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  1. AU="Davis, Madison J"
  2. AU="Tatsuya Sato"
  3. AU="Berg, G P A"
  4. AU=Corti Davide
  5. AU="Pilcher"
  6. AU=Brown D M
  7. AU="Donald Bellgrau"
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  9. AU=Pham Minh Tan
  10. AU="Caniglia, John L"
  11. AU="Rao, Jiajia"
  12. AU="Vincent, Steve"
  13. AU="Oguntade, Habibat A"
  14. AU="Shah, Nikita Chetan"
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  18. AU="Alessandro Achilli"
  19. AU="Julià Blanco"
  20. AU=Pardee Arthur B
  21. AU="Moossy, John J"
  22. AU="Ledger, Elizabeth V"
  23. AU="Abichandani, Deepa"
  24. AU="Piccinelli, Fabio"
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  27. AU=Buscombe John R
  28. AU=Meyer-Rusenberg Birthe
  29. AU="Jiang, Weiyan"
  30. AU="Mills, W"
  31. AU="Pintó, Rosa M."
  32. AU="Voisin, Tiphaine"
  33. AU="Takahashi, Hiromi"
  34. AU="Lin, Johnny"
  35. AU="Lee, Yu-Ru"
  36. AU="Safrankova, J."
  37. AU="Lanting, Linda L"
  38. AU=Koushik Nikhil S
  39. AU="Culhane, John"
  40. AU="Chippada, Appa Rao"
  41. AU="Hiroki Sato" AU="Hiroki Sato"
  42. AU="Al-Amer Eshraq"
  43. AU="Thanacoody, Ruben"
  44. AU="Lin, Chi-Wei"
  45. AU="Chidambaram, Vignesh"

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  1. Artikel ; Online: Exploring the Amino Acid Residue Requirements of the RNA Polymerase (RNAP) α Subunit C-Terminal Domain for Productive Interaction between Spx and RNAP of Bacillus subtilis.

    Birch, Cierra A / Davis, Madison J / Mbengi, Lea / Zuber, Peter

    Journal of bacteriology

    2017  Band 199, Heft 14

    Abstract: ... Bacillus ... ...

    Abstract Bacillus subtilis
    Mesh-Begriff(e) Alleles ; Amino Acid Sequence ; Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; DNA-Directed RNA Polymerases/genetics ; DNA-Directed RNA Polymerases/metabolism ; Gene Expression Regulation, Bacterial/physiology ; Genotype ; Models, Molecular ; Protein Conformation ; Protein Domains
    Chemische Substanzen Bacterial Proteins ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; RNA polymerase alpha subunit (EC 2.7.7.6)
    Sprache Englisch
    Erscheinungsdatum 2017-07-15
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.00124-17
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Commensal bacteria and fungi differentially regulate tumor responses to radiation therapy.

    Shiao, Stephen L / Kershaw, Kathleen M / Limon, Jose J / You, Sungyong / Yoon, Junhee / Ko, Emily Y / Guarnerio, Jlenia / Potdar, Alka A / McGovern, Dermot P B / Bose, Shikha / Dar, Tahir B / Noe, Paul / Lee, Jung / Kubota, Yuzu / Maymi, Viviana I / Davis, Madison J / Henson, Regina M / Choi, Rachel Y / Yang, Wensha /
    Tang, Jie / Gargus, Matthew / Prince, Alexander D / Zumsteg, Zachary S / Underhill, David M

    Cancer cell

    2021  Band 39, Heft 9, Seite(n) 1202–1213.e6

    Abstract: Studies suggest that the efficacy of cancer chemotherapy and immunotherapy is influenced by intestinal bacteria. However, the influence of the microbiome on radiation therapy is not as well understood, and the microbiome comprises more than bacteria. ... ...

    Abstract Studies suggest that the efficacy of cancer chemotherapy and immunotherapy is influenced by intestinal bacteria. However, the influence of the microbiome on radiation therapy is not as well understood, and the microbiome comprises more than bacteria. Here, we find that intestinal fungi regulate antitumor immune responses following radiation in mouse models of breast cancer and melanoma and that fungi and bacteria have opposite influences on these responses. Antibiotic-mediated depletion or gnotobiotic exclusion of fungi enhances responsiveness to radiation, whereas antibiotic-mediated depletion of bacteria reduces responsiveness and is associated with overgrowth of commensal fungi. Further, elevated intratumoral expression of Dectin-1, a primary innate sensor of fungi, is negatively associated with survival in patients with breast cancer and is required for the effects of commensal fungi in mouse models of radiation therapy.
    Mesh-Begriff(e) Animals ; Antifungal Agents/administration & dosage ; Antifungal Agents/pharmacology ; Bacteria/classification ; Bacteria/immunology ; Breast Neoplasms/immunology ; Breast Neoplasms/microbiology ; Breast Neoplasms/therapy ; Combined Modality Therapy ; Down-Regulation ; Female ; Fungi/classification ; Fungi/drug effects ; Fungi/immunology ; Gastrointestinal Microbiome/drug effects ; Gastrointestinal Microbiome/radiation effects ; Gene Expression Regulation, Neoplastic/radiation effects ; Humans ; Lectins, C-Type/genetics ; Melanoma/immunology ; Melanoma/microbiology ; Melanoma/therapy ; Mice ; Symbiosis ; T-Lymphocytes/metabolism ; Tumor-Associated Macrophages/metabolism ; Up-Regulation/drug effects ; Up-Regulation/radiation effects ; Xenograft Model Antitumor Assays
    Chemische Substanzen Antifungal Agents ; CLEC7A protein, human ; Lectins, C-Type
    Sprache Englisch
    Erscheinungsdatum 2021-07-29
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2078448-X
    ISSN 1878-3686 ; 1535-6108
    ISSN (online) 1878-3686
    ISSN 1535-6108
    DOI 10.1016/j.ccell.2021.07.002
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Arginase Is Essential for Survival of Leishmania donovani Promastigotes but Not Intracellular Amastigotes.

    Boitz, Jan M / Gilroy, Caslin A / Olenyik, Tamara D / Paradis, Dustin / Perdeh, Jasmine / Dearman, Kristie / Davis, Madison J / Yates, Phillip A / Li, Yuexin / Riscoe, Michael K / Ullman, Buddy / Roberts, Sigrid C

    Infection and immunity

    2016  Band 85, Heft 1

    Abstract: Studies of Leishmania donovani have shown that both ornithine decarboxylase and spermidine synthase, two enzymes of the polyamine biosynthetic pathway, are critical for promastigote proliferation and required for maximum infection in mice. However, the ... ...

    Abstract Studies of Leishmania donovani have shown that both ornithine decarboxylase and spermidine synthase, two enzymes of the polyamine biosynthetic pathway, are critical for promastigote proliferation and required for maximum infection in mice. However, the importance of arginase (ARG), the first enzyme of the polyamine pathway in Leishmania, has not been analyzed in L. donovani To test ARG function in intact parasites, we generated Δarg null mutants in L. donovani and evaluated their ability to proliferate in vitro and trigger infections in mice. The Δarg knockout was incapable of growth in the absence of polyamine supplementation, but the auxotrophic phenotype could be bypassed by addition of either millimolar concentrations of ornithine or micromolar concentrations of putrescine or by complementation with either glycosomal or cytosolic versions of ARG. Spermidine supplementation of the medium did not circumvent the polyamine auxotrophy of the Δarg line. Although ARG was found to be essential for ornithine and polyamine synthesis, ornithine decarboxylase appeared to be the rate-limiting enzyme for polyamine production. Mouse infectivity studies revealed that the Δarg lesion reduced parasite burdens in livers by an order of magnitude but had little impact on the numbers of parasites recovered from spleens. Thus, ARG is essential for proliferation of promastigotes but not intracellular amastigotes. Coupled with previous studies, these data support a model in which L. donovani amastigotes readily salvage ornithine and have some access to host spermidine pools, while host putrescine appears to be unavailable for salvage by the parasite.
    Mesh-Begriff(e) Animals ; Arginase/metabolism ; Cells, Cultured ; Cytosol/metabolism ; Cytosol/parasitology ; Female ; Leishmania donovani/metabolism ; Leishmania infantum/metabolism ; Leishmania infantum/parasitology ; Leishmaniasis, Visceral/metabolism ; Leishmaniasis, Visceral/parasitology ; Mice ; Mice, Inbred BALB C ; Microbodies/metabolism ; Microbodies/parasitology ; Ornithine Decarboxylase/metabolism ; Polyamines/metabolism ; Putrescine/metabolism
    Chemische Substanzen Polyamines ; Arginase (EC 3.5.3.1) ; Ornithine Decarboxylase (EC 4.1.1.17) ; Putrescine (V10TVZ52E4)
    Sprache Englisch
    Erscheinungsdatum 2016-12-29
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 218698-6
    ISSN 1098-5522 ; 0019-9567
    ISSN (online) 1098-5522
    ISSN 0019-9567
    DOI 10.1128/IAI.00554-16
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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