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  1. Article ; Online: Solving the nuclear pore puzzle.

    Schwartz, Thomas U

    Science (New York, N.Y.)

    2022  Volume 376, Issue 6598, Page(s) 1158–1159

    Abstract: Using a battery of tools, the architecture of the nuclear pore complex is revealed. ...

    Abstract Using a battery of tools, the architecture of the nuclear pore complex is revealed.
    MeSH term(s) Active Transport, Cell Nucleus ; Animals ; Humans ; Nuclear Pore/chemistry ; Nuclear Pore Complex Proteins/chemistry
    Chemical Substances Nuclear Pore Complex Proteins
    Language English
    Publishing date 2022-06-09
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.abq4792
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  2. Article: FHODs: Nuclear tethered formins for nuclear mechanotransduction.

    Antoku, Susumu / Schwartz, Thomas U / Gundersen, Gregg G

    Frontiers in cell and developmental biology

    2023  Volume 11, Page(s) 1160219

    Abstract: In this review, we discuss FHOD formins with a focus on recent studies that reveal a new role for them as critical links for nuclear mechanotransduction. The FHOD family in vertebrates comprises two structurally related proteins, FHOD1 ... ...

    Abstract In this review, we discuss FHOD formins with a focus on recent studies that reveal a new role for them as critical links for nuclear mechanotransduction. The FHOD family in vertebrates comprises two structurally related proteins, FHOD1 and
    Language English
    Publishing date 2023-05-04
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2023.1160219
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  3. Article ; Online: FHODs

    Susumu Antoku / Thomas U. Schwartz / Gregg G. Gundersen

    Frontiers in Cell and Developmental Biology, Vol

    Nuclear tethered formins for nuclear mechanotransduction

    2023  Volume 11

    Abstract: In this review, we discuss FHOD formins with a focus on recent studies that reveal a new role for them as critical links for nuclear mechanotransduction. The FHOD family in vertebrates comprises two structurally related proteins, FHOD1 and FHOD3. Their ... ...

    Abstract In this review, we discuss FHOD formins with a focus on recent studies that reveal a new role for them as critical links for nuclear mechanotransduction. The FHOD family in vertebrates comprises two structurally related proteins, FHOD1 and FHOD3. Their similar biochemical properties suggest overlapping and redundant functions. FHOD1 is widely expressed, FHOD3 less so, with highest expression in skeletal (FHOD1) and cardiac (FHOD3) muscle where specific splice isoforms are expressed. Unlike other formins, FHODs have strong F-actin bundling activity and relatively weak actin polymerization activity. These activities are regulated by phosphorylation by ROCK and Src kinases; bundling is additionally regulated by ERK1/2 kinases. FHODs are unique among formins in their association with the nuclear envelope through direct, high affinity binding to the outer nuclear membrane proteins nesprin-1G and nesprin-2G. Recent crystallographic structures reveal an interaction between a conserved motif in one of the spectrin repeats (SRs) of nesprin-1G/2G and a site adjacent to the regulatory domain in the amino terminus of FHODs. Nesprins are components of the LINC (linker of nucleoskeleton and cytoskeleton) complex that spans both nuclear membranes and mediates bidirectional transmission of mechanical forces between the nucleus and the cytoskeleton. FHODs interact near the actin-binding calponin homology (CH) domains of nesprin-1G/2G enabling a branched connection to actin filaments that presumably strengthens the interaction. At the cellular level, the tethering of FHODs to the outer nuclear membrane mechanically couples perinuclear actin arrays to the nucleus to move and position it in fibroblasts, cardiomyocytes, and potentially other cells. FHODs also function in adhesion maturation during cell migration and in the generation of sarcomeres, activities distant from the nucleus but that are still influenced by it. Human genetic studies have identified multiple FHOD3 variants linked to dilated and hypertrophic cardiomyopathies, ...
    Keywords nucleus ; LINC complex ; FHOD ; formins ; mechanotransduction ; actin filaments ; Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2023-05-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
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  4. Article ; Online: HIV-1 capsids enter the FG phase of nuclear pores like a transport receptor.

    Fu, Liran / Weiskopf, Erika N / Akkermans, Onno / Swanson, Nicholas A / Cheng, Shiya / Schwartz, Thomas U / Görlich, Dirk

    Nature

    2024  Volume 626, Issue 8000, Page(s) 843–851

    Abstract: HIV-1 infection requires nuclear entry of the viral genome. Previous evidence suggests that this entry proceeds through nuclear pore complexes (NPCs), with the 120 × 60 nm capsid squeezing through an approximately 60-nm-wide central ... ...

    Abstract HIV-1 infection requires nuclear entry of the viral genome. Previous evidence suggests that this entry proceeds through nuclear pore complexes (NPCs), with the 120 × 60 nm capsid squeezing through an approximately 60-nm-wide central channel
    MeSH term(s) Humans ; Active Transport, Cell Nucleus ; Capsid/chemistry ; Capsid/metabolism ; Glycine/metabolism ; HIV-1/chemistry ; HIV-1/genetics ; HIV-1/metabolism ; Nuclear Pore/chemistry ; Nuclear Pore/metabolism ; Nuclear Pore/virology ; Nuclear Pore Complex Proteins/chemistry ; Nuclear Pore Complex Proteins/metabolism ; Permeability ; Phenylalanine/metabolism ; Solubility ; Virus Internalization ; Capsid Proteins/chemistry ; Capsid Proteins/metabolism
    Chemical Substances Glycine (TE7660XO1C) ; Nuclear Pore Complex Proteins ; Phenylalanine (47E5O17Y3R) ; Capsid Proteins
    Language English
    Publishing date 2024-01-24
    Publishing country England
    Document type Journal Article
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-023-06966-w
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  5. Article ; Online: The Structure Inventory of the Nuclear Pore Complex.

    Schwartz, Thomas U

    Journal of molecular biology

    2016  Volume 428, Issue 10 Pt A, Page(s) 1986–2000

    Abstract: The nuclear pore complex (NPC) is the principal gateway for molecular exchange between nucleus and cytoplasm across the nuclear envelope. Due to its sheer size of estimated 50-112MDa and its complex buildup from about 500-1000 individual proteins, it is ... ...

    Abstract The nuclear pore complex (NPC) is the principal gateway for molecular exchange between nucleus and cytoplasm across the nuclear envelope. Due to its sheer size of estimated 50-112MDa and its complex buildup from about 500-1000 individual proteins, it is a difficult object to study for structural biologists. Here, I review the extensive ensemble of high-resolution structures of the building blocks of the NPC. Concurrent with the increase in size and complexity, these latest, large structures and assemblies can now be used as the basis for hybrid approaches, primarily in combination with cryo-electron microscopic analysis, generating the first structure-based assembly models of the NPC. Going forward, the structures will be critically important for a detailed analysis of the NPC, including function, evolution, and assembly.
    MeSH term(s) Animals ; Cryoelectron Microscopy/methods ; Cytoplasm/physiology ; Nuclear Pore/physiology
    Language English
    Publishing date 2016-05-22
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2016.03.015
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  6. Article ; Online: Adjuvant and neoadjuvant immunotherapies in hepatocellular carcinoma.

    Llovet, Josep M / Pinyol, Roser / Yarchoan, Mark / Singal, Amit G / Marron, Thomas U / Schwartz, Myron / Pikarsky, Eli / Kudo, Masatoshi / Finn, Richard S

    Nature reviews. Clinical oncology

    2024  Volume 21, Issue 4, Page(s) 294–311

    Abstract: Liver cancer, specifically hepatocellular carcinoma (HCC), is the sixth most common cancer and the third leading cause of cancer mortality worldwide. The development of effective systemic therapies, particularly those involving immune-checkpoint ... ...

    Abstract Liver cancer, specifically hepatocellular carcinoma (HCC), is the sixth most common cancer and the third leading cause of cancer mortality worldwide. The development of effective systemic therapies, particularly those involving immune-checkpoint inhibitors (ICIs), has substantially improved the outcomes of patients with advanced-stage HCC. Approximately 30% of patients are diagnosed with early stage disease and currently receive potentially curative therapies, such as resection, liver transplantation or local ablation, which result in median overall survival durations beyond 60 months. Nonetheless, up to 70% of these patients will have disease recurrence within 5 years of resection or local ablation. To date, the results of randomized clinical trials testing adjuvant therapy in patients with HCC have been negative. This major unmet need has been addressed with the IMbrave 050 trial, demonstrating a recurrence-free survival benefit in patients with a high risk of relapse after resection or local ablation who received adjuvant atezolizumab plus bevacizumab. In parallel, studies testing neoadjuvant ICIs alone or in combination in patients with early stage disease have also reported efficacy. In this Review, we provide a comprehensive overview of the current approaches to manage patients with early stage HCC. We also describe the tumour immune microenvironment and the mechanisms of action of ICIs and cancer vaccines in this setting. Finally, we summarize the available evidence from phase II/III trials of neoadjuvant and adjuvant approaches and discuss emerging clinical trials, identification of biomarkers and clinical trial design considerations for future studies.
    MeSH term(s) Humans ; Carcinoma, Hepatocellular/drug therapy ; Carcinoma, Hepatocellular/pathology ; Liver Neoplasms/drug therapy ; Neoadjuvant Therapy ; Neoplasm Recurrence, Local ; Immunotherapy/methods ; Tumor Microenvironment
    Language English
    Publishing date 2024-02-29
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2491410-1
    ISSN 1759-4782 ; 1759-4774
    ISSN (online) 1759-4782
    ISSN 1759-4774
    DOI 10.1038/s41571-024-00868-0
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  7. Article: Neoadjuvant Immunotherapy for Hepatocellular Carcinoma.

    Marron, Thomas U / Schwartz, Myron / Corbett, Virginia / Merad, Miriam

    Journal of hepatocellular carcinoma

    2022  Volume 9, Page(s) 571–581

    Abstract: The treatment paradigm for hepatocellular carcinoma (HCC) had been stagnant until recently, with new combinations of targeted and immunotherapies entering the first- and second-line setting for patients with advanced disease. This improvement in ... ...

    Abstract The treatment paradigm for hepatocellular carcinoma (HCC) had been stagnant until recently, with new combinations of targeted and immunotherapies entering the first- and second-line setting for patients with advanced disease. This improvement in therapeutic options is well timed given the rise in rates of HCC globally; additionally, screening high-risk patients has also led to an increase in detection of early HCC lesions, identifying patients who can be treated with curative intent approaches such as surgery. Unfortunately, the vast majority of patients who undergo surgical resection develop recurrent HCC, either due to disease recurrence from residual micrometastatic disease or de novo primaries, and there are no perioperative therapies that have demonstrated the ability to significantly improve survival for these patients. Given the survival benefit that immunotherapy has imparted to patients with advanced HCC, and recent studies in other tumor types demonstrating perioperative-in particular neoadjuvant-immunotherapy significantly improves outcomes, there is substantial interest in neoadjuvant immunotherapy for patients with resectable HCC. Three recently reported small studies looking at anti-PD-1 antibodies alone or in combination have demonstrated significant pathologic response to brief pre-operative interventions, and support exploring this approach in larger registrational studies. With these developments the clinical outlook for HCC patients, with both early and advanced disease, is rapidly improving.
    Language English
    Publishing date 2022-06-30
    Publishing country New Zealand
    Document type Journal Article ; Review
    ZDB-ID 2780784-8
    ISSN 2253-5969
    ISSN 2253-5969
    DOI 10.2147/JHC.S340935
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  8. Article ; Online: Finding the missing link.

    Schwartz, Thomas U

    eLife

    2014  Volume 3, Page(s) e03128

    Abstract: The discovery of an ancient protein complex reveals the evolutionary relationships between the proteins that help to form vesicles. ...

    Abstract The discovery of an ancient protein complex reveals the evolutionary relationships between the proteins that help to form vesicles.
    MeSH term(s) Dictyostelium/genetics ; Protein Transport ; Protozoan Proteins/genetics
    Chemical Substances Protozoan Proteins
    Language English
    Publishing date 2014-05-27
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.03128
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  9. Article ; Online: Recombinant Purification of the Periplasmic Portion of the LINC Complex.

    Cruz, Victor E / Schwartz, Thomas U

    Methods in molecular biology (Clifton, N.J.)

    2018  Volume 1840, Page(s) 17–23

    Abstract: Recombinant expression of proteins and their complexes is the routine laboratory procedure to generate pure reagents for biochemical and structural studies. Here we present the standard procedure developed in our lab for the production of milligram ... ...

    Abstract Recombinant expression of proteins and their complexes is the routine laboratory procedure to generate pure reagents for biochemical and structural studies. Here we present the standard procedure developed in our lab for the production of milligram quantities of stoichiometric SUN-KASH complexes. The protocol was specifically developed for the purification of the periplasmic portion of LINC complexes.
    MeSH term(s) Chromatography, Affinity ; Humans ; Multiprotein Complexes/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/isolation & purification ; Nuclear Proteins/metabolism ; Periplasmic Proteins/genetics ; Periplasmic Proteins/isolation & purification ; Proteolysis ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism
    Chemical Substances Multiprotein Complexes ; Nuclear Proteins ; Periplasmic Proteins ; Recombinant Proteins
    Language English
    Publishing date 2018-09-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-8691-0_2
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  10. Article ; Online: Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif.

    Nordeen, Sarah A / Turman, Daniel L / Schwartz, Thomas U

    Nature communications

    2020  Volume 11, Issue 1, Page(s) 6060

    Abstract: The hallmark of the eukaryotic cell is the complex endomembrane system that compartmentalizes cellular functions. Transport into and out of the nucleus occurs through the nuclear pore complex (NPC). The heptameric Nup84 or Y complex is an essential ... ...

    Abstract The hallmark of the eukaryotic cell is the complex endomembrane system that compartmentalizes cellular functions. Transport into and out of the nucleus occurs through the nuclear pore complex (NPC). The heptameric Nup84 or Y complex is an essential scaffolding component of the NPC. Here we report two nanobody-bound structures: the full-length Nup84-Nup133 C-terminal domain complex and the Nup133 N-terminal domain, both from S. cerevisiae. Together with previously published structures, this work enables the structural description of the entire 575 kDa Y complex from one species. The structure of Nup84-Nup133
    MeSH term(s) Amino Acid Motifs ; Cell Membrane/metabolism ; Conserved Sequence ; Humans ; Models, Molecular ; Nuclear Pore Complex Proteins/chemistry ; Nuclear Pore Complex Proteins/metabolism ; Protein Domains ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Sequence Homology, Amino Acid
    Chemical Substances NUP133 protein, S cerevisiae ; NUP84 protein, S cerevisiae ; Nuclear Pore Complex Proteins ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2020-11-27
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-020-19885-5
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