Tyrosine replacement in P-selectin glycoprotein ligand-1 affects distinct kinetic and mechanical properties of bonds with P- and L-selectin.
about
E-selectin ligand complexes adopt an extended high-affinity conformation.Von Willebrand factor-A1 domain binds platelet glycoprotein Ibα in multiple states with distinctive force-dependent dissociation kineticsCX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesionFunctional 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-selectinTyrosine sulfation enhances but is not required for PSGL-1 rolling adhesion on P-selectin.Complement factor H, vitronectin, and opticin are tyrosine-sulfated proteins of the retinal pigment epitheliumComparison of PSGL-1 microbead and neutrophil rolling: microvillus elongation stabilizes P-selectin bond clusters.The Effects of Load on E-Selectin Bond Rupture and Bond Formation.P-selectin glycoprotein ligand-1-deficient mice have impaired leukocyte tethering to E-selectin under flow.A structure-based sliding-rebinding mechanism for catch bonds.Flow-enhanced adhesion regulated by a selectin interdomain hinge.Selectin catch-slip kinetics encode shear threshold adhesive behavior of rolling leukocytesEvolutionary conservation of P-selectin glycoprotein ligand-1 primary structure and functionThe high affinity selectin glycan ligand C2-O-sLex and mRNA transcripts of the core 2 beta-1,6-N-acetylglucosaminyltransferase (C2GnT1) gene are highly expressed in human colorectal adenocarcinomas.Fibulin 2, a tyrosine O-sulfated protein, is up-regulated following retinal detachment.C2-O-sLeX glycoproteins are E-selectin ligands that regulate invasion of human colon and hepatic carcinoma cells.Dimerization of a selectin and its ligand stabilizes cell rolling and enhances tether strength in shear flowHuman L-selectin preferentially binds synthetic glycosulfopeptides modeled after endoglycan and containing tyrosine sulfate residues and sialyl Lewis x in core 2 O-glycansDiffusion of microspheres in shear flow near a wall: use to measure binding rates between attached molecules.Kinetics of GPIbalpha-vWF-A1 tether bond under flow: effect of GPIbalpha mutations on the association and dissociation rates.A semianalytic model of leukocyte rolling.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 simulationsThe two-pathway model for the catch-slip transition in biological adhesion.P-selectin glycoprotein ligand-1 forms dimeric interactions with E-selectin but monomeric interactions with L-selectin on cell surfaces.Selectin receptor-ligand bonds: Formation limited by shear rate and dissociation governed by the Bell modelChemically distinct transition states govern rapid dissociation of single L-selectin bonds under force.Transport governs flow-enhanced cell tethering through L-selectin at threshold shear.The state diagram for cell adhesion under flow: leukocyte rolling and firm adhesion.O-glycans direct selectin ligands to lipid rafts on leukocytes.Transport features, reaction kinetics and receptor biomechanics controlling selectin and integrin mediated cell adhesion.Tyrosine replacement of PSGL-1 reduces association kinetics with P- and L-selectin on the cell membrane.Cytoplasmic anchorage of L-selectin controls leukocyte capture and rolling by increasing the mechanical stability of the selectin tether.Avidity enhancement of L-selectin bonds by flow: shear-promoted rotation of leukocytes turn labile bonds into functional tethers.Distinct molecular and cellular contributions to stabilizing selectin-mediated rolling under flow.Stiff substrates enhance monocytic cell capture through E-selectin but not P-selectinAdhesive dynamics simulations of the mechanical shedding of L-selectin from the neutrophil surface.Bromelain decreases neutrophil interactions with P-selectin, but not E-selectin, in vitro by proteolytic cleavage of P-selectin glycoprotein ligand-1Glycosylation in immune cell trafficking.
P2860
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P2860
Tyrosine replacement in P-selectin glycoprotein ligand-1 affects distinct kinetic and mechanical properties of bonds with P- and L-selectin.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Tyrosine replacement in P-sele ...... bonds with P- and L-selectin.
@ast
Tyrosine replacement in P-sele ...... bonds with P- and L-selectin.
@en
type
label
Tyrosine replacement in P-sele ...... bonds with P- and L-selectin.
@ast
Tyrosine replacement in P-sele ...... bonds with P- and L-selectin.
@en
prefLabel
Tyrosine replacement in P-sele ...... bonds with P- and L-selectin.
@ast
Tyrosine replacement in P-sele ...... bonds with P- and L-selectin.
@en
P2093
P2860
P356
P1476
Tyrosine replacement in P-sele ...... f bonds with P- and L-selectin
@en
P2093
M U Nollert
R D Cummings
R P McEver
V Ramachandran
P2860
P304
13771-13776
P356
10.1073/PNAS.96.24.13771
P407
P50
P577
1999-11-01T00:00:00Z