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  1. Book ; Online ; E-Book: Pseudokinases

    Jura, Natalia / Murphy, James M.

    (Issn)

    2022  

    Author's details edited by Natalia Jura and James Murphy
    Series title Issn
    Keywords Protein kinases ; Enzymology
    Subject code 572.792
    Language English
    Size 1 online resource (838 pages)
    Publisher Academic press
    Publishing place Oxford, England ; San Diego, California ; Cambridge, Massachusetts
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 0-323-91542-6 ; 9780323915410 ; 978-0-323-91542-7 ; 0323915418
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Article ; Online: Preface.

    Jura, Natalia / Murphy, James M

    Methods in enzymology

    2022  Volume 667, Page(s) xxi–xxiv

    Language English
    Publishing date 2022-04-13
    Publishing country United States
    Document type Editorial
    ISSN 1557-7988
    ISSN (online) 1557-7988
    DOI 10.1016/S0076-6879(22)00186-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Piquing our interest: Insights into the role of PEAK3 in signaling and disease.

    Paul, Michael D / Torosyan, Hayarpi / Jura, Natalia

    Science signaling

    2022  Volume 15, Issue 722, Page(s) eabm9396

    Abstract: Pseudokinases are critical signaling hubs that are increasingly appreciated as important disease targets. In this issue ... ...

    Abstract Pseudokinases are critical signaling hubs that are increasingly appreciated as important disease targets. In this issue of
    MeSH term(s) Signal Transduction
    Language English
    Publishing date 2022-02-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 2417226-1
    ISSN 1937-9145 ; 1945-0877
    ISSN (online) 1937-9145
    ISSN 1945-0877
    DOI 10.1126/scisignal.abm9396
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Structural dynamics of the active HER4 and HER2/HER4 complexes is finely tuned by different growth factors and glycosylation.

    Trenker, Raphael / Diwanji, Devan / Bingham, Tanner / Verba, Kliment A / Jura, Natalia

    eLife

    2024  Volume 12

    Abstract: Human Epidermal growth factor Receptor 4 (HER4 or ERBB4) carries out essential functions in the development and maintenance of the cardiovascular and nervous systems. HER4 activation is regulated by a diverse group of extracellular ligands including the ... ...

    Abstract Human Epidermal growth factor Receptor 4 (HER4 or ERBB4) carries out essential functions in the development and maintenance of the cardiovascular and nervous systems. HER4 activation is regulated by a diverse group of extracellular ligands including the neuregulin (NRG) family and betacellulin (BTC), which promote HER4 homodimerization or heterodimerization with other HER receptors. Important cardiovascular functions of HER4 are exerted via heterodimerization with its close homolog and orphan receptor, HER2. To date structural insights into ligand-mediated HER4 activation have been limited to crystallographic studies of HER4 ectodomain homodimers in complex with NRG1β. Here, we report cryo-EM structures of near full-length HER2/HER4 heterodimers and full-length HER4 homodimers bound to NRG1β and BTC. We show that the structures of the heterodimers bound to either ligand are nearly identical and that in both cases the HER2/HER4 heterodimer interface is less dynamic than those observed in structures of HER2/EGFR and HER2/HER3 heterodimers. In contrast, structures of full-length HER4 homodimers bound to NRG1β and BTC display more large-scale dynamics mirroring states previously reported for EGFR homodimers. Our structures also reveal the presence of multiple glycan modifications within HER4 ectodomains, modeled for the first time in HER receptors, that distinctively contribute to the stabilization of HER4 homodimer interfaces over those of HER2/HER4 heterodimers.
    MeSH term(s) Humans ; Receptor, ErbB-2/metabolism ; Signal Transduction ; Glycosylation ; Ligands ; Receptor, ErbB-4/metabolism ; Carrier Proteins/metabolism
    Chemical Substances Receptor, ErbB-2 (EC 2.7.10.1) ; Ligands ; Receptor, ErbB-4 (EC 2.7.10.1) ; Carrier Proteins
    Language English
    Publishing date 2024-03-18
    Publishing country England
    Document type Journal Article
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.92873
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Structural dynamics of the active HER4 and HER2/HER4 complexes is finely tuned by different growth factors and glycosylation.

    Trenker, Raphael / Diwanji, Devan / Bingham, Tanner / Verba, Kliment A / Jura, Natalia

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Human Epidermal growth factor Receptor 4 (HER4 or ERBB4) carries out essential functions in the development and maintenance of the cardiovascular and nervous systems. HER4 activation is regulated by a diverse group of extracellular ligands including the ... ...

    Abstract Human Epidermal growth factor Receptor 4 (HER4 or ERBB4) carries out essential functions in the development and maintenance of the cardiovascular and nervous systems. HER4 activation is regulated by a diverse group of extracellular ligands including the neuregulin (NRG) family and betacellulin (BTC), which promote HER4 homodimerization or heterodimerization with other HER receptors. Important cardiovascular functions of HER4 are exerted via heterodimerization with its close homolog and orphan receptor, HER2. To date structural insights into ligand-mediated HER4 activation have been limited to crystallographic studies of HER4 ectodomain homodimers in complex with NRG1β. Here we report cryo-EM structures of near full-length HER2/HER4 heterodimers and full-length HER4 homodimers bound to NRG1β and BTC. We show that the structures of the heterodimers bound to either ligand are nearly identical and that in both cases the HER2/HER4 heterodimer interface is less dynamic than those observed in structures of HER2/EGFR and HER2/HER3 heterodimers. In contrast, structures of full-length HER4 homodimers bound to NRG1β and BTC display more large-scale dynamics mirroring states previously reported for EGFR homodimers. Our structures also reveal the presence of multiple glycan modifications within HER4 ectodomains, modeled for the first time in HER receptors, that distinctively contribute to the stabilization of HER4 homodimer interfaces over those of HER2/HER4 heterodimers.
    Language English
    Publishing date 2024-01-04
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.10.06.561161
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Trapping Tribbles: Nanobody-assisted structure of the TRIB2 pseudokinase.

    Santana, Frederick R / Linossi, Edmond M / Jura, Natalia

    Structure (London, England : 1993)

    2022  Volume 30, Issue 11, Page(s) 1465–1467

    Abstract: TRIB2, a member of the human Tribbles pseudokinase family, functions as a molecular scaffold in diverse signaling pathways. In this issue of Structure, Jamieson et al. report the first high-resolution structure of TRIB2 bound to a nanobody that offers ... ...

    Abstract TRIB2, a member of the human Tribbles pseudokinase family, functions as a molecular scaffold in diverse signaling pathways. In this issue of Structure, Jamieson et al. report the first high-resolution structure of TRIB2 bound to a nanobody that offers insights into its "active-like" state.
    MeSH term(s) Humans ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Protein Serine-Threonine Kinases/genetics ; Signal Transduction
    Chemical Substances Calcium-Calmodulin-Dependent Protein Kinases (EC 2.7.11.17) ; Intracellular Signaling Peptides and Proteins ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; TRIB2 protein, human (EC 2.7.11.17)
    Language English
    Publishing date 2022-11-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2022.10.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4141: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Article: Selected transgenic murine models of human autoimmune liver diseases.

    Trzos, Katarzyna / Pydyn, Natalia / Jura, Jolanta / Kotlinowski, Jerzy

    Pharmacological reports : PR

    2022  Volume 74, Issue 2, Page(s) 263–272

    Abstract: Murine models of human diseases are of outmost importance for both studying molecular mechanisms driving their development and testing new treatment strategies. In this review, we first discuss the etiology and risk factors for autoimmune liver disease, ... ...

    Abstract Murine models of human diseases are of outmost importance for both studying molecular mechanisms driving their development and testing new treatment strategies. In this review, we first discuss the etiology and risk factors for autoimmune liver disease, including primary biliary cholangitis, autoimmune hepatitis and primary sclerosing cholangitis. Second, we highlight important features of murine transgenic models that make them useful for basic scientists, drug developers and clinical researchers. Next, a brief description of each disease is followed by the characterization of selected animal models.
    MeSH term(s) Animals ; Autoimmune Diseases/genetics ; Disease Models, Animal ; Hepatitis, Autoimmune/genetics ; Humans ; Liver Diseases/genetics ; Mice ; Risk Factors
    Language English
    Publishing date 2022-01-15
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2186248-5
    ISSN 1734-1140
    ISSN 1734-1140
    DOI 10.1007/s43440-021-00351-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 861: 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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  8. Article ; Online: Receptor tyrosine kinase activation: From the ligand perspective.

    Trenker, Raphael / Jura, Natalia

    Current opinion in cell biology

    2020  Volume 63, Page(s) 174–185

    Abstract: Receptor tyrosine kinases (RTKs) are single-span transmembrane receptors in which relatively conserved intracellular kinase domains are coupled to divergent extracellular modules. The extracellular domains initiate receptor signaling upon binding to ... ...

    Abstract Receptor tyrosine kinases (RTKs) are single-span transmembrane receptors in which relatively conserved intracellular kinase domains are coupled to divergent extracellular modules. The extracellular domains initiate receptor signaling upon binding to either soluble or membrane-embedded ligands. The diversity of extracellular domain structures allows for coupling of many unique signaling inputs to intracellular tyrosine phosphorylation. The combinatorial power of this receptor system is further increased by the fact that multiple ligands can typically interact with the same receptor. Such ligands often act as biased agonists and initiate distinct signaling responses via activation of the same receptor. Mechanisms behind such biased agonism are largely unknown for RTKs, especially at the level of receptor-ligand complex structure. Using recent progress in understanding the structures of active RTK signaling units, we discuss selected mechanisms by which ligands couple receptor activation to distinct signaling outputs.
    MeSH term(s) Animals ; Cell Membrane/drug effects ; Cell Membrane/metabolism ; Enzyme Activation/drug effects ; Humans ; Ligands ; Phosphorylation ; Receptor Protein-Tyrosine Kinases/agonists ; Receptor Protein-Tyrosine Kinases/chemistry ; Receptor Protein-Tyrosine Kinases/metabolism ; Signal Transduction/drug effects ; Signal Transduction/physiology
    Chemical Substances Ligands ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1)
    Language English
    Publishing date 2020-02-27
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2020.01.016
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2963: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  9. Article ; Online: Mutant HER2 needs mutant HER3 to be an effective oncogene.

    Trenker, Raphael / Diwanji, Devan / Jura, Natalia

    Cell reports. Medicine

    2021  Volume 2, Issue 8, Page(s) 100361

    Abstract: Hanker et al. reveal that co-occurring missense mutations in the human epidermal growth factor receptor 2 (HER2) and its catalytically inactive homolog HER3 synergize to promote oncogenic signaling by the HER2/HER3 complex. ...

    Abstract Hanker et al. reveal that co-occurring missense mutations in the human epidermal growth factor receptor 2 (HER2) and its catalytically inactive homolog HER3 synergize to promote oncogenic signaling by the HER2/HER3 complex.
    Language English
    Publishing date 2021-08-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ISSN 2666-3791
    ISSN (online) 2666-3791
    DOI 10.1016/j.xcrm.2021.100361
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Efficient expression, purification, and visualization by cryo-EM of unliganded near full-length HER3.

    Diwanji, Devan / Trenker, Raphael / Jura, Natalia / Verba, Kliment A

    Methods in enzymology

    2022  Volume 667, Page(s) 611–632

    Abstract: Biochemical analyses of membrane receptor kinases have been limited by challenges in obtaining sufficient homogeneous receptor samples for downstream structural and biophysical characterization. Here, we report a suite of methods for the efficient ... ...

    Abstract Biochemical analyses of membrane receptor kinases have been limited by challenges in obtaining sufficient homogeneous receptor samples for downstream structural and biophysical characterization. Here, we report a suite of methods for the efficient expression, purification, and visualization by cryo-electron microscopy (cryo-EM) of near full-length Human Epidermal Growth Factor Receptor 3 (HER3), a receptor tyrosine pseudokinase, in the unliganded state. Through transient mammalian cell expression, a two-step purification with detergent exchange into lauryl maltose neopentyl glycol (LMNG), and freezing devoid of background detergent micelle, we obtained ~6Å reconstructions of the ~60kDa fully-glycosylated unliganded extracellular domain of HER3 from just 30mL of suspension culture. The reconstructions reveal previously unappreciated extracellular domain dynamics and glycosylation sites.
    MeSH term(s) Animals ; Cryoelectron Microscopy/methods ; Detergents ; Humans ; Mammals ; Micelles
    Chemical Substances Detergents ; Micelles
    Language English
    Publishing date 2022-04-05
    Publishing country United States
    Document type Journal Article
    ISSN 1557-7988
    ISSN (online) 1557-7988
    DOI 10.1016/bs.mie.2022.03.048
    Database MEDical Literature Analysis and Retrieval System OnLINE

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