Kinetic analysis of ligand binding to interleukin-2 receptor complexes created on an optical biosensor surface.
about
Crystal Structure of the interleukin-15.interleukin-15 receptor alpha complex: insights into trans and cis presentationPeptides targeting caspase inhibitors.Identification of troponin C antagonists from a phage-displayed random peptide library.Cyclic peptides as non-carboxyl-terminal ligands of syntrophin PDZ domains.Extending the range of rate constants available from BIACORE: interpreting mass transport-influenced binding data.Modeling the receptor pharmacology, pharmacokinetics, and pharmacodynamics of NKTR-214, a kinetically-controlled interleukin-2 (IL2) receptor agonist for cancer immunotherapy.Simultaneous measurement of 10,000 protein-ligand affinity constants using microarray-based kinetic constant assays.Quantitative Contribution of IL2Rγ to the Dynamic Formation of IL2-IL2R Complexes.Solution assembly of the pseudo-high affinity and intermediate affinity interleukin-2 receptor complexesInteraction affinity between cytokine receptor components on the cell surface.Slow-dissociation effect of common signaling subunit beta c on IL5 and GM-CSF receptor assembly.Identification of a gene for an ancient cytokine, interleukin 15-like, in mammals; interleukins 2 and 15 co-evolved with this third family member, all sharing binding motifs for IL-15Rα.Structural insights into the common γ-chain family of cytokines and receptors from the interleukin-7 pathway.Molecular dissection of the interactions of an antitumor interleukin-2-derived mutein on a phage display-based platform.Overview of the quantitation of protein interactions.Increased endosomal sorting of ligand to recycling enhances potency of an interleukin-2 analog.Probing the binding mechanism and affinity of tanezumab, a recombinant humanized anti-NGF monoclonal antibody, using a repertoire of biosensors.Cell-to-cell variability analysis dissects the plasticity of signaling of common γ chain cytokines in T cells.Label-free determination of protein-ligand binding constants using mass spectrometry and validation using surface plasmon resonance and isothermal titration calorimetry.P15 peptide stimulates chondrogenic commitment and endochondral ossification.Use of GPI-anchored proteins to study biomolecular interactions by surface plasmon resonance.Possible mechanism for the alpha subunit of the interleukin-2 receptor (CD25) to influence interleukin-2 receptor signal transduction
P2860
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P2860
Kinetic analysis of ligand binding to interleukin-2 receptor complexes created on an optical biosensor surface.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Kinetic analysis of ligand bin ...... an optical biosensor surface.
@ast
Kinetic analysis of ligand bin ...... an optical biosensor surface.
@en
type
label
Kinetic analysis of ligand bin ...... an optical biosensor surface.
@ast
Kinetic analysis of ligand bin ...... an optical biosensor surface.
@en
prefLabel
Kinetic analysis of ligand bin ...... an optical biosensor surface.
@ast
Kinetic analysis of ligand bin ...... an optical biosensor surface.
@en
P2093
P2860
P921
P356
P1433
P1476
Kinetic analysis of ligand bin ...... an optical biosensor surface.
@en
P2093
D G Myszka
P R Arulanantham
T A Morton
T L Ciardelli
P2860
P304
P356
10.1002/PRO.5560051209
P577
1996-12-01T00:00:00Z