Výsledky vyhledávání - "R M, Scarborough"

Immunologic analysis of the cloned platelet thrombin receptor activation mechanism: evidence supporting receptor cleavage, release of the N-terminal peptide, and insertion of the tethered ligand into a protected environment

Autor: K J, Norton, R M, Scarborough, J L, Kutok, M A, Escobedo, L, Nannizzi, B S, Coller

Publikováno v: Blood. 82:2125-2136

The recently cloned functional thrombin receptor is thought to be activated by thrombin cleavage of the bond between R41 and S42, followed by the insertion of the new N-terminal region (“tethered ligand”) into an unknown site in the receptor. Ant

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d17f300c2a0e337526ff1bbb580a2eb
https://doi.org/10.1182/blood.v82.7.2125.bloodjournal8272125

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Spirocyclic nonpeptide glycoprotein IIb-IIIa antagonists. Part 2: design of potent antagonists containing the 3-azaspiro[5.5]undecanes

Autor: A, Pandey, J, Seroogy, D, Volkots, M S, Smyth, J, Rose, M M, Mehrotra, J, Heath, G, Ruhter, T, Schotten, R M, Scarborough

Publikováno v: Bioorganicmedicinal chemistry letters. 11(10)

The synthesis and biological activity of novel glycoprotein IIb-IlIa anatagonists containing 3-azaspiro[5.5]undec-9-yl nucleus are described. The potent activity of these compounds as platelet aggregation inhibitors demonstrates the utility of the mo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::af39e623841a517b4c4afde34bb0e3fc
https://pubmed.ncbi.nlm.nih.gov/11392540

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Structure-activity relationships of beta-amino acid-containing integrin antagonists

Autor: R M, Scarborough

Publikováno v: Current medicinal chemistry. 6(10)

Interest in the development of specific antagonists of the beta3 family of integrins (platelet alphaIIbbeta3 and the vitronectin receptor alphavbeta3) has been principally driven by efforts to design more potent antithrombotic agents than either aspi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3401b5892d6add58806da0c391297235
https://pubmed.ncbi.nlm.nih.gov/10519908

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Endocytosis of fibrinogen into megakaryocyte and platelet alpha-granules is mediated by alpha IIb beta 3 (glycoprotein IIb-IIIa)

Autor: P, Handagama, R M, Scarborough, M A, Shuman, D F, Bainton

Publikováno v: Blood. 82(1)

Recently, we showed that platelet alpha-granule fibrinogen is derived entirely from endocytic uptake and not from megakaryocyte synthesis, as previously thought. In this present report, we identify the receptor that mediates endocytosis. We have foun

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8ba1678b53f1f6ca1d2fa4055613d0f1
https://pubmed.ncbi.nlm.nih.gov/8391871

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Design of potent and specific integrin antagonists. Peptide antagonists with high specificity for glycoprotein IIb-IIIa

Autor: R M, Scarborough, M A, Naughton, W, Teng, J W, Rose, D R, Phillips, L, Nannizzi, A, Arfsten, A M, Campbell, I F, Charo

Publikováno v: The Journal of biological chemistry. 268(2)

Members of the snake venon-derived, "disintegrin" peptide family containing the Arg-Gly-Asp (RGD) amino acid sequence are among the most potent inhibitors of the binding of adhesive proteins to platelet glycoprotein (GP) IIb-IIIa. However, GPIIb-IIIa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::679eb6de36ac165daacac3f65ae2fd20
https://pubmed.ncbi.nlm.nih.gov/8419315

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Characterization of the integrin specificities of disintegrins isolated from American pit viper venoms

Autor: R M, Scarborough, J W, Rose, M A, Naughton, D R, Phillips, L, Nannizzi, A, Arfsten, A M, Campbell, I F, Charo

Publikováno v: The Journal of biological chemistry. 268(2)

A new series of homologous disintegrins was isolated from the venoms of new world pit viper genus Bothrops, Crotalus, and Lachesis. The relative activities of each disintegrin in blocking adhesive protein binding activities of GPIIb-IIIa, alpha v bet

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2220f8e58a797bf712640a6851be699e
https://pubmed.ncbi.nlm.nih.gov/8419314

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Tethered ligand agonist peptides. Structural requirements for thrombin receptor activation reveal mechanism of proteolytic unmasking of agonist function

Autor: R M, Scarborough, M A, Naughton, W, Teng, D T, Hung, J, Rose, T K, Vu, V I, Wheaton, C W, Turck, S R, Coughlin

Publikováno v: The Journal of biological chemistry. 267(19)

The human platelet thrombin receptor is activated when thrombin cleaves its receptor's amino-terminal extension to reveal a new amino terminus that functions as a tethered peptide ligand. Exactly how this "agonist peptide domain" remains cryptic with

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::451ecb90fe50bef1384bfb5ffbaa6466
https://pubmed.ncbi.nlm.nih.gov/1320011

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