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  • American Association for the Advancement of Science (AAAS)  (3)
  • 2015-2019  (1)
  • 1985-1989  (1)
  • 1975-1979  (1)
  • 1
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    Prostaglandin E1 inhibitis platelet aggregation by a pathway independent of adenosine 3',5'-monophosphate (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-04-14
    Description: Aggregation of human blood platelets induced by adenosine diphosphate or 1-epinephrine was inhibited when the platelets were suspended in plasma which had been previously exposed to an insolubilized omega-aminohexylagarose derivative of prostaglandin E1. This decrease of platelet aggregation was not accompanied by a change in the concentration of adenosine 3',5'-monophosphate (cyclic AMP) in platelets. The results demonstrate the existence of an alternative pathway independent of cyclic AMP for the inhibition of platelet aggregation by plasma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sinha, A K -- Colman, R W -- New York, N.Y. -- Science. 1978 Apr 14;200(4338):202-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/204997" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/antagonists & inhibitors ; Cyclic AMP/*blood ; Epinephrine/antagonists & inhibitors ; Humans ; Plasma/physiology ; Platelet Aggregation/*drug effects ; Prostaglandins E, Synthetic/*pharmacology ; Sepharose/analogs & derivatives ; 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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    Prostacyclin stimulation of the activation of blood coagulation factor X by platelets (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-24
    Description: When platelets were incubated with prostacyclin, prostaglandin E1, or prostaglandin D2 at concentrations insufficient to increase the level of adenosine 3',5'-monophosphate (cyclic AMP), coagulation factor X was activated by a platelet cysteine protease. Prostacyclin or prostaglandin E1 at higher concentrations increased the cyclic AMP level and inhibited the activation of factor X by platelets. Inhibition of platelet adenylate cyclase by 2',5'-dideoxyadenosine allowed the activation of the protease at higher concentrations of the autocoids. Prostaglandins A1, A2, B1, B2, E2, F2 alpha, 6-keto-prostaglandin F1 alpha, and thromboxane B2, which do not affect platelet cyclic AMP level, did not stimulate the protease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dutta-Roy, A K -- Ray, T K -- Sinha, A K -- New York, N.Y. -- Science. 1986 Jan 24;231(4736):385-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3001935" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Alprostadil/pharmacology ; Animals ; Blood Platelets/*drug effects/metabolism/physiology ; Cattle ; Cyclic AMP/metabolism ; Deoxyadenosines/analogs & derivatives/pharmacology ; *Dideoxyadenosine/*analogs & derivatives ; Epoprostenol/*pharmacology ; Factor X/*physiology ; Humans ; Peptide Hydrolases/metabolism ; Prostaglandin D2 ; Prostaglandins/pharmacology ; Prostaglandins D/pharmacology
    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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    [Research Article] Distortion of histone octamer core promotes nucleosome mobilization by a chromatin remodeler (2017)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2017-01-20
    Description: Adenosine 5′-triphosphate (ATP)–dependent chromatin remodeling enzymes play essential biological roles by mobilizing nucleosomal DNA. Yet, how DNA is mobilized despite the steric constraints placed by the histone octamer remains unknown. Using methyl transverse relaxation–optimized nuclear magnetic resonance spectroscopy on a 450-kilodalton complex, we show that the chromatin remodeler, SNF2h, distorts the histone octamer. Binding of SNF2h in an activated ATP state changes the dynamics of buried histone residues. Preventing octamer distortion by site-specific disulfide linkages inhibits nucleosome sliding by SNF2h while promoting octamer eviction by the SWI-SNF complex, RSC. Our findings indicate that the histone core of a nucleosome is more plastic than previously imagined and that octamer deformation plays different roles based on the type of chromatin remodeler. Octamer plasticity may contribute to chromatin regulation beyond ATP-dependent remodeling. Authors: Kalyan K. Sinha, John D. Gross, Geeta J. Narlikar
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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