinetics. With kinFRET, the kinetics of conformational changes of NAs (DNA or RNA) upon analyte binding can be directly followed via a FRET signal using a chip-based biosensor. We demonstrate the utility of this approach with two representative examples. First, we monitored the conformational changes of different formats of an aptamer (MN19) upon interaction with small-molecule analytes. Second, we characterized the binding kinetics of RNA recognition by tandem K homology (KH) domains of the human insulin-like growth factor II mRNA-binding protein 3 (IMP3), which reveals distinct kinetic contributions of the two KH domains. Our data demonstrate that kinFRET is well suited to study the kinetics and conformational changes of NA-analyte interactions.
    Mesh-Begriff(e) Humans ; Fluorescence Resonance Energy Transfer/methods ; Nucleic Acids ; RNA/chemistry ; Proteins ; DNA/chemistry
    Chemische Substanzen Nucleic Acids ; RNA (63231-63-0) ; Proteins ; DNA (9007-49-2)
    Sprache Englisch
    Erscheinungsdatum 2023-12-07
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 2379-3694
    ISSN (online) 2379-3694
    DOI 10.1021/acssensors.3c01527
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Combinatorial recognition of clustered RNA elements by the multidomain RNA-binding protein IMP3.

    Schneider, Tim / Hung, Lee-Hsueh / Aziz, Masood / Wilmen, Anna / Thaum, Stephanie / Wagner, Jacqueline / Janowski, Robert / Müller, Simon / Schreiner, Silke / Friedhoff, Peter / Hüttelmaier, Stefan / Niessing, Dierk / Sattler, Michael / Schlundt, Andreas / Bindereif, Albrecht

    Nature communications

    2019  Band 10, Heft 1, Seite(n) 2266

    Abstract: How multidomain RNA-binding proteins recognize their specific target sequences, based on a combinatorial code, represents a fundamental unsolved question and has not been studied systematically so far. Here we focus on a prototypical multidomain RNA- ... ...

    Abstract How multidomain RNA-binding proteins recognize their specific target sequences, based on a combinatorial code, represents a fundamental unsolved question and has not been studied systematically so far. Here we focus on a prototypical multidomain RNA-binding protein, IMP3 (also called IGF2BP3), which contains six RNA-binding domains (RBDs): four KH and two RRM domains. We establish an integrative systematic strategy, combining single-domain-resolved SELEX-seq, motif-spacing analyses, in vivo iCLIP, functional validation assays, and structural biology. This approach identifies the RNA-binding specificity and RNP topology of IMP3, involving all six RBDs and a cluster of up to five distinct and appropriately spaced CA-rich and GGC-core RNA elements, covering a >100 nucleotide-long target RNA region. Our generally applicable approach explains both specificity and flexibility of IMP3-RNA recognition, allows the prediction of IMP3 targets, and provides a paradigm for the function of multivalent interactions with multidomain RNA-binding proteins in gene regulation.
    Mesh-Begriff(e) Gene Expression Regulation/physiology ; High-Throughput Nucleotide Sequencing/methods ; Models, Molecular ; Protein Binding/physiology ; RNA, Messenger/chemistry ; RNA, Messenger/metabolism ; RNA-Binding Motifs/physiology ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/isolation & purification ; RNA-Binding Proteins/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; SELEX Aptamer Technique ; Sequence Analysis, DNA/methods
    Chemische Substanzen IGF2BP3 protein, human ; RNA, Messenger ; RNA-Binding Proteins ; Recombinant Proteins
    Sprache Englisch
    Erscheinungsdatum 2019-05-22
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-019-09769-8
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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