Amino acid residues in the alpha IIb subunit that are critical for ligand binding to integrin alpha IIbbeta 3 are clustered in the beta-propeller model.
about
Structure and function of the platelet integrin alphaIIbbeta3Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin α IIb β 3Molecular basis of the recognition of nephronectin by integrin alpha8beta1Epitopes in α8β1 and other RGD-binding integrins delineate classes of integrin-blocking antibodies and major binding loops in α subunitsHeparin modulates the conformation and signaling of platelet integrin αIIbβ3Ligand-induced Epitope Masking: DISSOCIATION OF INTEGRIN α5β1-FIBRONECTIN COMPLEXES ONLY BY MONOCLONAL ANTIBODIES WITH AN ALLOSTERIC MODE OF ACTION.Glanzmann thrombasthenia: state of the art and future directions.Humanized mouse model of thrombosis is predictive of the clinical efficacy of antiplatelet agents.Combined protein- and nucleic acid-level effects of rs1143679 (R77H), a lupus-predisposing variant within ITGAMInsights into integrin-ligand binding and activation from the first crystal structure.The interaction of integrin αIIbβ3 with fibrin occurs through multiple binding sites in the αIIb β-propeller domain.EmTIP, a T-Cell immunomodulatory protein secreted by the tapeworm Echinococcus multilocularis is important for early metacestode development.Humanizing thrombi in mice.Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeuticsDynamic regulation of fibrinogen: integrin αIIbβ3 binding.Tests of the extension and deadbolt models of integrin activationThe integrins.Species differences in small molecule binding to alpha IIb beta 3 are the result of sequence differences in 2 loops of the alpha IIb beta propellerOn the activation of integrin αIIbβ3: outside-in and inside-out pathways.Comparison of common platelet receptors between the chacma baboon (Papio ursinus) and human for use in pre-clinical human-targeted anti-platelet studies.A 13-bp deletion in alpha(IIb) gene is a founder mutation that predominates in Palestinian-Arab patients with Glanzmann thrombasthenia.Mutations in and near the second calcium-binding domain of integrin alphaIIb affect the structure and function of integrin alphaIIbbeta3.Structural requirements for activation in alphaIIb beta3 integrin.Mapping the ligand-binding pocket of integrin alpha5beta1 using a gain-of-function approach.Key interactions in integrin ectodomain responsible for global conformational change detected by elastic network normal-mode analysis.Structure of an integrin-ligand complex deduced from solution x-ray scattering and site-directed mutagenesis.Mapping the binding domains of the alpha(IIb) subunit. A study performed on the activated form of the platelet integrin alpha(IIb)beta(3).Membrane-proximal {alpha}/{beta} stalk interactions differentially regulate integrin activation.Identification of a novel binding site for platelet integrins alpha IIb beta 3 (GPIIbIIIa) and alpha 5 beta 1 in the gamma C-domain of fibrinogen.Novel mutations in Thai patients with glanzmann thrombasthenia.Expanding the Mutation Spectrum Affecting αIIbβ3 Integrin in Glanzmann Thrombasthenia: Screening of the ITGA2B and ITGB3 Genes in a Large International Cohort.
P2860
Q24536159-33F38F76-D1B6-49EC-8C6E-059F1E2EA4ADQ27651670-E3CCF88C-4EE3-44FF-B032-BA84D29209D0Q28507330-2C334723-053D-4E61-9F89-2F313C5C0D50Q28607846-CCDF2235-7510-4D91-A18C-CB7419D9BCD0Q30513893-1337D562-49D9-49D1-A811-DED6D9DCA3FFQ30826108-1F9CBFEC-650D-48C1-BF0E-45F4186DE3E4Q33571529-FF9FEB0B-B322-46A6-9C9D-C45771423777Q33789829-14C41EED-50B7-4D18-BCCC-CF6BF5485015Q33847584-8251DFED-1E7B-41FF-8F45-78D01C572E6CQ34731123-695062C4-F9EC-4F4C-AD7C-83DD07180DA7Q35066799-B9E16D8E-76E7-4EEF-9E4F-CF724672C653Q35083536-D8AC9234-2A3C-43D9-9813-E65F7B1A9984Q35109254-0E8DC745-D891-4200-948B-76F7A3BE75F5Q35213036-E5B4527A-DCAD-4D21-AEFD-1E3102197BB5Q35533290-A0425084-C18A-4A79-915B-4050DEF06997Q35951243-8CBE0B80-8680-4260-9E5E-079B9E38D398Q36837362-F783C494-0E38-455D-B656-56D83D395F51Q37071125-B5515CC2-77BE-43DA-B975-0F453DC8F2BEQ37204375-67CE7631-4DA0-4B3E-9DDE-EDFD25B7D435Q38943762-1E6C9D59-28DA-4F41-A5FA-70333AE6E1B0Q40339375-D63680A0-5C78-4D72-AAC7-2FF80F06F075Q40608458-BDB21803-CEC6-4FB3-87BF-9349994FF38EQ41500222-EABDAEDE-C3FF-496F-BE88-F5FB314502E4Q41963794-63B24505-0640-4DA3-8F79-64ACC437F275Q42183468-A65B1DC4-7AB5-41A1-BB8E-431D319B0869Q44519392-4A33797F-45B3-4835-94EC-357FB37646DAQ44569954-01316B9A-0F96-4A55-82BC-F1D648300D38Q46465757-E8A314B6-536E-444E-9C9C-FFFC8A2446B9Q47844689-1A7AC680-D180-421A-8481-381F9ED1B6A3Q48099018-74357E45-9A6C-4C6F-A232-23667FAB6723Q49155547-BA73262D-98D3-40FF-AA1F-86CEE2EF0EC3
P2860
Amino acid residues in the alpha IIb subunit that are critical for ligand binding to integrin alpha IIbbeta 3 are clustered in the beta-propeller model.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
Amino acid residues in the alp ...... d in the beta-propeller model.
@en
Amino acid residues in the alp ...... d in the beta-propeller model.
@nl
type
label
Amino acid residues in the alp ...... d in the beta-propeller model.
@en
Amino acid residues in the alp ...... d in the beta-propeller model.
@nl
prefLabel
Amino acid residues in the alp ...... d in the beta-propeller model.
@en
Amino acid residues in the alp ...... d in the beta-propeller model.
@nl
P2093
P2860
P356
P1476
Amino acid residues in the alp ...... d in the beta-propeller model.
@en
P2093
P2860
P304
44275-44283
P356
10.1074/JBC.M107021200
P407
P577
2001-09-13T00:00:00Z