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  • 1
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    NOBEL 2012 Chemistry: Studies of a ubiquitous receptor family (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-12-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roth, Bryan L -- Marshall, Fiona H -- England -- Nature. 2012 Dec 6;492(7427):57. doi: 10.1038/492057a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23222609" target="_blank"〉PubMed〈/a〉
    Keywords: Biochemistry/history ; *Chemistry/history ; Drug Discovery/history ; High-Throughput Screening Assays/history ; History, 20th Century ; History, 21st Century ; Humans ; *Nobel Prize ; Receptors, G-Protein-Coupled/genetics/isolation & purification/*metabolism ; Structure-Activity Relationship
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Structure of class B GPCR corticotropin-releasing factor receptor 1 (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-07-19
    Description: Structural analysis of class B G-protein-coupled receptors (GPCRs), cell-surface proteins that respond to peptide hormones, has been restricted to the amino-terminal extracellular domain, thus providing little understanding of the membrane-spanning signal transduction domain. The corticotropin-releasing factor receptor type 1 is a class B receptor which mediates the response to stress and has been considered a drug target for depression and anxiety. Here we report the crystal structure of the transmembrane domain of the human corticotropin-releasing factor receptor type 1 in complex with the small-molecule antagonist CP-376395. The structure provides detailed insight into the architecture of class B receptors. Atomic details of the interactions of the receptor with the non-peptide ligand that binds deep within the receptor are described. This structure provides a model for all class B GPCRs and may aid in the design of new small-molecule drugs for diseases of brain and metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hollenstein, Kaspar -- Kean, James -- Bortolato, Andrea -- Cheng, Robert K Y -- Dore, Andrew S -- Jazayeri, Ali -- Cooke, Robert M -- Weir, Malcolm -- Marshall, Fiona H -- England -- Nature. 2013 Jul 25;499(7459):438-43. doi: 10.1038/nature12357. Epub 2013 Jul 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City AL7 3AX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23863939" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Aminopyridines/chemistry/metabolism/pharmacology ; Binding Sites ; Conserved Sequence ; Crystallography, X-Ray ; HEK293 Cells ; Humans ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Structure, Tertiary ; Receptors, Corticotropin-Releasing Hormone/antagonists & ; inhibitors/*chemistry/*classification/metabolism ; Receptors, Dopamine D3/antagonists & inhibitors/chemistry/classification
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Structure of class C GPCR metabotropic glutamate receptor 5 transmembrane domain (2014)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2014-07-22
    Description: Metabotropic glutamate receptors are class C G-protein-coupled receptors which respond to the neurotransmitter glutamate. Structural studies have been restricted to the amino-terminal extracellular domain, providing little understanding of the membrane-spanning signal transduction domain. Metabotropic glutamate receptor 5 is of considerable interest as a drug target in the treatment of fragile X syndrome, autism, depression, anxiety, addiction and movement disorders. Here we report the crystal structure of the transmembrane domain of the human receptor in complex with the negative allosteric modulator, mavoglurant. The structure provides detailed insight into the architecture of the transmembrane domain of class C receptors including the precise location of the allosteric binding site within the transmembrane domain and key micro-switches which regulate receptor signalling. This structure also provides a model for all class C G-protein-coupled receptors and may aid in the design of new small-molecule drugs for the treatment of brain disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dore, Andrew S -- Okrasa, Krzysztof -- Patel, Jayesh C -- Serrano-Vega, Maria -- Bennett, Kirstie -- Cooke, Robert M -- Errey, James C -- Jazayeri, Ali -- Khan, Samir -- Tehan, Ben -- Weir, Malcolm -- Wiggin, Giselle R -- Marshall, Fiona H -- England -- Nature. 2014 Jul 31;511(7511):557-62. doi: 10.1038/nature13396. Epub 2014 Jul 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City, Hertfordshire AL7 3AX, UK [2]. ; Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City, Hertfordshire AL7 3AX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25042998" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Binding Sites ; Crystallography, X-Ray ; HEK293 Cells ; Humans ; *Models, Molecular ; Protein Structure, Tertiary ; Receptor, Metabotropic Glutamate 5/*chemistry ; Rhodopsin/chemistry
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 4
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    Extra-helical binding site of a glucagon receptor antagonist (2016)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2016-04-26
    Description: Glucagon is a 29-amino-acid peptide released from the alpha-cells of the islet of Langerhans, which has a key role in glucose homeostasis. Glucagon action is transduced by the class B G-protein-coupled glucagon receptor (GCGR), which is located on liver, kidney, intestinal smooth muscle, brain, adipose tissue, heart and pancreas cells, and this receptor has been considered an important drug target in the treatment of diabetes. Administration of recently identified small-molecule GCGR antagonists in patients with type 2 diabetes results in a substantial reduction of fasting and postprandial glucose concentrations. Although an X-ray structure of the transmembrane domain of the GCGR has previously been solved, the ligand (NNC0640) was not resolved. Here we report the 2.5 A structure of human GCGR in complex with the antagonist MK-0893 (ref. 4), which is found to bind to an allosteric site outside the seven transmembrane (7TM) helical bundle in a position between TM6 and TM7 extending into the lipid bilayer. Mutagenesis of key residues identified in the X-ray structure confirms their role in the binding of MK-0893 to the receptor. The unexpected position of the binding site for MK-0893, which is structurally similar to other GCGR antagonists, suggests that glucagon activation of the receptor is prevented by restriction of the outward helical movement of TM6 required for G-protein coupling. Structural knowledge of class B receptors is limited, with only one other ligand-binding site defined--for the corticotropin-releasing hormone receptor 1 (CRF1R)--which was located deep within the 7TM bundle. We describe a completely novel allosteric binding site for class B receptors, providing an opportunity for structure-based drug design for this receptor class and furthering our understanding of the mechanisms of activation of these receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jazayeri, Ali -- Dore, Andrew S -- Lamb, Daniel -- Krishnamurthy, Harini -- Southall, Stacey M -- Baig, Asma H -- Bortolato, Andrea -- Koglin, Markus -- Robertson, Nathan J -- Errey, James C -- Andrews, Stephen P -- Teobald, Iryna -- Brown, Alastair J H -- Cooke, Robert M -- Weir, Malcolm -- Marshall, Fiona H -- England -- Nature. 2016 Apr 25;533(7602):274-7. doi: 10.1038/nature17414.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City, Hertfordshire AL7 3AX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27111510" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 5
    Electronic Resource
    Electronic Resource
    Light as a Factor in Sexual Periodicity (1932)
    [s.l.] : Nature Publishing Group
    Nature 129 (1932), S. 344-361 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] IN the discussion which followed the papers by Dr. J. R. Baker and Mr. R. M. Ranson and Prof. T. H. Bissonette, read before the Royal Society on Feb. 4, I suggested that their conclusions concerning light as a factor in sexual periodicity involved a principle of wide application. Dr. Baker had ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/129344b0
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  • 6
    Electronic Resource
    Electronic Resource
    Biological Fact and Theory (1927)
    [s.l.] : Nature Publishing Group
    Nature 119 (1927), S. 563-563 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THE discussion in NATURE under the above heading appears to me to be based in large measure upon failure to realise the character of scientific knowledge. Such misunderstanding is to be deprecated as being contrary to the interests of further progress in biology. I beg leave, therefore, to ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/119563b0
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  • 7
    Electronic Resource
    Electronic Resource
    The Ovarian Hormones (1929)
    [s.l.] : Nature Publishing Group
    Nature 124 (1929), S. 94-94 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THE writer of an article on “The Hormones of the Sexual Glands” in NATURE of June 15, p. 913, says that “the castrous reaction of ovariectomised animals following an injection of ‘œstrin’ appears incomplete, in that copulation is only infrequently observed, and in the spayed bitch the hormone ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/124094c0
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  • 8
    Electronic Resource
    Electronic Resource
    The Corpus Luteum and the Cause of Birth (1928)
    [s.l.] : Nature Publishing Group
    Nature 122 (1928), S. 242-242 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] As I pointed out in the article referred to by Prof. Thomson Flynn in NATURE of June 30, p. 1020 (Biol. Rev., 2, 129; 1927), parturition is certainly due to several factors, of which the decline of the corpus luteum is probably one. Moreover, the enlargement of the pregnant uterus is ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/122242e0
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  • 9
    Electronic Resource
    Electronic Resource
    Image orthicon threshold detection of stars and satellites
    Amsterdam : Elsevier
    Infrared Physics 4 (1964), S. 199-208 
    Details
    ISSN: 0020-0891
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0020-0891(64)90026-0
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  • 10
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    The GABAB receptor interacts directly with the related transcription factors CREB2 and ATFx (2000)
    National Academy of Sciences
    Details
    Publication Date: 2000-11-21
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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