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  1. Article ; Online: PAR2 biased signaling on the move.

    Nieman, Marvin T

    Blood

    2024  Volume 143, Issue 10, Page(s) 835–836

    MeSH term(s) Factor VIIa ; Monocytes
    Chemical Substances Factor VIIa (EC 3.4.21.21)
    Language English
    Publishing date 2024-03-07
    Publishing country United States
    Document type Editorial ; Comment
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood.2023023489
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Book ; Online ; Conference proceedings: Proceedings of KININ2018CLE, Cleveland, Ohio, June 18-20, 2018: A Compendium of the Presentations

    Schmaier, Alvin H. / Nieman, Marvin T. / McCrae, Keith / Karnik, Sadashiva / Bosco Pesquero, Joao

    2020  

    Keywords Medicine ; bradykinin ; factor XII ; kallikrein ; renin ; angiotensin
    Size 1 electronic resource (147 pages)
    Publisher Frontiers Media SA
    Document type Book ; Online ; Conference proceedings
    Note English ; Open Access
    HBZ-ID HT021230514
    ISBN 9782889633326 ; 2889633322
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  3. Article ; Online: Flipping the script: defining the reversibility of platelet activation.

    Nieman, Marvin T / Neeves, Keith B

    Journal of thrombosis and haemostasis : JTH

    2023  Volume 21, Issue 5, Page(s) 1102–1103

    MeSH term(s) Humans ; Platelet Activation
    Language English
    Publishing date 2023-04-28
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 2112661-6
    ISSN 1538-7836 ; 1538-7933
    ISSN (online) 1538-7836
    ISSN 1538-7933
    DOI 10.1016/j.jtha.2023.02.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MO 295: Show issues

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  4. Article ; Online: RAPid signaling in platelets.

    Nieman, Marvin T

    Blood

    2018  Volume 132, Issue 18, Page(s) 1864–1865

    MeSH term(s) Animals ; Blood Platelets ; Mice ; Protein Isoforms ; Signal Transduction ; Thrombopoiesis
    Chemical Substances Protein Isoforms
    Language English
    Publishing date 2018-10-31
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood-2018-09-872093
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: The domino effect triggered by the tethered ligand of the protease activated receptors.

    Han, Xu / Nieman, Marvin T

    Thrombosis research

    2020  Volume 196, Page(s) 87–98

    Abstract: Protease activated receptors (PARs) are G-protein coupled receptors (GPCRs) that have a unique activation mechanism. Unlike other GPCRs that can be activated by free ligands, under physiological conditions, PARs are activated by the tethered ligand, ... ...

    Abstract Protease activated receptors (PARs) are G-protein coupled receptors (GPCRs) that have a unique activation mechanism. Unlike other GPCRs that can be activated by free ligands, under physiological conditions, PARs are activated by the tethered ligand, which is a part of their N-terminus that is unmasked by proteolysis. It has been 30 years since the first member of the family, PAR1, was identified. In this review, we will discuss this unique tethered ligand mediate receptor activation of PARs in detail: how they interact with the proteases, the complex structural rearrangement of the receptors upon activation, and the termination of the signaling. We also summarize the structural studies of the PARs and how single nucleotide polymorphisms impact the receptor reactivity. Finally, we review the current strategies for inhibiting PAR function with therapeutic targets for anti-thrombosis. The focus of this review is PAR1 and PAR4 as they are the thrombin signal mediators on human platelets and therapeutics targets. We also include the structural studies of PAR2 as it informs the mechanism of action for PARs in general.
    MeSH term(s) Humans ; Ligands ; Receptor, PAR-1/genetics ; Receptors, G-Protein-Coupled ; Receptors, Proteinase-Activated ; Receptors, Thrombin ; Signal Transduction ; Thrombin/metabolism
    Chemical Substances Ligands ; Receptor, PAR-1 ; Receptors, G-Protein-Coupled ; Receptors, Proteinase-Activated ; Receptors, Thrombin ; Thrombin (EC 3.4.21.5)
    Language English
    Publishing date 2020-08-04
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 121852-9
    ISSN 1879-2472 ; 0049-3848
    ISSN (online) 1879-2472
    ISSN 0049-3848
    DOI 10.1016/j.thromres.2020.08.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Protease-activated receptors in hemostasis.

    Nieman, Marvin T

    Blood

    2016  Volume 128, Issue 2, Page(s) 169–177

    Abstract: Protease signaling in cells elicits multiple physiologically important responses via protease-activated receptors (PARs). There are 4 members of this family of G-protein-coupled receptors (PAR1-4). PARs are activated by proteolysis of the N terminus to ... ...

    Abstract Protease signaling in cells elicits multiple physiologically important responses via protease-activated receptors (PARs). There are 4 members of this family of G-protein-coupled receptors (PAR1-4). PARs are activated by proteolysis of the N terminus to reveal a tethered ligand. The rate-limiting step of PAR signaling is determined by the efficiency of proteolysis of the N terminus, which is regulated by allosteric binding sites, cofactors, membrane localization, and receptor dimerization. This ultimately controls the initiation of PAR signaling. In addition, these factors also control the cellular response by directing signaling toward G-protein or β-arrestin pathways. PAR1 signaling on endothelial cells is controlled by the activating protease and heterodimerization with PAR2 or PAR3. As a consequence, the genetic and epigenetic control of PARs and their cofactors in physiologic and pathophysiologic conditions have the potential to influence cellular behavior. Recent studies have uncovered polymorphisms that result in PAR4 sequence variants with altered reactivity that interact to influence platelet response. This further demonstrates how interactions within the plasma membrane can control the physiological output. Understanding the structural rearrangement following PAR activation and how PARs are allosterically controlled within the plasma membrane will determine how best to target this family of receptors therapeutically. The purpose of this article is to review how signaling from PARs is influenced by alternative cleavage sites and the physical interactions within the membrane. Going forward, it will be important to relate the altered signaling to the molecular arrangement of PARs in the cell membrane and to determine how these may be influenced genetically.
    MeSH term(s) Cell Membrane/metabolism ; Endothelial Cells/metabolism ; Hemostasis/physiology ; Protein Multimerization/physiology ; Receptors, Proteinase-Activated/metabolism ; Signal Transduction/physiology
    Chemical Substances Receptors, Proteinase-Activated
    Language English
    Publishing date 2016-04-28
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood-2015-11-636472
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: PARtitioning protease signaling.

    Nieman, Marvin T

    Blood

    2015  Volume 125, Issue 12, Page(s) 1853–1855

    Abstract: In this issue of Blood, Aisiku et al describe a novel class of protease-activated receptor-1 (PAR1) inhibitors that block proinflammatory pathways but spare cytoprotective signaling in endothelial cells. These compounds, parmodulins, target the ... ...

    Abstract In this issue of Blood, Aisiku et al describe a novel class of protease-activated receptor-1 (PAR1) inhibitors that block proinflammatory pathways but spare cytoprotective signaling in endothelial cells. These compounds, parmodulins, target the cytoplasmic face of PAR1, where they selectively interfere with Gαq, but not Gα12/13. This strategy of blocking specific pathways provides the ability to modulate the activity of receptors with multiple functions (such as PAR1) and may have therapeutic advantages.
    MeSH term(s) Animals ; Endothelium, Vascular/injuries ; Humans ; Lactones/adverse effects ; Pyridines/adverse effects ; Receptor, PAR-1/antagonists & inhibitors ; Thrombosis/drug therapy ; Thrombosis/prevention & control
    Chemical Substances Lactones ; Pyridines ; Receptor, PAR-1 ; vorapaxar (ZCE93644N2)
    Language English
    Publishing date 2015-03-18
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood-2015-01-623835
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Protease activated receptor 4: a backup receptor or a dark horse as a target in antiplatelet therapy?

    Han, Xu / Nieman, Marvin T

    Annals of translational medicine

    2017  Volume 6, Issue 3, Page(s) 56

    Language English
    Publishing date 2017-12-18
    Publishing country China
    Document type Editorial ; Comment
    ZDB-ID 2893931-1
    ISSN 2305-5847 ; 2305-5839
    ISSN (online) 2305-5847
    ISSN 2305-5839
    DOI 10.21037/atm.2017.11.36
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: PAR4 (Protease-Activated Receptor 4): PARticularly Important 4 Antiplatelet Therapy.

    Han, Xu / Nieman, Marvin T

    Arteriosclerosis, thrombosis, and vascular biology

    2017  Volume 38, Issue 2, Page(s) 287–289

    MeSH term(s) Humans ; Platelet Aggregation Inhibitors ; Receptors, Thrombin ; Thrombosis
    Chemical Substances Platelet Aggregation Inhibitors ; Receptors, Thrombin ; protease-activated receptor 4 (JWE1M73YZN)
    Language English
    Publishing date 2017-12-27
    Publishing country United States
    Document type Editorial ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 1221433-4
    ISSN 1524-4636 ; 1079-5642
    ISSN (online) 1524-4636
    ISSN 1079-5642
    DOI 10.1161/ATVBAHA.117.310550
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Protease-activated receptors: An illustrated review.

    Han, Xu / Nieman, Marvin T / Kerlin, Bryce A

    Research and practice in thrombosis and haemostasis

    2020  Volume 5, Issue 1, Page(s) 17–26

    Abstract: Proteases are important regulators of cell behavior, survival, and apoptosis. They communicate to cells directly through a special class of G-protein-coupled receptors known as protease-activated receptors (PARs). N-terminal PAR proteolysis unmasks a neo- ...

    Abstract Proteases are important regulators of cell behavior, survival, and apoptosis. They communicate to cells directly through a special class of G-protein-coupled receptors known as protease-activated receptors (PARs). N-terminal PAR proteolysis unmasks a neo-N-terminus, which serves as a tethered ligand to activate PARs. Using this unique irreversible activation mechanism, PARs relay information across cell membranes. The year 2020 is the 30th year since discovery of the first member of this family, PAR1. In this illustrated review, we highlight achievements in the PAR field over the past 3 decades. Additionally, the known expression profiles of PARs in human tissues and across species are portrayed. We also illustrate the tethered ligand activation mechanism, which is unique to PARs, and PAR regulatory mechanisms. PAR1 was originally named "thrombin receptor" because thrombin was the first protease identified to activate PAR1. However, over the past 30 years, a growing number of proteases have been found to cleave PARs and trigger differential downstream signaling depending on cleavage site, cell type, and species. We exemplify the diversity of PAR1-mediated signaling outcomes in platelets and endothelial cells as pertinent examples to the hemostasis, thrombosis, and vascular biology fields. Further, the termination and regulation of PAR signaling via endocytosis and currently available pharmacologic approaches are depicted. We conclude with portrayal of clinically translational aspects of PAR biology including pharmacologic manipulation and single-nucleotide polymorphisms.
    Language English
    Publishing date 2020-12-06
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 2475-0379
    ISSN (online) 2475-0379
    DOI 10.1002/rth2.12454
    Database MEDical Literature Analysis and Retrieval System OnLINE

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