Dimerization of a selectin and its ligand stabilizes cell rolling and enhances tether strength in shear flow
about
Clustering endothelial E-selectin in clathrin-coated pits and lipid rafts enhances leukocyte adhesion under flowCatch bonds govern adhesion through L-selectin at threshold shearQuantitative Characterization of E-selectin Interaction with Native CD44 and P-selectin Glycoprotein Ligand-1 (PSGL-1) Using a Real Time Immunoprecipitation-based Binding Assay.Lateral clustering of platelet GP Ib-IX complexes leads to up-regulation of the adhesive function of integrin alpha IIbbeta 3Functional analysis of the combined role of the O-linked branching enzyme core 2 beta1-6-N-glucosaminyltransferase and dimerization of P-selectin glycoprotein ligand-1 in rolling on P-selectinGlycosyltransferase-programmed stereosubstitution (GPS) to create HCELL: engineering a roadmap for cell migrationBinding of ADAM28 to P-selectin glycoprotein ligand-1 enhances P-selectin-mediated leukocyte adhesion to endothelial cellsComparison of PSGL-1 microbead and neutrophil rolling: microvillus elongation stabilizes P-selectin bond clusters.Molecular stiffness of selectins.The Effects of Load on E-Selectin Bond Rupture and Bond Formation.Action at a distance: lengthening adhesion bonds with poly(ethylene glycol) spacers enhances mechanically stressed affinity for improved vascular targeting of microparticlesNano-motion dynamics are determined by surface-tethered selectin mechanokinetics and bond formation.Neutrophil-bead collision assay: pharmacologically induced changes in membrane mechanics regulate the PSGL-1/P-selectin adhesion lifetime.The molecular mechanics of P- and L-selectin lectin domains binding to PSGL-1P-selectin glycoprotein ligand-1-deficient mice have impaired leukocyte tethering to E-selectin under flow.Nano-to-micro scale dynamics of P-selectin detachment from leukocyte interfaces. III. Numerical simulation of tethering under flowEvolutionary conservation of P-selectin glycoprotein ligand-1 primary structure and functionDynamics of unbinding of cell adhesion molecules: transition from catch to slip bonds.Two by two: the pairings of P-selectin and P-selectin glycoprotein ligand 1.Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow: the GPIb(alpha)-vWF tether bond.Biomechanics of leukocyte rollingKinetics of GPIbalpha-vWF-A1 tether bond under flow: effect of GPIbalpha mutations on the association and dissociation rates.Force history dependence of receptor-ligand dissociation.Low force decelerates L-selectin dissociation from P-selectin glycoprotein ligand-1 and endoglycan.Effect of microvillus deformability on leukocyte adhesion explored using adhesive dynamics simulationsP-selectin glycoprotein ligand-1 forms dimeric interactions with E-selectin but monomeric interactions with L-selectin on cell surfaces.Cytoplasmic domain of P-selectin glycoprotein ligand-1 facilitates dimerization and export from the endoplasmic reticulumL-selectin transmembrane and cytoplasmic domains are monomeric in membranes.Transport governs flow-enhanced cell tethering through L-selectin at threshold shear.PSGL-1 and mTOR regulate translation of ROCK-1 and physiological functions of macrophages.Fibrin serves as a divalent ligand that regulates neutrophil-mediated melanoma cells adhesion to endothelium under shear conditionsCytoplasmic anchorage of L-selectin controls leukocyte capture and rolling by increasing the mechanical stability of the selectin tether.Signal-dependent distribution of cell surface P-selectin in clathrin-coated pits affects leukocyte rolling under flowDistinct molecular and cellular contributions to stabilizing selectin-mediated rolling under flow.Distinct kinetic and mechanical properties govern mucin 16- and podocalyxin-mediated tumor cell adhesion to E- and L-selectin in shear flow.Stiff substrates enhance monocytic cell capture through E-selectin but not P-selectinDynamic alterations of membrane tethers stabilize leukocyte rolling on P-selectinRolling cell adhesionPSGL-1-dependent myeloid leukocyte activation.Duplicated binding sites for (1-->3)-beta-D-glucan in the horseshoe crab coagulation factor G: implications for a molecular basis of the pattern recognition in innate immunity.
P2860
Q24301203-03909752-15AA-4730-A25B-0C193DD1A426Q24677022-2887E527-514D-44C5-8A6C-4EF65275CEE7Q27313560-610B895E-C83F-4324-A864-F54197D04344Q28216733-04C6CAD7-AF0B-48E1-BFE9-A200329D6BCBQ28251004-B9C345A8-C37C-4E78-81DB-0BAE47B118F7Q28251644-E4D0B781-0852-4E79-85AF-DD1C0DF83479Q28307734-7B32672A-0CB7-4DD4-A5D0-DE5E8E146516Q30309150-5943E815-C902-426C-A326-82BC06189496Q30427805-8AA9E8F7-6406-46E8-BE6C-895DEF994E1EQ30432073-56F4ADCD-E93F-4060-8911-4E4EF4B0072DQ30433477-B04443E7-2222-4A28-84F4-0C8AB890E023Q30437627-45180552-B9BD-46B4-BFE2-0FD6A767A788Q30445741-739A9F76-9EB6-422F-A07C-AD40ADCF32D7Q30447415-FF3CF8BB-7C77-4D9F-9E32-2CE08B4B1116Q30453100-A4950C08-67CF-4839-A13A-C88EB1366EF5Q33209499-388579AF-5607-4EF0-BE45-A16C8DF8F5F9Q33299016-FD26FF67-233A-4145-9EFE-ED4724ED3D12Q33836369-C6397F7A-AE32-4605-B70E-D6CA5717F566Q33942883-DDE7FC9E-F264-4E37-BE4C-86A17E34B063Q34178256-F951A747-3E45-4F0C-B20E-ABE9D4357D5EQ34180215-E89C8F8E-A3BE-4501-B2A3-FDDE266A90EBQ34184053-9848309B-7A33-4F5C-9747-5FAB61D2CE62Q34189025-5C755626-69AD-457A-89A3-1A66ACD2BEA2Q34271778-8733D6E1-4D45-4269-9A7A-A7F48502BDCFQ34350381-7A0ADAE9-8980-4796-99F7-9A78EC74E6ACQ34603261-5F19580B-83AB-493E-AE05-03299911D016Q34685383-33AA748B-7BA6-4DD9-B3A0-E1B1DD3C11ECQ34810114-5AA3E183-21B1-4DFD-945F-BD43E4E9EB46Q35220087-51DFADC3-7525-4B75-8C44-5D89F44973E8Q35612494-3378F826-8E14-4498-81D6-053C0D15BEA0Q35900663-F173467B-76B8-4750-8E5D-410CB4180ED0Q36294017-7FC96031-904D-4945-B440-1FBF621A1CBCQ36324917-E14702CC-C197-4F30-8CBE-95B96B2B360BQ36325671-02498E13-5EB4-4EDA-A4EC-3EA2329718D5Q36413037-AD9F1DBD-86BB-447B-AEFF-1B8E4B3C1F05Q36502506-59BD8370-F608-44F3-814C-A1D1CDD2C731Q37534814-3BFA610D-E00C-4E5B-9382-2CF36C480619Q37540219-8E841DC0-6C2F-42C8-AF4D-656DAC83421DQ37585925-E689C9ED-7CDA-405D-8F13-0A55FD482204Q38292261-47FB0ED1-5A2E-434B-8B4F-860A4C833E6B
P2860
Dimerization of a selectin and its ligand stabilizes cell rolling and enhances tether strength in shear flow
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Dimerization of a selectin and ...... tether strength in shear flow
@ast
Dimerization of a selectin and ...... tether strength in shear flow
@en
type
label
Dimerization of a selectin and ...... tether strength in shear flow
@ast
Dimerization of a selectin and ...... tether strength in shear flow
@en
prefLabel
Dimerization of a selectin and ...... tether strength in shear flow
@ast
Dimerization of a selectin and ...... tether strength in shear flow
@en
P2093
P2860
P356
P1476
Dimerization of a selectin and ...... tether strength in shear flow
@en
P2093
M M Kobzdej
M U Nollert
R D Cummings
R P McEver
T K Epperson
V Ramachandran
P2860
P304
10166-10171
P356
10.1073/PNAS.171248098
P407
P577
2001-07-31T00:00:00Z