Zobrazeno 1 - 10
of 966
pro vyhledávání: '"C, Stahle"'
Publikováno v:
Biochemistry. 47:2884-2892
This investigation examined the molecular mechanisms that enable the alphaIIbbeta3 integrin to bind efficiently, tightly, and selectively to echistatin, an RGD disintegrin. We used surface plasmon resonance spectroscopy to measure the rate, extent, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5087ed51c2be28facb47f4f0aac95921
https://doi.org/10.1021/bi701877a
https://doi.org/10.1021/bi701877a
Publikováno v:
Journal of Thrombosis and Haemostasis. 5:542-550
Background Drugs that block platelet-platelet and platelet-fibrin interactions via the alpha(IIb)beta(3) (glycoprotein IIb/IIIa) receptor are used daily in patients undergoing percutaneous coronary interventions. Along with expected increases in spon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a0819492e78d52d6c88f61a5c88d33f
https://doi.org/10.1111/j.1538-7836.2007.02351.x
https://doi.org/10.1111/j.1538-7836.2007.02351.x
Publikováno v:
Thrombosis and Haemostasis. 87:910-917
SummaryA biophysical approach tested the hypothesis that tirofiban, like eptifibatide, perturbs GpIIb/IIIa structure. Tirofiban bound tightly to platelet GpIIb/IIIa (EC50 ∼ 24 nmol/L) and effectively inhibited platelet aggregation (IC50 ∼ 37 nmol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::30fd337ea10502e39b37bb329d79cfa3
https://doi.org/10.1055/s-0037-1613104
https://doi.org/10.1055/s-0037-1613104
Autor:
Douglas S. Lyles, W.G Jerome, V Del Gaizo, Margie O. McKenzie, M Adams, T Lasher, Mary C. Stahle, Roy R. Hantgan
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1540(1):82-95
The platelet integrin αIIbβ3 exhibits bidirectional signaling, in that intracellular messengers enable adhesive macromolecules to bind to its ectodomain, while ligation promotes the association of cytoskeletal proteins with its cytoplasmic domains.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d23b0193b6ecc62fc53517ea15b9d48
Autor:
Meulewaeter, Evelyn1 (AUTHOR), Eylenbosch, Anke1 (AUTHOR), Verhaeghe, Evelien1 (AUTHOR), Soenen, Rani1 (AUTHOR), Lambert, Jo1 (AUTHOR) Jo.Lambert@uzgent.be
Publikováno v:
Dermatology & Therapy. Oct2024, Vol. 14 Issue 10, p2889-2903. 15p.
Autor:
Lebwohl, Mark G.1 (AUTHOR) lebwohl@aol.com, Armstrong, April W.2 (AUTHOR), Alexis, Andrew F.3 (AUTHOR), Lain, Edward L.4 (AUTHOR), Jacobson, Abby A.5 (AUTHOR)
Publikováno v:
Dermatology & Therapy. Oct2024, Vol. 14 Issue 10, p2709-2726. 18p.
Autor:
GH Mickisch, I Aksentijevich, PV Schoenlein, LJ Goldstein, H Galski, C Stahle, DH Sachs, I Pastan, MM Gottesman
Publikováno v:
Blood. 79:1087-1093
Many human cancers that are initially responsive to chemotherapy eventually fail to respond to treatment. For some drugs, dose escalation that may be required for a cure cannot be achieved because sensitive tissues such as bone marrow (BM) limit cyto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c34c561a695784d07c41e631e21323cf
https://doi.org/10.1182/blood.v79.4.1087.1087
https://doi.org/10.1182/blood.v79.4.1087.1087
Autor:
Mary C. Stahle, Roy R. Hantgan
Publikováno v:
Biochemistry. 48(35)
This investigation addressed the paradox that disintegrins and small RGD-ligands readily bind to the resting alphaIIbbeta3 integrin, while macromolecules with similar integrin recognition motifs require an activated, or primed, receptor. Three struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b925de41faa82558f5bbeb998285e253
https://pubmed.ncbi.nlm.nih.gov/19640007
https://pubmed.ncbi.nlm.nih.gov/19640007
Autor:
Mary C. Stahle, Clinton Orebaugh, Jillian G. Rouse, Luke Burnett, Roy R. Hantgan, Mark Van Dyke
Publikováno v:
The FASEB Journal. 23
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::770c8500becaff9ae2d297db9371dfdc
https://doi.org/10.1096/fasebj.23.1_supplement.638.4
https://doi.org/10.1096/fasebj.23.1_supplement.638.4
Autor:
Mary C. Stahle, Mary Ann McLane, David A. Horita, Sergiy Yakovlev, Mattia Rocco, John H. Connor, Leonid Medved, Roy R. Hantgan
Publikováno v:
Protein science : a publication of the Protein Society. 15(8)
This study tested the hypothesis that high-affinity binding of macromolecular ligands to the alphaIIbbeta3 integrin is tightly coupled to binding-site remodeling, an induced-fit process that shifts a conformational equilibrium from a resting toward a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57df6c7f36d1588b50345c7c24fe7d3d
https://pubmed.ncbi.nlm.nih.gov/16877710
https://pubmed.ncbi.nlm.nih.gov/16877710