Viewing affirmative mentions of binding of IL2 (H. sapiens) and P4HB (H. sapiens)

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Saltzman et al. (1989)p55IL-2Antibodies that inhibit binding of IL-2 to p55 had no effect on the IL-2-induced tyrosine phosphorylations in YT cells, while antibodies that block the binding of IL-2 to p75 completely inhibited the phosphorylations.
Lowenthal and Greene (1987)p55IL-2In this report, we have investigated the kinetics of IL-2 binding to the alpha (p55) and beta (p70) IL-2 binding proteins and compared these properties with ligand binding to the high-affinity IL-2-R.
Lowenthal and Greene (1987)p55IL-2The association and dissociation of IL-2 to the alpha (p55) chain occurred with very rapid kinetics (t 1/2 = 4-10 s).
Sauvé et al. (1991)p55IL-2These results confirm the importance of the B alpha-helix in IL-2 as the locus for p55-receptor binding and support a revised model of IL-2-IL-2 receptor interaction.
Sauvé et al. (1991)p55IL-2The dissociation constants of Arg-38 and Phe-42 analogs for p70 were consistent with intermediate-affinity binding; the Kd values were not significantly affected by the presence of p55 in binding to the high-affinity IL-2 receptor complex.
Minamoto et al. (1989)p55interleukin 2The Tac antigen (p55, CD25) is a 55 kDa glycoprotein that binds interleukin 2 at low affinity (Kd congruent to 10-50 nM).
Sauvé et al. (1991)p55IL-2Human interleukin 2 (IL-2) analogs with defined amino acid substitutions were used to identify specific residues that interact with the 55-kDa subunit (p55) or alpha chain of the human IL-2 receptor.
Galanaud et al. (1990)p55-p70IL-2The interaction of IL-4 with its own receptors might influence the state of p55-p70/75 complex association or act on a third subunit of the IL-2 receptor.
Waldmann (1987)p55IL-2Cell lines bearing either the p55, Tac, or the p75 peptide alone manifested low-affinity IL-2 binding, whereas cell lines bearing both peptides manifested both high- and low-affinity receptors.
Waldmann (1987)p55IL-2Cell lines bearing either the p55, Tac, or the p75 peptide alone manifested low-affinity IL-2 binding, whereas cell lines bearing both peptides manifested both high- and low-affinity receptors.
Perkins et al. (1993)p55IL-2The role of IL-2 interaction with p75 and p55 receptor molecules in the stimulation of cell proliferation.
Begley et al. (1990)p55IL-2In the HCL samples, a small number of high-affinity IL-2 binding sites were detected (27-90) while the majority of binding sites (2100-10,800) were typical of low-affinity p55 Tac binding.
Waldmann and Tsudo (1988)p55IL-2Cell lines bearing either the p55, Tac, or the p75 peptide alone manifested low-affinity IL-2 binding, whereas cell lines bearing both peptides manifested both high- and low-affinity receptors.
Tomizawa et al. (1991)p55IL-2The high-affinity interleukin-2 (IL-2) receptor (IL-2R) consists of the non-covalent association of at least two subunits, p55 and p70-75, capable of binding IL-2 with low and intermediate affinity, respectively.
Collins et al. (1988)p55interleukin 2Analogs of interleukin 2 containing defined amino acid substitutions and deletions were assayed for bioactivity and for competitive binding to the high-affinity human interleukin 2 receptor complex and its two component subunits, a 55-kDa subunit (p55 or TAC) and a 70-kDa subunit (p70).
Wong et al. (1990)p55IL-2Monoclonal antibodies were used to determine the relationships between epitopes on the p55 chain of the IL-2 receptor and high-affinity IL-2 binding.
Tsudo et al. (1989)p55IL-2The high-affinity IL-2R results from the noncovalent association between at least two subunits; alpha (p55) and beta (p70), both of which are capable of binding IL-2 with a low and intermediate affinity, respectively.
Shindo et al. (1990)p55IL-2These results show that the signalling through the IL-2/IL-2R system down-regulates KOLT-2 (CD28) antigen by way of the interaction between IL-2 and IL-2R (p70), irrespective of IL-2R (p55)/Tac.
Tsudo et al. (1989)p55IL-2The human high-affinity receptor for interleukin 2 (IL-2) has been proposed as being a membrane complex composed of at least two distinct polypeptide chains: p55 (alpha chain), recognized by the anti-Tac monoclonal antibody (mAb), and p75 (beta chain), both of which are capable of binding IL-2.
Rebollo et al. (1992)p55IL-2Immunochemical characterization of antigenic domains on human IL-2: spatially distinct epitopes are associated with binding to the p55 and p70 subunits of IL-2 receptor.
Wong et al. (1990)p55IL-2Together these data suggest that there are at least four distinct immunogenic epitopes on the human p55 chain, with three epitopes related to IL-2 binding.
Wong et al. (1990)p55IL-2These antibodies were used to map epitopes on the p55 chain and determine their relationship to high-affinity IL-2 binding.
Wong et al. (1990)p55IL-2-bindingThese studies indicated that the IL-2-binding site and site of interaction between the p55 and p70 chains are close together or identical.
Watson et al. (1988)p55IL2Growth of this clone was inhibited by the monoclonal antibody 2A3 which specifically blocked binding of human IL2 to the human p55 binding protein.
Watson et al. (1988)p55IL2If IL2 signal transduction involves binding to a surface heterodimeric receptor for IL2, it is argued that FD.huIL2R-2 cells contain an IL2 receptor complex of murine p70 and human p55 IL2-binding proteins.
Flemming et al. (1993)p55IL-2Mutation of Asp20 in human interleukin-2 (IL-2) to Lys is known to result in an IL-2 molecule with unchanged binding to the p55 subunit of the IL-2 receptor, but with greatly decreased affinity for the p75 subunit (Collins, L., Tsien, W.
Kanakura et al. (1993)p55IL-2The action of IL-2 is known to be mediated through binding to a specific IL-2 receptor (IL-2R) which comprises at least two distinct proteins: IL-2R alpha (p55) and IL-2R beta (p70-75).
Minamoto et al. (1990)p55IL-2Two IL-2R components have been identified as IL-2R alpha (p55, Tac Ag) and IL-2R beta (p70-75) chains, both bind IL-2 with low and intermediate affinities, respectively.
Osawa and Diamantstein (1989)p55IL-2In contrast, the mAb PC61, that was previously reported to recognize a determinant distal to the IL-2 binding site on the mouse p55 subunit of IL-2R and to dissociate IL-2 from the high-affinity IL-2R complex by altering the conformation of the p55 molecule itself, inhibited the low-affinity binding and cross-linking of IL-2 to the p55 molecule on mouse p55 cDNA-transfected cells.
Osawa and Diamantstein (1989)p55IL-2Both mAbs inhibited the high-affinity binding and crosslinking of IL-2 to the p55 + p75 heterodimeric complex on forskolin-treated YT cells.
Osawa and Diamantstein (1989)p55IL-2Remarkably, the AHT-107 did not inhibit the low-affinity binding and cross-linking of IL-2 to the p55 molecule on human p55 cDNA-transfected cells, while the AHT-54 as well as anti-Tac did so.
Collins (1989)p55IL 2While the murine p55 showed an identical species preference to the murine p55/p75 high-affinity complex, the human p55 had an equal affinity for human and murine IL 2.