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  1. Book ; Online: Paris Climate Agreement: Beacon of Hope

    Salawitch, Ross J. / Canty, Timothy P. / Hope, Austin P. / Tribett, Walter R. / Bennett, Brian F.

    (Springer Climate)

    2017  

    Author's details Ross J. Salawitch, Timothy P. Canty, Austin P. Hope, Walter R. Tribett, Brian F. Bennett
    Series title Springer Climate
    Keywords Environment ; Climate change ; Energy industries
    Subject code 577.27
    Language English
    Size 1 Online-Ressource (XVII, 186 p. 58 illus., 54 illus. in color)
    Publisher Springer International Publishing ; Imprint: Springer
    Publishing place Cham
    Document type Book ; Online
    HBZ-ID HT019227505
    ISBN 978-3-319-46939-3 ; 9783319469386 ; 3-319-46939-8 ; 331946938X
    DOI 10.1007/978-3-319-46939-3
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Article ; Online: Proteasome Inhibition Reprograms Chromatin Landscape in Breast Cancer.

    Kinyamu, H Karimi / Bennett, Brian D / Ward, James M / Archer, Trevor K

    Cancer research communications

    2024  Volume 4, Issue 4, Page(s) 1082–1099

    Abstract: The 26S proteasome is the major protein degradation machinery in cells. Cancer cells use the proteasome to modulate gene expression networks that promote tumor growth. Proteasome inhibitors have emerged as effective cancer therapeutics, but how they work ...

    Abstract The 26S proteasome is the major protein degradation machinery in cells. Cancer cells use the proteasome to modulate gene expression networks that promote tumor growth. Proteasome inhibitors have emerged as effective cancer therapeutics, but how they work mechanistically remains unclear. Here, using integrative genomic analysis, we discovered unexpected reprogramming of the chromatin landscape and RNA polymerase II (RNAPII) transcription initiation in breast cancer cells treated with the proteasome inhibitor MG132. The cells acquired dynamic changes in chromatin accessibility at specific genomic loci termed differentially open chromatin regions (DOCR). DOCRs with decreased accessibility were promoter proximal and exhibited unique chromatin architecture associated with divergent RNAPII transcription. Conversely, DOCRs with increased accessibility were primarily distal to transcription start sites and enriched in oncogenic superenhancers predominantly accessible in non-basal breast tumor subtypes. These findings describe the mechanisms by which the proteasome modulates the expression of gene networks intrinsic to breast cancer biology.
    Significance: Our study provides a strong basis for understanding the mechanisms by which proteasome inhibitors exert anticancer effects. We find open chromatin regions that change during proteasome inhibition, are typically accessible in non-basal breast cancers.
    MeSH term(s) Chromatin/genetics ; Proteasome Endopeptidase Complex/genetics ; Proteasome Inhibitors/pharmacology ; Proteolysis ; Genomics ; Neoplasms
    Chemical Substances Chromatin ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Proteasome Inhibitors
    Language English
    Publishing date 2024-04-16
    Publishing country United States
    Document type Journal Article
    ISSN 2767-9764
    ISSN (online) 2767-9764
    DOI 10.1158/2767-9764.CRC-23-0476
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Book ; Online: Paris Climate Agreement: Beacon of Hope

    Salawitch, Ross J. / Canty, Timothy P. / Hope, Austin P. / Tribett, Walter R. / Bennett, Brian F.

    2017  

    Keywords Environmental economics ; Manufacturing industries ; Pharmaceutical industries ; Earth sciences, geography, environment, planning ; Biochemical engineering ; Climate Change ; Climate Change Management and Policy ; Energy Economics
    Size 1 Online-Ressource
    Publisher Springer Nature
    Publishing place Cham
    Document type Book ; Online
    Note English ; Open Access
    HBZ-ID HT021029034
    ISBN 9783319730370 ; 3319730371
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  4. Article: Proteasome inhibition reprograms chromatin landscape in breast cancer.

    Kinyamu, H Karimi / Bennett, Brian D / Ward, James M / Archer, Trevor

    bioRxiv : the preprint server for biology

    2023  

    Abstract: The 26S proteasome is the major protein degradation machinery in cells. Cancer cells use the proteasome to modulate gene expression networks that promote tumor growth. Proteasome inhibitors have emerged as effective cancer therapeutics, but how they work ...

    Abstract The 26S proteasome is the major protein degradation machinery in cells. Cancer cells use the proteasome to modulate gene expression networks that promote tumor growth. Proteasome inhibitors have emerged as effective cancer therapeutics, but how they work mechanistically remains unclear. Here, using integrative genomic analysis, we discovered unexpected reprogramming of the chromatin landscape and RNAPII transcription initiation in breast cancer cells treated with the proteasome inhibitor MG132. The cells acquired dynamic changes in chromatin accessibility at specific genomic loci termed Differentially Open Chromatin Regions (DOCRs). DOCRs with decreased accessibility were promoter proximal and exhibited unique chromatin architecture associated with divergent RNAPII transcription. Conversely, DOCRs with increased accessibility were primarily distal to transcription start sites and enriched in oncogenic super enhancers predominantly accessible in non-basal breast tumor subtypes. These findings describe the mechanisms by which the proteasome modulates the expression of gene networks intrinsic to breast cancer biology.
    Highlights: Proteasome inhibition uncovers
    Language English
    Publishing date 2023-10-17
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.10.13.562284
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Sequence meets function—microbiota and cardiovascular disease

    Kim, Myungsuk / Huda, Md Nazmul / Bennett, Brian J.

    Cardiovascular Research. 2022 Feb., v. 118, no. 2

    2022  

    Abstract: The discovery that gut-microbiota plays a profound role in human health has opened a new avenue of basic and clinical research. Application of ecological approaches where the bacterial 16S rRNA gene is queried has provided a number of candidate bacteria ... ...

    Abstract The discovery that gut-microbiota plays a profound role in human health has opened a new avenue of basic and clinical research. Application of ecological approaches where the bacterial 16S rRNA gene is queried has provided a number of candidate bacteria associated with coronary artery disease and hypertension. We examine the associations between gut microbiota and a variety of cardiovascular disease (CVD) including atherosclerosis, coronary artery disease, and blood pressure. These approaches are associative in nature and there is now increasing interest in identifying the mechanisms underlying these associations. We discuss three potential mechanisms including: gut permeability and endotoxemia, increased immune system activation, and microbial derived metabolites. In addition to discussing these potential mechanisms we highlight current studies manipulating the gut microbiota or microbial metabolites to move beyond sequence-based association studies. The goal of these mechanistic studies is to determine the mode of action by which the gut microbiota may affect disease susceptibility and severity. Importantly, the gut microbiota appears to have a significant effect on host metabolism and CVD by producing metabolites entering the host circulatory system such as short-chain fatty acids and trimethylamine N-Oxide. Therefore, the intersection of metabolomics and microbiota research may yield novel targets to reduce disease susceptibility. Finally, we discuss approaches to demonstrate causality such as specific diet changes, inhibition of microbial pathways, and fecal microbiota transplant.
    Keywords atherosclerosis ; biomedical research ; blood pressure ; circulatory system ; coronary artery disease ; diet ; digestive system ; disease susceptibility ; endotoxemia ; genes ; human health ; hypertension ; immune system ; intestinal microorganisms ; mechanism of action ; metabolism ; metabolites ; metabolomics ; permeability ; trimethylamine
    Language English
    Dates of publication 2022-02
    Size p. 399-412.
    Publishing place Oxford University Press (OUP)
    Document type Article
    ZDB-ID 80340-6
    ISSN 1755-3245 ; 0008-6363
    ISSN (online) 1755-3245
    ISSN 0008-6363
    DOI 10.1093/cvr/cvab030
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 71/513: Show issues

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  6. Article ; Online: Chow diet in mouse aging studies: nothing regular about it.

    Lee, Jennifer / Purello, Chloe / Booth, Sarah L / Bennett, Brian / Wiley, Christopher D / Korstanje, Ron

    GeroScience

    2023  Volume 45, Issue 3, Page(s) 2079–2084

    Abstract: Chow diet is used in the majority of rodent studies and, although assumed to be standardized for dietary source and nutritional contents, it varies widely across commercial formulations. Similarly, current approaches to study aging in rodents involve a ... ...

    Abstract Chow diet is used in the majority of rodent studies and, although assumed to be standardized for dietary source and nutritional contents, it varies widely across commercial formulations. Similarly, current approaches to study aging in rodents involve a single-diet formulation across the lifespan and overlook age-specific nutritional requirements, which may have long-term effects on aging processes. Together, these nutrition-based disparities represent major gaps in geroscience research, affecting the interpretation and reproducibility of the studies. This perspective aims to raise awareness on the importance of rodent diet formulation and proposes that geroscientists include detailed descriptions of all experimental diets and feeding protocols. Detailed reporting of diets will enhance rigor and reproducibility of aging rodent studies and lead to more translational outcomes in geroscience research.
    MeSH term(s) Animals ; Mice ; Reproducibility of Results ; Diet ; Rodentia ; Aging ; Longevity
    Language English
    Publishing date 2023-04-20
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2886586-8
    ISSN 2509-2723 ; 2509-2715
    ISSN (online) 2509-2723
    ISSN 2509-2715
    DOI 10.1007/s11357-023-00775-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1502: 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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  7. Article ; Online: Genetic screen identified PRMT5 as a neuroprotection target against cerebral ischemia.

    Wu, Haoyang / Lv, Peiyuan / Wang, Jinyu / Bennett, Brian / Wang, Jiajia / Li, Pishun / Peng, Yi / Hu, Guang / Lin, Jiaji

    eLife

    2024  Volume 12

    Abstract: Epigenetic regulators present novel opportunities for both ischemic stroke research and therapeutic interventions. While previous work has implicated that they may provide neuroprotection by potentially influencing coordinated sets of genes and pathways, ...

    Abstract Epigenetic regulators present novel opportunities for both ischemic stroke research and therapeutic interventions. While previous work has implicated that they may provide neuroprotection by potentially influencing coordinated sets of genes and pathways, most of them remain largely uncharacterized in ischemic conditions. In this study, we used the oxygen-glucose deprivation (OGD) model in the immortalized mouse hippocampal neuronal cell line HT-22 and carried out an RNAi screen on epigenetic regulators. PRMT5 was identified as a novel negative regulator of neuronal cell survival after OGD, which presented a phenotype of translocation from the cytosol to the nucleus upon oxygen and energy depletion both in vitro and in vivo. PRMT5 bound to the chromatin and a large number of promoter regions to repress downstream gene expression. Silencing
    MeSH term(s) Animals ; Mice ; Brain Ischemia/genetics ; Glucose ; Hedgehog Proteins ; Neuroprotection/genetics ; Oxygen ; Phenotype ; Protein-Arginine N-Methyltransferases/genetics
    Chemical Substances Glucose (IY9XDZ35W2) ; Hedgehog Proteins ; Oxygen (S88TT14065) ; Prmt5 protein, mouse (EC 2.1.1.319) ; Protein-Arginine N-Methyltransferases (EC 2.1.1.319)
    Language English
    Publishing date 2024-02-19
    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.89754
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Role of second-sphere arginine residues in metal binding and metallocentre assembly in nitrile hydratases.

    Miller, Callie / Huntoon, Delanie / Kaley, Nicholas / Ogutu, Irene / Fiedler, Adam T / Bennett, Brian / Liu, Dali / Holz, Richard

    Journal of inorganic biochemistry

    2024  Volume 256, Page(s) 112565

    Abstract: Two conserved second-sphere βArg (R) residues in nitrile hydratases (NHase), that form hydrogen bonds with the catalytically essential sulfenic and sulfinic acid ligands, were mutated to Lys and Ala residues in the Co-type NHase from Pseudonocardia ... ...

    Abstract Two conserved second-sphere βArg (R) residues in nitrile hydratases (NHase), that form hydrogen bonds with the catalytically essential sulfenic and sulfinic acid ligands, were mutated to Lys and Ala residues in the Co-type NHase from Pseudonocardia thermophila JCM 3095 (PtNHase) and the Fe-type NHase from Rhodococcus equi TG328-2 (ReNHase). Only five of the eight mutants (PtNHase βR52A, βR52K, βR157A, βR157K and ReNHase βR61A) were successfully expressed and purified. Apart from the PtNHase βR52A mutant that exhibited no detectable activity, the k
    MeSH term(s) Hydro-Lyases/chemistry ; Hydro-Lyases/metabolism ; Hydro-Lyases/genetics ; Arginine/chemistry ; Rhodococcus equi/enzymology ; Rhodococcus equi/genetics ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Actinomycetales/enzymology ; Actinomycetales/genetics ; Catalytic Domain
    Chemical Substances Hydro-Lyases (EC 4.2.1.-) ; nitrile hydratase (EC 4.2.1.-) ; Arginine (94ZLA3W45F) ; Bacterial Proteins
    Language English
    Publishing date 2024-04-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 162843-4
    ISSN 1873-3344 ; 0162-0134
    ISSN (online) 1873-3344
    ISSN 0162-0134
    DOI 10.1016/j.jinorgbio.2024.112565
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.B 1730: 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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  9. Article: Modulating the Microbiota as a Therapeutic Intervention for Type 2 Diabetes.

    Huda, M Nazmul / Kim, Myungsuk / Bennett, Brian J

    Frontiers in endocrinology

    2021  Volume 12, Page(s) 632335

    Abstract: Mounting evidence suggested that the gut microbiota has a significant role in the metabolism and disease status of the host. In particular, Type 2 Diabetes (T2D), which has a complex etiology that includes obesity and chronic low-grade inflammation, is ... ...

    Abstract Mounting evidence suggested that the gut microbiota has a significant role in the metabolism and disease status of the host. In particular, Type 2 Diabetes (T2D), which has a complex etiology that includes obesity and chronic low-grade inflammation, is modulated by the gut microbiota and microbial metabolites. Current literature supports that unbalanced gut microbial composition (dysbiosis) is a risk factor for T2D. In this review, we critically summarize the recent findings regarding the role of gut microbiota in T2D. Beyond these associative studies, we focus on the causal relationship between microbiota and T2D established using fecal microbiota transplantation (FMT) or probiotic supplementation, and the potential underlying mechanisms such as byproducts of microbial metabolism. These microbial metabolites are small molecules that establish communication between microbiota and host cells. We critically summarize the associations between T2D and microbial metabolites such as short-chain fatty acids (SCFAs) and trimethylamine N-Oxide (TMAO). Additionally, we comment on how host genetic architecture and the epigenome influence the microbial composition and thus how the gut microbiota may explain part of the missing heritability of T2D found by GWAS analysis. We also discuss future directions in this field and how approaches such as FMT, prebiotics, and probiotics supplementation are being considered as potential therapeutics for T2D.
    MeSH term(s) Diabetes Mellitus, Type 2/etiology ; Diabetes Mellitus, Type 2/therapy ; Dysbiosis/complications ; Dysbiosis/therapy ; Fecal Microbiota Transplantation ; Gastrointestinal Microbiome/physiology ; Humans ; Prebiotics ; Probiotics/therapeutic use
    Chemical Substances Prebiotics
    Language English
    Publishing date 2021-04-07
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 2592084-4
    ISSN 1664-2392
    ISSN 1664-2392
    DOI 10.3389/fendo.2021.632335
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Insight into the Maturation Process of the Nitrile Hydratase Active Site.

    Ogutu, Irene R A M / Holz, Richard C / Bennett, Brian

    Inorganic chemistry

    2021  Volume 60, Issue 8, Page(s) 5432–5435

    Abstract: The metal binding motif of all nitrile hydratases (NHases, EC 4.2.1.84) is highly conserved (CXXCSCX) in the α-subunit. Accordingly, an eight amino acid peptide (VCTLCSCY), based on the metal binding motif of the Co-type NHase ... ...

    Abstract The metal binding motif of all nitrile hydratases (NHases, EC 4.2.1.84) is highly conserved (CXXCSCX) in the α-subunit. Accordingly, an eight amino acid peptide (VCTLCSCY), based on the metal binding motif of the Co-type NHase from
    MeSH term(s) Binding Sites ; Ferric Compounds/chemistry ; Ferric Compounds/metabolism ; Hydro-Lyases/chemistry ; Hydro-Lyases/metabolism ; Molecular Structure ; Pseudonocardia/enzymology ; Rhodococcus equi/enzymology
    Chemical Substances Ferric Compounds ; Hydro-Lyases (EC 4.2.1.-) ; nitrile hydratase (EC 4.2.1.-)
    Language English
    Publishing date 2021-03-29
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1484438-2
    ISSN 1520-510X ; 0020-1669
    ISSN (online) 1520-510X
    ISSN 0020-1669
    DOI 10.1021/acs.inorgchem.0c02924
    Database MEDical Literature Analysis and Retrieval System OnLINE

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