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  1. Article ; Online: Pirated Siderophores Promote Sporulation in Bacillus subtilis.

    Grandchamp, Gabrielle M / Caro, Lews / Shank, Elizabeth A

    Applied and environmental microbiology

    2017  Volume 83, Issue 10

    Abstract: In microbial communities, bacteria chemically and physically interact with one another. Some of these interactions are mediated by secreted specialized metabolites that act as either intraspecies or interspecies signals to alter gene expression and to ... ...

    Abstract In microbial communities, bacteria chemically and physically interact with one another. Some of these interactions are mediated by secreted specialized metabolites that act as either intraspecies or interspecies signals to alter gene expression and to change cell physiology.
    MeSH term(s) Bacillus subtilis/genetics ; Bacillus subtilis/growth & development ; Bacillus subtilis/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Enterobactin/metabolism ; Gene Expression Regulation, Bacterial ; Iron/metabolism ; Oligopeptides/metabolism ; Siderophores/metabolism ; Spores, Bacterial/genetics ; Spores, Bacterial/metabolism
    Chemical Substances Bacterial Proteins ; Oligopeptides ; Siderophores ; bacillibactin ; Enterobactin (28384-96-5) ; Iron (E1UOL152H7)
    Language English
    Publishing date 2017-05-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 223011-2
    ISSN 1098-5336 ; 0099-2240
    ISSN (online) 1098-5336
    ISSN 0099-2240
    DOI 10.1128/AEM.03293-16
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: A Dual-Species Biofilm with Emergent Mechanical and Protective Properties.

    Yannarell, Sarah M / Grandchamp, Gabrielle M / Chen, Shih-Yuan / Daniels, Karen E / Shank, Elizabeth A

    Journal of bacteriology

    2019  Volume 201, Issue 18

    Abstract: Many microbes coexist within biofilms, or multispecies communities of cells encased in an extracellular matrix. However, little is known about the microbe-microbe interactions relevant for creating these structures. In this study, we explored a striking ... ...

    Abstract Many microbes coexist within biofilms, or multispecies communities of cells encased in an extracellular matrix. However, little is known about the microbe-microbe interactions relevant for creating these structures. In this study, we explored a striking dual-species biofilm between
    MeSH term(s) Bacillus subtilis/metabolism ; Bacterial Proteins/metabolism ; Biofilms/growth & development ; Extracellular Matrix/metabolism ; Extracellular Matrix/physiology ; Pantoea/metabolism
    Chemical Substances Bacterial Proteins
    Language English
    Publishing date 2019-08-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.00670-18
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.50: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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  3. Article ; Online: A new human NHERF1 mutation decreases renal phosphate transporter NPT2a expression by a PTH-independent mechanism.

    Courbebaisse, Marie / Leroy, Christine / Bakouh, Naziha / Salaün, Christine / Beck, Laurent / Grandchamp, Bernard / Planelles, Gabrielle / Hall, Randy A / Friedlander, Gérard / Prié, Dominique

    PloS one

    2012  Volume 7, Issue 4, Page(s) e34764

    Abstract: Background: The sodium-hydrogen exchanger regulatory factor 1 (NHERF1) binds to the main renal phosphate transporter NPT2a and to the parathyroid hormone (PTH) receptor. We have recently identified mutations in NHERF1 that decrease renal phosphate ... ...

    Abstract Background: The sodium-hydrogen exchanger regulatory factor 1 (NHERF1) binds to the main renal phosphate transporter NPT2a and to the parathyroid hormone (PTH) receptor. We have recently identified mutations in NHERF1 that decrease renal phosphate reabsorption by increasing PTH-induced cAMP production in the renal proximal tubule.
    Methods: We compared relevant parameters of phosphate homeostasis in a patient with a previously undescribed mutation in NHERF1 and in control subjects. We expressed the mutant NHERF1 protein in Xenopus Oocytes and in cultured cells to study its effects on phosphate transport and PTH-induced cAMP production.
    Results: We identified in a patient with inappropriate renal phosphate reabsorption a previously unidentified mutation (E68A) located in the PDZ1 domain of NHERF1.We report the consequences of this mutation on NHERF1 function. E68A mutation did not modify cAMP production in the patient. PTH-induced cAMP synthesis and PKC activity were not altered by E68A mutation in renal cells in culture. In contrast to wild-type NHERF1, expression of the E68A mutant in Xenopus oocytes and in human cells failed to increase phosphate transport. Pull down experiments showed that E68A mutant did not interact with NPT2a, which robustly interacted with wild type NHERF1 and previously identified mutants. Biotinylation studies revealed that E68A mutant was unable to increase cell surface expression of NPT2a.
    Conclusions: Our results indicate that the PDZ1 domain is critical for NHERF1-NPT2a interaction in humans and for the control of NPT2a expression at the plasma membrane. Thus we have identified a new mechanism of renal phosphate loss and shown that different mutations in NHERF1 can alter renal phosphate reabsorption via distinct mechanisms.
    MeSH term(s) Aged ; Animals ; Cell Line, Tumor ; Cells, Cultured ; Cyclic AMP/metabolism ; HeLa Cells ; Humans ; Kidney Tubules, Proximal/metabolism ; Mutation ; Oocytes/metabolism ; Opossums ; Parathyroid Hormone/metabolism ; Phosphate Transport Proteins/biosynthesis ; Phosphate Transport Proteins/genetics ; Phosphates/metabolism ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein Kinase C/metabolism ; Sodium-Hydrogen Exchangers/genetics ; Sodium-Hydrogen Exchangers/metabolism ; Sodium-Phosphate Cotransporter Proteins, Type IIa/genetics ; Sodium-Phosphate Cotransporter Proteins, Type IIa/metabolism ; Xenopus laevis/genetics ; Xenopus laevis/metabolism
    Chemical Substances Parathyroid Hormone ; Phosphate Transport Proteins ; Phosphates ; Phosphoproteins ; SLC34A1 protein, human ; Sodium-Hydrogen Exchangers ; Sodium-Phosphate Cotransporter Proteins, Type IIa ; sodium-hydrogen exchanger regulatory factor ; Cyclic AMP (E0399OZS9N) ; Protein Kinase C (EC 2.7.11.13)
    Language English
    Publishing date 2012-04-10
    Publishing country United States
    Document type Case Reports ; Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0034764
    Database MEDical Literature Analysis and Retrieval System OnLINE

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