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  1. Article ; Online: Assay of Endocannabinoid Oxidation by Cytochrome P450.

    Snider, Natasha T / Hollenberg, Paul F

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

    2022  Volume 2576, Page(s) 317–327

    Abstract: Cytochrome P450 enzymes are a large family of heme-containing proteins that have important functions in the biotransformation of xenobiotics, including pharmacologic and environmental agents, as well as endogenously produced chemicals with broad ... ...

    Abstract Cytochrome P450 enzymes are a large family of heme-containing proteins that have important functions in the biotransformation of xenobiotics, including pharmacologic and environmental agents, as well as endogenously produced chemicals with broad structural and functional diversity. Anandamide and 2-arachidonoylglycerol (2-AG) are substrates for P450s expressed in multiple tissues, leading to the production of a diverse set of mono- and di-oxygenated metabolites. This chapter describes tools and methods that have been used to identify major endocannabinoid metabolizing P450s and their corresponding products using subcellular tissue fractions, cultured cells, and purified recombinant enzymes in a reconstituted system.
    MeSH term(s) Cytochrome P-450 Enzyme System/metabolism ; Endocannabinoids/metabolism ; Heme/metabolism ; Microsomes, Liver ; Oxidation-Reduction ; Recombinant Proteins/metabolism ; Xenobiotics/metabolism
    Chemical Substances Endocannabinoids ; Recombinant Proteins ; Xenobiotics ; Heme (42VZT0U6YR) ; Cytochrome P-450 Enzyme System (9035-51-2)
    Language English
    Publishing date 2022-09-24
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2728-0_27
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  2. Article ; Online: Assembly of NFL and desmin intermediate filaments: Headed in the right direction.

    Faridounnia, Maryam / Snider, Natasha T

    Proceedings of the National Academy of Sciences of the United States of America

    2021  Volume 118, Issue 13

    MeSH term(s) Desmin ; Intermediate Filaments
    Chemical Substances Desmin
    Language English
    Publishing date 2021-03-09
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2102176118
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  3. Article ; Online: Stability dynamics of neurofilament and GFAP networks and protein fragments.

    Phillips, Cassandra L / Faridounnia, Maryam / Armao, Diane / Snider, Natasha T

    Current opinion in cell biology

    2023  Volume 85, Page(s) 102266

    Abstract: Neurofilaments (NFs) and GFAP are cytoskeletal intermediate filaments (IFs) that support cellular processes unfolding within the uniquely complex environments of neurons and astrocytes, respectively. This review highlights emerging concepts on the ... ...

    Abstract Neurofilaments (NFs) and GFAP are cytoskeletal intermediate filaments (IFs) that support cellular processes unfolding within the uniquely complex environments of neurons and astrocytes, respectively. This review highlights emerging concepts on the transitions between stable and destabilized IF networks in the nervous system. While self-association between transiently structured low-complexity IF domains promotes filament assembly, the opposing destabilizing actions of phosphorylation-mediated filament severing facilitate faster intracellular transport. Cellular proteases, including caspases and calpains, produce a variety of IF fragments, which may interact with N-degron and C-degron pathways of the protein degradation machinery. The rapid adoption of NF and GFAP-based clinical biomarker tests is contrasted with the lagging understanding of the dynamics between the native IF proteins and their fragments.
    MeSH term(s) Intermediate Filaments/metabolism ; Cytoskeleton/metabolism ; Nervous System ; Neurons ; Phosphorylation
    Language English
    Publishing date 2023-10-20
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2023.102266
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2963: Show issues Location:
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  4. Article ; Online: Kidney keratins: cytoskeletal stress responders with biomarker potential.

    Snider, Natasha T

    Kidney international

    2016  Volume 89, Issue 4, Page(s) 738–740

    Abstract: Keratins are cytoskeletal filamentous proteins that support the structural integrity of epithelial cells. Deficiency of the major simple epithelial keratins K8, K18, and K19 increases susceptibility to hepatobiliary injury, but keratin function in kidney ...

    Abstract Keratins are cytoskeletal filamentous proteins that support the structural integrity of epithelial cells. Deficiency of the major simple epithelial keratins K8, K18, and K19 increases susceptibility to hepatobiliary injury, but keratin function in kidney injury has not been addressed. Djudjaj et al. examined renal keratins in health and disease, in both mice and humans. Their findings lay the foundation for pursuing keratins as markers and regulators of renal tubular epithelial injury.
    MeSH term(s) Animals ; Biomarkers/metabolism ; Cytoskeleton/metabolism ; Epithelial Cells/metabolism ; Humans ; Keratin-8 ; Keratins ; Kidney/metabolism
    Chemical Substances Biomarkers ; Keratin-8 ; Keratins (68238-35-7)
    Language English
    Publishing date 2016-04
    Publishing country United States
    Document type Comment ; Journal Article
    ZDB-ID 120573-0
    ISSN 1523-1755 ; 0085-2538
    ISSN (online) 1523-1755
    ISSN 0085-2538
    DOI 10.1016/j.kint.2015.12.040
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 797: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: The elegant complexity of mammalian ecto-5'-nucleotidase (CD73).

    Alcedo, Karel P / Bowser, Jessica L / Snider, Natasha T

    Trends in cell biology

    2021  Volume 31, Issue 10, Page(s) 829–842

    Abstract: Purinergic signaling is a fundamental mechanism used by all cells to control their internal activities and interact with the environment. A key component of the purinergic system, the enzyme ecto-5'-nucleotidase (CD73) catalyzes the last step in the ... ...

    Abstract Purinergic signaling is a fundamental mechanism used by all cells to control their internal activities and interact with the environment. A key component of the purinergic system, the enzyme ecto-5'-nucleotidase (CD73) catalyzes the last step in the extracellular metabolism of ATP to form adenosine. Efforts to harness the therapeutic potential of endogenous adenosine in cancer have culminated in the ongoing clinical development of multiple CD73-targeting antibodies and small-molecule inhibitors. However, recent studies are painting an increasingly complex picture of CD73 mRNA and protein regulation and function in cellular homeostasis, physiological adaptation, and disease development. This review discusses the latest conceptual and methodological advances that are helping to unravel the complexity of this important enzyme that was identified nearly 90 years ago.
    MeSH term(s) 5'-Nucleotidase/genetics ; 5'-Nucleotidase/metabolism ; Adenosine ; Adenosine Monophosphate ; Animals ; RNA, Messenger ; Signal Transduction
    Chemical Substances RNA, Messenger ; Adenosine Monophosphate (415SHH325A) ; 5'-Nucleotidase (EC 3.1.3.5) ; Adenosine (K72T3FS567)
    Language English
    Publishing date 2021-06-08
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2021.05.008
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    Zs.MG 25: Show issues
    Zs.MO 113: Show issues
    Zs.A 3410: 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: Calpain-mediated proteolysis of vimentin filaments is augmented in giant axonal neuropathy fibroblasts exposed to hypotonic stress.

    Phillips, Cassandra L / Fu, Dong / Herring, Laura E / Armao, Diane / Snider, Natasha T

    Frontiers in cell and developmental biology

    2022  Volume 10, Page(s) 1008542

    Abstract: Giant Axonal Neuropathy (GAN) is a pediatric neurodegenerative disease caused by loss-of-function mutations in the E3 ubiquitin ligase adaptor gigaxonin, which is encoded by ... ...

    Abstract Giant Axonal Neuropathy (GAN) is a pediatric neurodegenerative disease caused by loss-of-function mutations in the E3 ubiquitin ligase adaptor gigaxonin, which is encoded by the
    Language English
    Publishing date 2022-11-01
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2022.1008542
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  7. Article ; Online: Calpain-mediated proteolysis of vimentin filaments is augmented in giant axonal neuropathy fibroblasts exposed to hypotonic stress

    Cassandra L. Phillips / Dong Fu / Laura E. Herring / Diane Armao / Natasha T. Snider

    Frontiers in Cell and Developmental Biology, Vol

    2022  Volume 10

    Abstract: Giant Axonal Neuropathy (GAN) is a pediatric neurodegenerative disease caused by loss-of-function mutations in the E3 ubiquitin ligase adaptor gigaxonin, which is encoded by the KLHL16 gene. Gigaxonin regulates the degradation of multiple intermediate ... ...

    Abstract Giant Axonal Neuropathy (GAN) is a pediatric neurodegenerative disease caused by loss-of-function mutations in the E3 ubiquitin ligase adaptor gigaxonin, which is encoded by the KLHL16 gene. Gigaxonin regulates the degradation of multiple intermediate filament (IF) proteins, including neurofilaments, GFAP, and vimentin, which aggregate in GAN patient cells. Understanding how IFs and their aggregates are processed under stress can reveal new GAN disease mechanisms and potential targets for therapy. Here we tested the hypothesis that hypotonic stress-induced vimentin proteolysis is impaired in GAN. In both GAN and control fibroblasts exposed to hypotonic stress, we observed time-dependent vimentin cleavage that resulted in two prominent ∼40–45 kDa fragments. However, vimentin proteolysis occurred more rapidly and extensively in GAN cells compared to unaffected controls as both fragments were generated earlier and at 4-6-fold higher levels. To test enzymatic involvement, we determined the expression levels and localization of the calcium-sensitive calpain proteases-1 and -2 and their endogenous inhibitor calpastatin. While the latter was not affected, the expression of both calpains was 2-fold higher in GAN cells compared to control cells. Moreover, pharmacologic inhibition of calpains with MDL-28170 or MG-132 attenuated vimentin cleavage. Imaging analysis revealed striking colocalization between large perinuclear vimentin aggregates and calpain-2 in GAN fibroblasts. This colocalization was dramatically altered by hypotonic stress, where selective breakdown of filaments over aggregates occurred rapidly in GAN cells and coincided with calpain-2 cytoplasmic redistribution. Finally, mass spectrometry-based proteomics revealed that phosphorylation at Ser-412, located at the junction between the central “rod” domain and C-terminal “tail” domain on vimentin, is involved in this stress response. Over-expression studies using phospho-deficient and phospho-mimic mutants revealed that Ser-412 is important for filament ...
    Keywords protease ; fragments ; protein aggregation ; gigaxonin ; post-translational modifications ; Biology (General) ; QH301-705.5
    Subject code 572
    Language English
    Publishing date 2022-11-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: The sweet side of vimentin.

    Snider, Natasha T / Ku, Nam-On / Omary, M Bishr

    eLife

    2018  Volume 7

    Abstract: A protein modification called O-linked glycosylation regulates the interactions between vimentin molecules under normal conditions, and the ability ... ...

    Abstract A protein modification called O-linked glycosylation regulates the interactions between vimentin molecules under normal conditions, and the ability of
    MeSH term(s) Acetylglucosamine ; Glycosylation ; Intermediate Filaments ; Protein Processing, Post-Translational ; Vimentin
    Chemical Substances Vimentin ; Acetylglucosamine (V956696549)
    Language English
    Publishing date 2018-03-07
    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.35336
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  9. Article ; Online: Alternative Splicing in Hepatocellular Carcinoma.

    Lee, Seung Eun / Alcedo, Karel P / Kim, Hong Jin / Snider, Natasha T

    Cellular and molecular gastroenterology and hepatology

    2020  Volume 10, Issue 4, Page(s) 699–712

    Abstract: Hepatocellular carcinoma (HCC) accounts for the majority of primary liver cancer cases, with more than 850,000 new diagnoses per year globally. Recent trends in the United States have shown that liver cancer mortality has continued to increase in both ... ...

    Abstract Hepatocellular carcinoma (HCC) accounts for the majority of primary liver cancer cases, with more than 850,000 new diagnoses per year globally. Recent trends in the United States have shown that liver cancer mortality has continued to increase in both men and women, while 5-year survival remains below 20%. Understanding key mechanisms that drive chronic liver disease progression to HCC can reveal new therapeutic targets and biomarkers for early detection of HCC. In that regard, many studies have underscored the importance of alternative splicing as a source of novel HCC prognostic markers and disease targets. Alternative splicing of pre-mRNA provides functional diversity to the genome, and endows cells with the ability to rapidly remodel the proteome. Genes that control fundamental processes, such as metabolism, cell proliferation, and apoptosis, are altered globally in HCC by alternative splicing. This review highlights the major splicing factors, RNA binding proteins, transcriptional targets, and signaling pathways that are of key relevance to HCC. We highlight primary research from the past 3-5 years involving functional interrogation of alternative splicing in rodent and human liver, using both large-scale transcriptomic and focused mechanistic approaches. Because this is a rapidly advancing field, we anticipate that it will be transformative for the future of basic liver biology, as well as HCC diagnosis and management.
    MeSH term(s) Alternative Splicing ; Animals ; Carcinoma, Hepatocellular/genetics ; Gene Expression Regulation, Neoplastic ; Humans ; Liver Neoplasms/genetics ; RNA/genetics ; Transcriptome
    Chemical Substances RNA (63231-63-0)
    Language English
    Publishing date 2020-05-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2819778-1
    ISSN 2352-345X ; 2352-345X
    ISSN (online) 2352-345X
    ISSN 2352-345X
    DOI 10.1016/j.jcmgh.2020.04.018
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  10. Article ; Online: Assays for Posttranslational Modifications of Intermediate Filament Proteins.

    Snider, Natasha T / Omary, M Bishr

    Methods in enzymology

    2016  Volume 568, Page(s) 113–138

    Abstract: Intermediate filament (IF) proteins are known to be regulated by a number of posttranslational modifications (PTMs). Phosphorylation is the best-studied IF PTM, whereas ubiquitination, sumoylation, acetylation, glycosylation, ADP-ribosylation, ... ...

    Abstract Intermediate filament (IF) proteins are known to be regulated by a number of posttranslational modifications (PTMs). Phosphorylation is the best-studied IF PTM, whereas ubiquitination, sumoylation, acetylation, glycosylation, ADP-ribosylation, farnesylation, and transamidation are less understood in functional terms but are known to regulate specific IFs under various contexts. The number and diversity of IF PTMs is certain to grow along with rapid advances in proteomic technologies. Therefore, the need for a greater understanding of the implications of PTMs to the structure, organization, and function of the IF cytoskeleton has become more apparent with the increased availability of data from global profiling studies of normal and diseased specimens. This chapter will provide information on established methods for the isolation and monitoring of IF PTMs along with the key reagents that are necessary to carry out these experiments.
    MeSH term(s) Acetylation ; Animals ; Biological Assay/methods ; Glycosylation ; Humans ; Intermediate Filament Proteins/metabolism ; Phosphorylation ; Protein Processing, Post-Translational ; Proteomics/methods ; Ubiquitination
    Chemical Substances Intermediate Filament Proteins
    Language English
    Publishing date 2016
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1557-7988 ; 0076-6879
    ISSN (online) 1557-7988
    ISSN 0076-6879
    DOI 10.1016/bs.mie.2015.09.005
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