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  • Nature Publishing Group  (4)
  • American Association for the Advancement of Science (AAAS)  (3)
  • 2005-2009  (7)
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  • 1
    Electronic Resource
    Electronic Resource
    Analysis of published PKD1 gene sequence variants (2007)
    [s.l.] : Nature Publishing Group
    Nature genetics 39 (2007), S. 427-428 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] To the Editor: We retrospectively reviewed published variants in the PKD1 genes and detected errors in 39 of 771 variants (5.06% (95% c.i., 3.62–6.85)). All arose from human processing mistakes. As peer-reviewed publication is no safeguard for those considering the clinical significance of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/ng0407-427
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Functional diversification of closely related ARF-GEFs in protein secretion and recycling (2007)
    [s.l.] : Nature Publishing Group
    Nature 448 (2007), S. 488-492 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Guanine-nucleotide exchange factors on ADP-ribosylation factor GTPases (ARF-GEFs) regulate vesicle formation in time and space by activating ARF substrates on distinct donor membranes. Mammalian GBF1 (ref. 2) and yeast Gea1/2 (ref. 3) ARF-GEFs act at Golgi membranes, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature05967
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  • 3
    Electronic Resource
    Electronic Resource
    Synthetic chemistry Making a natural fuel cell (2005)
    [s.l.] : Nature Publishing Group
    Nature 433 (2005), S. 589-591 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A host of microbes metabolize hydrogen with high efficiency by using enzymes known as hydrogenases. These enzymes are exquisite miniature hydrogen fuel cells, and are based on a combination of sulphur and iron atoms, and sometimes a single nickel atom. On page 610 of this issue, Tard et al. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/433589a
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  • 4
    Electronic Resource
    Electronic Resource
    Two stellar components in the halo of the Milky Way (2007)
    [s.l.] : Nature Publishing Group
    Nature 450 (2007), S. 1020-1025 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The halo of the Milky Way provides unique elemental abundance and kinematic information on the first objects to form in the Universe, and this information can be used to tightly constrain models of galaxy formation and evolution. Although the halo was once considered a single component, evidence ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature06460
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  • 5
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    Absence of the SRC-2 coactivator results in a glycogenopathy resembling Von Gierke's disease (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-11-29
    Description: Hepatic glucose production is critical for basal brain function and survival when dietary glucose is unavailable. Glucose-6-phosphatase (G6Pase) is an essential, rate-limiting enzyme that serves as a terminal gatekeeper for hepatic glucose release into the plasma. Mutations in G6Pase result in Von Gierke's disease (glycogen storage disease-1a), a potentially fatal genetic disorder. We have identified the transcriptional coactivator SRC-2 as a regulator of fasting hepatic glucose release, a function that SRC-2 performs by controlling the expression of hepatic G6Pase. SRC-2 modulates G6Pase expression directly by acting as a coactivator with the orphan nuclear receptor RORalpha. In addition, SRC-2 ablation, in both a whole-body and liver-specific manner, resulted in a Von Gierke's disease phenotype in mice. Our results position SRC-2 as a critical regulator of mammalian glucose production.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2668604/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2668604/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chopra, Atul R -- Louet, Jean-Francois -- Saha, Pradip -- An, Jie -- Demayo, Franco -- Xu, Jianming -- York, Brian -- Karpen, Saul -- Finegold, Milton -- Moore, David -- Chan, Lawrence -- Newgard, Christopher B -- O'Malley, Bert W -- DK58242/DK/NIDDK NIH HHS/ -- HL51586/HL/NHLBI NIH HHS/ -- P01 DK059820/DK/NIDDK NIH HHS/ -- P01 DK059820-08/DK/NIDDK NIH HHS/ -- P01 DK58398/DK/NIDDK NIH HHS/ -- P01 DK59820/DK/NIDDK NIH HHS/ -- R01 DK056239/DK/NIDDK NIH HHS/ -- R01 DK056239-08/DK/NIDDK NIH HHS/ -- U19 DK062434/DK/NIDDK NIH HHS/ -- U19 DK062434-07/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2008 Nov 28;322(5906):1395-9. doi: 10.1126/science.1164847.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Baylor College of Medicine, 1 Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19039140" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Fasting ; Female ; Gene Expression Profiling ; Gene Expression Regulation, Enzymologic ; Glucose/*metabolism ; Glucose-6-Phosphatase/*genetics/metabolism ; Glycogen Storage Disease Type I/*genetics/metabolism ; Hepatocytes/metabolism ; Kidney/metabolism ; Liver/*metabolism ; Liver Glycogen/metabolism ; Male ; Mice ; Mice, Knockout ; Nuclear Receptor Coactivator 2/genetics/*metabolism ; RNA Interference ; Receptors, Retinoic Acid/metabolism ; Response Elements ; Transcription, Genetic ; Triglycerides/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
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    Regulation of a cyclin-CDK-CDK inhibitor complex by inositol pyrophosphates (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-04-07
    Description: In budding yeast, phosphate starvation triggers inhibition of the Pho80-Pho85 cyclin-cyclin-dependent kinase (CDK) complex by the CDK inhibitor Pho81, leading to expression of genes involved in nutrient homeostasis. We isolated myo-d-inositol heptakisphosphate (IP7) as a cellular component that stimulates Pho81-dependent inhibition of Pho80-Pho85. IP7 is necessary for Pho81-dependent inhibition of Pho80-Pho85 in vitro. Moreover, intracellular concentrations of IP7 increased upon phosphate starvation, and yeast mutants defective in IP7 production failed to inhibit Pho80-Pho85 in response to phosphate starvation. These observations reveal regulation of a cyclin-CDK complex by a metabolite and suggest that a complex metabolic network mediates signaling of phosphate availability.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2211727/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2211727/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Young-Sam -- Mulugu, Sashidhar -- York, John D -- O'Shea, Erin K -- DK070272/DK/NIDDK NIH HHS/ -- HL055672/HL/NHLBI NIH HHS/ -- R01 GM051377/GM/NIGMS NIH HHS/ -- R01 GM051377-15/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 6;316(5821):109-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Faculty of Arts and Sciences Center for Systems Biology, Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17412959" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/metabolism ; Cyclin-Dependent Kinases/*antagonists & inhibitors/metabolism ; Cyclins/*antagonists & inhibitors/metabolism ; DNA-Binding Proteins/metabolism ; Inositol Phosphates/*metabolism ; Phosphotransferases (Phosphate Group Acceptor)/genetics/metabolism ; Recombinant Proteins/metabolism ; Repressor Proteins/*antagonists & inhibitors/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/*antagonists & inhibitors/*metabolism ; Signal Transduction ; Transcription Factors/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 7
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    A conserved family of enzymes that phosphorylate inositol hexakisphosphate (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-04-07
    Description: Inositol pyrophosphates are a diverse group of high-energy signaling molecules whose cellular roles remain an active area of study. We report a previously uncharacterized class of inositol pyrophosphate synthase and find it is identical to yeast Vip1 and Asp1 proteins, regulators of actin-related protein-2/3 (ARP 2/3) complexes. Vip1 and Asp1 acted as enzymes that encode inositol hexakisphosphate (IP6) and inositol heptakisphosphate (IP7) kinase activities. Alterations in kinase activity led to defects in cell growth, morphology, and interactions with ARP complex members. The functionality of Asp1 and Vip1 may provide cells with increased signaling capacity through metabolism of IP6.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mulugu, Sashidhar -- Bai, Wenli -- Fridy, Peter C -- Bastidas, Robert J -- Otto, James C -- Dollins, D Eric -- Haystead, Timothy A -- Ribeiro, Anthony A -- York, John D -- 2-P30-CA14236-3/CA/NCI NIH HHS/ -- P30-CA-14236/CA/NCI NIH HHS/ -- R01-HL-55672/HL/NHLBI NIH HHS/ -- R33-DK-070272/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 6;316(5821):106-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Pharmacology and Cancer Biology, Duke University Medical Center, DUMC 3813, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17412958" target="_blank"〉PubMed〈/a〉
    Keywords: Actin-Related Protein 3/metabolism ; Amino Acid Sequence ; Animals ; Catalytic Domain ; Chromatography, High Pressure Liquid ; Conserved Sequence ; Cytoskeletal Proteins/chemistry/genetics/isolation & purification/*metabolism ; Humans ; Inositol Phosphates/metabolism ; Molecular Sequence Data ; Phosphorylation ; Phosphotransferases (Phosphate Group Acceptor)/chemistry/genetics/isolation & ; purification/*metabolism ; Phytic Acid/*metabolism ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/isolation & purification/metabolism ; Saccharomyces cerevisiae/*enzymology/genetics ; Saccharomyces cerevisiae Proteins/chemistry/genetics/isolation & ; purification/metabolism ; Schizosaccharomyces/cytology/*enzymology/genetics/growth & development ; Schizosaccharomyces pombe Proteins/chemistry/genetics/isolation & ; purification/*metabolism ; *Sequence Alignment ; Substrate Specificity ; Temperature
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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