Mouse interleukin-2 structure-function studies: substitutions in the first alpha-helix can specifically inactivate p70 receptor binding and mutations in the fifth alpha-helix can specifically inactivate p55 receptor binding
about
Definition and spatial location of mouse interleukin-2 residues that interact with its heterotrimeric receptorConversion of human interleukin-4 into a high affinity antagonist by a single amino acid replacement.Structure-function analysis of interleukin-5 utilizing mouse/human chimeric molecules.The interleukin 2 receptor (IL-2R): the IL-2R alpha subunit alters the function of the IL-2R beta subunit to enhance IL-2 binding and signaling by mechanisms that do not require binding of IL-2 to IL-2R alpha subunit.Role of interleukin-2 and herpes simplex virus 1 in central nervous system demyelination in miceLocalization in human interleukin 2 of the binding site to the alpha chain (p55) of the interleukin 2 receptorReceptors for interleukin-13 and interleukin-4 are complex and share a novel component that functions in signal transductionTwo distinct functional sites of human interleukin 4 are identified by variants impaired in either receptor binding or receptor activation.Structure-activity relationship study of human interleukin-3: role of the C-terminal region for biological activity.The amino-terminal helix of GM-CSF and IL-5 governs high affinity binding to their receptors.Partial agonist/antagonist mouse interleukin-2 proteins indicate that a third component of the receptor complex functions in signal transduction.Identification of three adjacent amino acids of interleukin-2 receptor beta chain which control the affinity and the specificity of the interaction with interleukin-2.Receptor antagonist and selective agonist derivatives of mouse interleukin-2.Receptor binding properties of four-helix-bundle growth factors deduced from electrostatic analysis.An interleukin 4 (IL-4) mutant protein inhibits both IL-4 or IL-13-induced human immunoglobulin G4 (IgG4) and IgE synthesis and B cell proliferation: support for a common component shared by IL-4 and IL-13 receptors
P2860
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P2860
Mouse interleukin-2 structure-function studies: substitutions in the first alpha-helix can specifically inactivate p70 receptor binding and mutations in the fifth alpha-helix can specifically inactivate p55 receptor binding
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Mouse interleukin-2 structure- ...... nactivate p55 receptor binding
@en
type
label
Mouse interleukin-2 structure- ...... nactivate p55 receptor binding
@en
prefLabel
Mouse interleukin-2 structure- ...... nactivate p55 receptor binding
@en
P2860
P1433
P1476
Mouse interleukin-2 structure- ...... nactivate p55 receptor binding
@en
P2093
Zurawski G
Zurawski SM
P2860
P304
P407
P577
1989-09-01T00:00:00Z