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  1. Article ; Online: The Burden of Cardiovascular Disease in the Post-COVID Era.

    Liu, Justin / Cepeda, Maria / Frangaj, Brulinda / Shimbo, Daichi

    Primary care

    2023  Volume 51, Issue 1, Page(s) 1–11

    Abstract: In 2019, before the COVID-19 pandemic, cardiovascular disease (CVD) was the leading cause of death. Since 2020, the pandemic has had far-reaching effects on the landscape of health care including CVD prevention and management. Recent decreases in life ... ...

    Abstract In 2019, before the COVID-19 pandemic, cardiovascular disease (CVD) was the leading cause of death. Since 2020, the pandemic has had far-reaching effects on the landscape of health care including CVD prevention and management. Recent decreases in life expectancy in the United States could potentially be explained by issues related to disruptions in CVD prevention and control of CVD risk factors from the COVID-19 pandemic. This article reviews the effects of the SARS-CoV-2 virus and the accompanying pandemic on CVD risk factor prevention and management in the United States. Potential solutions are also proposed for these patients.
    MeSH term(s) Humans ; United States/epidemiology ; Cardiovascular Diseases/epidemiology ; Cardiovascular Diseases/prevention & control ; Cardiovascular Diseases/etiology ; COVID-19 ; SARS-CoV-2 ; Pandemics ; Risk Factors
    Language English
    Publishing date 2023-09-01
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 604005-6
    ISSN 1558-299X ; 0095-4543
    ISSN (online) 1558-299X
    ISSN 0095-4543
    DOI 10.1016/j.pop.2023.08.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1154: 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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  2. Article ; Online: Regulated interaction of ID2 with the anaphase-promoting complex links progression through mitosis with reactivation of cell-type-specific transcription.

    Lee, Sang Bae / Garofano, Luciano / Ko, Aram / D'Angelo, Fulvio / Frangaj, Brulinda / Sommer, Danika / Gan, Qiwen / Kim, KyeongJin / Cardozo, Timothy / Iavarone, Antonio / Lasorella, Anna

    Nature communications

    2022  Volume 13, Issue 1, Page(s) 2089

    Abstract: Tissue-specific transcriptional activity is silenced in mitotic cells but it remains unclear whether the mitotic regulatory machinery interacts with tissue-specific transcriptional programs. We show that such cross-talk involves the controlled ... ...

    Abstract Tissue-specific transcriptional activity is silenced in mitotic cells but it remains unclear whether the mitotic regulatory machinery interacts with tissue-specific transcriptional programs. We show that such cross-talk involves the controlled interaction between core subunits of the anaphase-promoting complex (APC) and the ID2 substrate. The N-terminus of ID2 is independently and structurally compatible with a pocket composed of core APC/C subunits that may optimally orient ID2 onto the APC
    MeSH term(s) Anaphase ; Anaphase-Promoting Complex-Cyclosome/genetics ; Cell Cycle Proteins/metabolism ; Mitosis ; Serine
    Chemical Substances Cell Cycle Proteins ; Serine (452VLY9402) ; Anaphase-Promoting Complex-Cyclosome (EC 2.3.2.27)
    Language English
    Publishing date 2022-04-19
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; 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/s41467-022-29502-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Proline Hydroxylation Primes Protein Kinases for Autophosphorylation and Activation

    Lee, Sang Bae / Ko, Aram / Oh, Young Taek / Shi, Peiguo / D’Angelo, Fulvio / Frangaj, Brulinda / Koller, Antonius / Chen, Emily I / Cardozo, Timothy / Iavarone, Antonio / Lasorella, Anna

    Molecular cell. 2020 Aug. 06, v. 79, no. 3

    2020  

    Abstract: Activation of dual-specificity tyrosine-phosphorylation-regulated kinases 1A and 1B (DYRK1A and DYRK1B) requires prolyl hydroxylation by PHD1 prolyl hydroxylase. Prolyl hydroxylation of DYRK1 initiates a cascade of events leading to the release of ... ...

    Abstract Activation of dual-specificity tyrosine-phosphorylation-regulated kinases 1A and 1B (DYRK1A and DYRK1B) requires prolyl hydroxylation by PHD1 prolyl hydroxylase. Prolyl hydroxylation of DYRK1 initiates a cascade of events leading to the release of molecular constraints on von Hippel-Lindau (VHL) ubiquitin ligase tumor suppressor function. However, the proline residue of DYRK1 targeted by hydroxylation and the role of prolyl hydroxylation in tyrosine autophosphorylation of DYRK1 are unknown. We found that a highly conserved proline in the CMGC insert of the DYRK1 kinase domain is hydroxylated by PHD1, and this event precedes tyrosine autophosphorylation. Mutation of the hydroxylation acceptor proline precludes tyrosine autophosphorylation and folding of DYRK1, resulting in a kinase unable to preserve VHL function and lacking glioma suppression activity. The consensus proline sequence is shared by most CMGC kinases, and prolyl hydroxylation is essential for catalytic activation. Thus, formation of prolyl-hydroxylated intermediates is a novel mechanism of kinase maturation and likely a general mechanism of regulation of CMGC kinases in eukaryotes.
    Keywords catalytic activity ; eukaryotic cells ; glioma ; hydroxylation ; mutation ; procollagen-proline dioxygenase ; proline ; protein kinases ; protein phosphorylation ; tyrosine ; ubiquitin-protein ligase
    Language English
    Dates of publication 2020-0806
    Size p. 376-389.e8.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2020.06.021
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2005/501: Show issues

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  4. Article ; Online: LZTR1 Mutation Mediates Oncogenesis through Stabilization of EGFR and AXL.

    Ko, Aram / Hasanain, Mohammad / Oh, Young Taek / D'Angelo, Fulvio / Sommer, Danika / Frangaj, Brulinda / Tran, Suzanne / Bielle, Franck / Pollo, Bianca / Paterra, Rosina / Mokhtari, Karima / Soni, Rajesh Kumar / Peyre, Matthieu / Eoli, Marica / Papi, Laura / Kalamarides, Michel / Sanson, Marc / Iavarone, Antonio / Lasorella, Anna

    Cancer discovery

    2022  Volume 13, Issue 3, Page(s) 702–723

    Abstract: LZTR1 is the substrate-specific adaptor of a CUL3-dependent ubiquitin ligase frequently mutated in sporadic and syndromic cancer. We combined biochemical and genetic studies to identify LZTR1 substrates and interrogated their tumor-driving function in ... ...

    Abstract LZTR1 is the substrate-specific adaptor of a CUL3-dependent ubiquitin ligase frequently mutated in sporadic and syndromic cancer. We combined biochemical and genetic studies to identify LZTR1 substrates and interrogated their tumor-driving function in the context of LZTR1 loss-of-function mutations. Unbiased screens converged on EGFR and AXL receptor tyrosine kinases as LZTR1 interactors targeted for ubiquitin-dependent degradation in the lysosome. Pathogenic cancer-associated mutations of LZTR1 failed to promote EGFR and AXL degradation, resulting in dysregulated growth factor signaling. Conditional inactivation of Lztr1 and Cdkn2a in the mouse nervous system caused tumors in the peripheral nervous system including schwannoma-like tumors, thus recapitulating aspects of schwannomatosis, the prototype tumor predisposition syndrome sustained by LZTR1 germline mutations. Lztr1- and Cdkn2a-deleted tumors aberrantly accumulated EGFR and AXL and exhibited specific vulnerability to EGFR and AXL coinhibition. These findings explain tumorigenesis by LZTR1 inactivation and offer therapeutic opportunities to patients with LZTR1-mutant cancer.
    Significance: EGFR and AXL are substrates of LZTR1-CUL3 ubiquitin ligase. The frequent somatic and germline mutations of LZTR1 in human cancer cause EGFR and AXL accumulation and deregulated signaling. LZTR1-mutant tumors show vulnerability to concurrent inhibition of EGFR and AXL, thus providing precision targeting to patients affected by LZTR1-mutant cancer. This article is highlighted in the In This Issue feature, p. 517.
    MeSH term(s) Animals ; Humans ; Mice ; Carcinogenesis ; Cell Transformation, Neoplastic ; ErbB Receptors/genetics ; Mutation ; Neurilemmoma/genetics ; Neurilemmoma/metabolism ; Neurilemmoma/pathology ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Ubiquitins/genetics
    Chemical Substances EGFR protein, human (EC 2.7.10.1) ; ErbB Receptors (EC 2.7.10.1) ; LZTR1 protein, human ; Transcription Factors ; Ubiquitins
    Language English
    Publishing date 2022-11-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2625242-9
    ISSN 2159-8290 ; 2159-8274
    ISSN (online) 2159-8290
    ISSN 2159-8274
    DOI 10.1158/2159-8290.CD-22-0376
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6916: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Proline Hydroxylation Primes Protein Kinases for Autophosphorylation and Activation.

    Lee, Sang Bae / Ko, Aram / Oh, Young Taek / Shi, Peiguo / D'Angelo, Fulvio / Frangaj, Brulinda / Koller, Antonius / Chen, Emily I / Cardozo, Timothy / Iavarone, Antonio / Lasorella, Anna

    Molecular cell

    2020  Volume 79, Issue 3, Page(s) 376–389.e8

    Abstract: Activation of dual-specificity tyrosine-phosphorylation-regulated kinases 1A and 1B (DYRK1A and DYRK1B) requires prolyl hydroxylation by PHD1 prolyl hydroxylase. Prolyl hydroxylation of DYRK1 initiates a cascade of events leading to the release of ... ...

    Abstract Activation of dual-specificity tyrosine-phosphorylation-regulated kinases 1A and 1B (DYRK1A and DYRK1B) requires prolyl hydroxylation by PHD1 prolyl hydroxylase. Prolyl hydroxylation of DYRK1 initiates a cascade of events leading to the release of molecular constraints on von Hippel-Lindau (VHL) ubiquitin ligase tumor suppressor function. However, the proline residue of DYRK1 targeted by hydroxylation and the role of prolyl hydroxylation in tyrosine autophosphorylation of DYRK1 are unknown. We found that a highly conserved proline in the CMGC insert of the DYRK1 kinase domain is hydroxylated by PHD1, and this event precedes tyrosine autophosphorylation. Mutation of the hydroxylation acceptor proline precludes tyrosine autophosphorylation and folding of DYRK1, resulting in a kinase unable to preserve VHL function and lacking glioma suppression activity. The consensus proline sequence is shared by most CMGC kinases, and prolyl hydroxylation is essential for catalytic activation. Thus, formation of prolyl-hydroxylated intermediates is a novel mechanism of kinase maturation and likely a general mechanism of regulation of CMGC kinases in eukaryotes.
    MeSH term(s) Amino Acid Sequence ; Animals ; Binding Sites ; Brain Neoplasms/genetics ; Brain Neoplasms/metabolism ; Brain Neoplasms/pathology ; Cell Line, Tumor ; Crystallography, X-Ray ; Gene Expression Regulation, Neoplastic ; Glioma/genetics ; Glioma/metabolism ; Glioma/pathology ; HEK293 Cells ; Heterografts ; Humans ; Hydroxylation ; Hypoxia-Inducible Factor-Proline Dioxygenases/genetics ; Hypoxia-Inducible Factor-Proline Dioxygenases/metabolism ; Isoenzymes/chemistry ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Mice ; Mice, Nude ; Mitogen-Activated Protein Kinase 14/chemistry ; Mitogen-Activated Protein Kinase 14/genetics ; Mitogen-Activated Protein Kinase 14/metabolism ; Models, Molecular ; Mutation ; Neuroglia/metabolism ; Neuroglia/pathology ; Phosphorylation ; Proline/metabolism ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Processing, Post-Translational ; Protein Serine-Threonine Kinases/chemistry ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Protein Structure, Secondary ; Protein-Tyrosine Kinases/chemistry ; Protein-Tyrosine Kinases/genetics ; Protein-Tyrosine Kinases/metabolism ; Von Hippel-Lindau Tumor Suppressor Protein/genetics ; Von Hippel-Lindau Tumor Suppressor Protein/metabolism ; Dyrk Kinases
    Chemical Substances Isoenzymes ; Proline (9DLQ4CIU6V) ; EGLN2 protein, human (EC 1.14.11.29) ; Hypoxia-Inducible Factor-Proline Dioxygenases (EC 1.14.11.29) ; Von Hippel-Lindau Tumor Suppressor Protein (EC 2.3.2.27) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Mitogen-Activated Protein Kinase 14 (EC 2.7.11.24) ; VHL protein, human (EC 6.3.2.-)
    Language English
    Publishing date 2020-07-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2020.06.021
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5055: 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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  6. Article ; Online: Pathway-based classification of glioblastoma uncovers a mitochondrial subtype with therapeutic vulnerabilities.

    Garofano, Luciano / Migliozzi, Simona / Oh, Young Taek / D'Angelo, Fulvio / Najac, Ryan D / Ko, Aram / Frangaj, Brulinda / Caruso, Francesca Pia / Yu, Kai / Yuan, Jinzhou / Zhao, Wenting / Di Stefano, Anna Luisa / Bielle, Franck / Jiang, Tao / Sims, Peter / Suvà, Mario L / Tang, Fuchou / Su, Xiao-Dong / Ceccarelli, Michele /
    Sanson, Marc / Lasorella, Anna / Iavarone, Antonio

    Nature cancer

    2021  Volume 2, Issue 2, Page(s) 141–156

    Abstract: The transcriptomic classification of glioblastoma (GBM) has failed to predict survival and therapeutic vulnerabilities. A computational approach for unbiased identification of core biological traits of single cells and bulk tumors uncovered four tumor ... ...

    Abstract The transcriptomic classification of glioblastoma (GBM) has failed to predict survival and therapeutic vulnerabilities. A computational approach for unbiased identification of core biological traits of single cells and bulk tumors uncovered four tumor cell states and GBM subtypes distributed along neurodevelopmental and metabolic axes, classified as proliferative/progenitor, neuronal, mitochondrial and glycolytic/plurimetabolic. Each subtype was enriched with biologically coherent multiomic features. Mitochondrial GBM was associated with the most favorable clinical outcome. It relied exclusively on oxidative phosphorylation for energy production, whereas the glycolytic/plurimetabolic subtype was sustained by aerobic glycolysis and amino acid and lipid metabolism. Deletion of the glucose-proton symporter
    MeSH term(s) Glioblastoma/genetics ; Glioma/metabolism ; Glycolysis/genetics ; Humans ; Mitochondria/genetics ; Oxidative Phosphorylation
    Language English
    Publishing date 2021-01-11
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 2662-1347
    ISSN (online) 2662-1347
    DOI 10.1038/s43018-020-00159-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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