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  • 1
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    A G protein-linked receptor for parathyroid hormone and parathyroid hormone-related peptide (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-25
    Description: The complementary DNA encoding a 585-amino acid parathyroid hormone-parathyroid hormone-related peptide (PTH-PTHrP) receptor with seven potential membrane-spanning domains was cloned by COS-7 expression using an opossum kidney cell complementary DNA (cDNA) library. The expressed receptor binds PTH and PTHrP with equal affinity, and both ligands equivalently stimulate adenylate cyclase. Striking homology with the calcitonin receptor and lack of homology with other G protein-linked receptors indicate that receptors for these calcium-regulating hormones are related and represent a new family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Juppner, H -- Abou-Samra, A B -- Freeman, M -- Kong, X F -- Schipani, E -- Richards, J -- Kolakowski, L F Jr -- Hock, J -- Potts, J T Jr -- Kronenberg, H M -- DK 11794/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 15;254(5034):1024-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Endocrine Unit, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658941" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Membrane Glycoproteins/chemistry/genetics/metabolism ; Molecular Sequence Data ; Opossums ; Parathyroid Hormone/metabolism ; Parathyroid Hormone-Related Protein ; Proteins/metabolism ; Receptors, Cell Surface/chemistry/*genetics/metabolism ; Receptors, Parathyroid Hormone ; Sequence Alignment ; Solubility
    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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  • 2
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    Photosynthesis of previtamin D3 in human skin and the physiologic consequences (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-10-10
    Description: Photosynthesis of previtamin D3 can occur throughout the epidermis in the dermis when hypopigmented Caucasian skin is exposed to solar ultraviolet radiation. Once previtamin D3 is formed in the skin, it undergoes a temperature-dependent thermal isomerization that takes at least 3 days to complete. The vitamin D-binding protein preferentially translocates the thermal product, vitamin D3, into the circulation. These processes suggest a unique mechanism for the synthesis, storage, and slow, steady release of vitamin D3 from the skin into the circulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holick, M F -- MacLaughlin, J A -- Clark, M B -- Holick, S A -- Potts, J T Jr -- Anderson, R R -- Blank, I H -- Parrish, J A -- Elias, P -- AM25395-01/AM/NIADDK NIH HHS/ -- AM27334-01/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct 10;210(4466):203-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251551" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/metabolism ; Cholecalciferol/*biosynthesis ; Cholestadienols/*biosynthesis ; Dose-Response Relationship, Radiation ; Hot Temperature ; Humans ; Isomerism ; Photochemistry ; Rats ; Skin/cytology/*metabolism ; Ultraviolet Rays ; Vitamin D/metabolism ; Vitamin D-Binding Protein
    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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  • 3
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    Calcitonin messenger RNA encodes multiple polypeptides in a single precursor (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-07-24
    Description: Recombinant DNA techniques were used to analyze the structure of the messenger RNA encoding a precursor of calcitonin, a small calcium-regulating hormone of 32 amino acids. Analyses of the nucleotide sequences of cloned complementary DNA's comprising the entire coding sequence of the messenger RNA revealed that calcitonin is flanked at both its amino and carboxyl termini by peptide extensions linked to the hormone by short sequences of basic amino acids. The location of glycine next to the carboxyl terminal prolinamide of calcitonin is consistent with indications that glycine is required for the enzymatic amidation of proline to the prolinamide. During cellular biosynthesis, calcitonin arises from a large precursor protein by cleavages at both amino and carboxyl terminal residues of the hormone. These findings raise questions concerning the regulation of these cleavages and the potential biological functions of the precursor extensions derived from these cleavages.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobs, J W -- Goodman, R H -- Chin, W W -- Dee, P C -- Habener, J F -- Bell, N H -- Potts, J T Jr -- AM 27781-01/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 24;213(4506):457-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6264603" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcitonin/*genetics ; Cloning, Molecular ; DNA Restriction Enzymes ; DNA, Recombinant/*metabolism ; Macromolecular Substances ; Neoplasms, Experimental/metabolism ; Nucleic Acid Hybridization ; Peptide Biosynthesis ; Plants/metabolism ; Protein Biosynthesis ; RNA, Messenger/*genetics ; Rats ; Thyroid Neoplasms/metabolism ; Triticum/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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  • 4
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    A parathyroid hormone inhibitor in vivo: design and biological evaluation of a hormone analog (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-06-03
    Description: A synthetic analog of bovine parathyroid hormone (bPTH), [tyrosine-34] bPTH-(7-34)NH2, was found to inhibit parathyroid hormone action in vivo. When the analog and parathyroid hormone were infused simultaneously to rats at a molar ratio of 200 to 1, the analog inhibited the excretion of urinary phosphate and adenosine 3',5'-monophosphate. When infused alone at the same dose rate, the analog was devoid of agonist activity. The compound was prepared by following design principles developed for inhibitors of parathyroid hormone, and is believed to be the first antagonist of parathyroid hormone that is effective in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horiuchi, N -- Holick, M F -- Potts, J T Jr -- Rosenblatt, M -- AM11749/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1053-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6302844" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cyclic AMP/urine ; Dose-Response Relationship, Drug ; Male ; Parathyroid Hormone/*antagonists & inhibitors/*pharmacology ; Peptide Fragments/*pharmacology ; Phosphates/urine ; Rats
    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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