Low molecular weight, non-peptide fibrinogen receptor antagonists.
about
Affinity modulation of platelet integrin alphaIIbbeta3 by beta3-endonexin, a selective binding partner of the beta3 integrin cytoplasmic tailRegulation of the pp72syk protein tyrosine kinase by platelet integrin alpha IIb beta 3A model of platelet aggregation involving multiple interactions of thrombospondin-1, fibrinogen, and GPIIbIIIa receptor.The molecular adapter SLP-76 relays signals from platelet integrin alphaIIbbeta3 to the actin cytoskeleton.The therapeutic use of glycoprotein IIb/IIIa inhibitors in acute coronary syndromes.Actual Role of Platelet Glycoprotein IIb/IIIa Receptor Inhibitors as Adjunctive Pharmacological Therapy to Primary Angioplasty in Acute Myocardial Infarction: In the Light of Recent Randomized Trials and Observational Studies with Bivalirudin.Efficiency of platelet adhesion to fibrinogen depends on both cell activation and flowDeath effector domain protein PEA-15 potentiates Ras activation of extracellular signal receptor-activated kinase by an adhesion-independent mechanismA genetic analysis of integrin function: Glanzmann thrombasthenia in vitroModulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity.β-Subunit Binding Is Sufficient for Ligands to Open the Integrin αIIbβ3 Headpiece.Pharmacological antithrombotic adjuncts to percutaneous coronary intervention.Blood-borne tissue factor: another view of thrombosisConformational preferences of alpha-substituted proline analoguesStereoselective Synthesis of Quaternary Proline Analogues.Trans-dominant inhibition of integrin function.Progress in the research of GPIIb/IIIa antagonists.Mimicking Peptides… In Silico.Sequential regulation of the small GTPase Rap1 in human platelets.Distinct domains of CD98hc regulate integrins and amino acid transport.Class- and splice variant-specific association of CD98 with integrin beta cytoplasmic domains.Conformational variability of benzamidinium-based inhibitorsR-Ras C-terminal sequences are sufficient to confer R-Ras specificity to H-Ras.Breaking the integrin hinge. A defined structural constraint regulates integrin signaling.The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity.The amino-terminal one-third of alpha IIb defines the ligand recognition specificity of integrin alpha IIb beta 3.The death effector domain of PEA-15 is involved in its regulation of integrin activation.Platelet recruitment to venous stent thrombi.Computer-aided design of amino acid-based therapeutics: a review.Prevention of αIIbβ3 activation by non-steroidal antiinflammatory drugsMolecular insights into aggregates made of amphiphilic Fmoc-tetrapeptidesSelf-assembly of Fmoc-tetrapeptides based on the RGDS cell adhesion motif
P2860
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P2860
Low molecular weight, non-peptide fibrinogen receptor antagonists.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh-hant
name
Low molecular weight, non-peptide fibrinogen receptor antagonists.
@en
Low molecular weight, non-peptide fibrinogen receptor antagonists.
@nl
type
label
Low molecular weight, non-peptide fibrinogen receptor antagonists.
@en
Low molecular weight, non-peptide fibrinogen receptor antagonists.
@nl
prefLabel
Low molecular weight, non-peptide fibrinogen receptor antagonists.
@en
Low molecular weight, non-peptide fibrinogen receptor antagonists.
@nl
P2093
P356
P1476
Low molecular weight, non-peptide fibrinogen receptor antagonists.
@en
P2093
Edenhofer A
Hürzeler M
Trzeciak A
P304
P356
10.1021/JM00101A017
P407
P577
1992-11-01T00:00:00Z