Viewing affirmative mentions of binding of IL2 (H. sapiens) and IL2RB (H. sapiens)

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Hakimi et al. (1987)IL-2RIL-2This immunosorbent receptor assay offers a simple and rapid method for studying the binding of IL-2 to human IL-2R.
Moreau et al. (1995)IL-2RIL-2Epitope of mAb 3H9 is localized between residues 30 and 54 and does not affect the binding of IL-2 to IL-2R alpha.
Suzuki et al. (1989)p75IL-2TU11 mAb did not block IL-2 binding to the high-affinity IL-2R at all and precipitated p75 bound with IL-2.
Moreau et al. (1995)IL-2RIL-2These observations have lead to the hypothesis that its epitope is related to an IL-2 area involved in binding with IL-2R beta chain.
Moreau et al. (1995)IL-2RIL-2Characterization of a monoclonal antibody directed against the NH2 terminal area of interleukin-2 (IL-2) and inhibiting specifically the binding of IL-2 to IL-2 receptor beta chain (IL-2R beta).
Moreau et al. (1995)IL-2RIL-2This further demonstrates that the NH2 terminal area of IL-2 is critical for IL-2/IL-2R beta interactions.
Hakimi et al. (1987)IL-2RIL-2The soluble forms of IL-2R were shown to retain IL-2 affinity shown by cell-surface IL-2R (Kd approximately 18 nM) and were purified to homogeneity using IL-2 affinity chromatography.
Hatakeyama et al. (1989)p70-75IL-2Interleukin-2 (IL-2) binds to two distinct receptor molecules, the IL-2 receptor alpha (IL-2R alpha, p55) chain and the newly identified IL-2 receptor beta (IL-2R beta, p70-75) chain.
Audrain et al. (1991)p75 chainIL-2TU27 and IL-2 bound to the isolated p75 chain expressed by YT-2C2 cells with respective dissociation constants (Kd) of 1.3 and 1 nM.
Siegel et al. (1987)IL-2RIL-2A novel glycoprotein (IL-2R beta), identified on several lymphocytoid cell lines, has the ability to bind IL-2 alone and to associate with Tac antigen (IL-2R alpha) to form high-affinity IL-2 receptors.
Tomizawa et al. (1991)p70-75IL-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.
Sugamura et al. (1990)IL-2RIL-2-bindingWe previously established a monoclonal antibody, TU11 mAb, which is specific for human IL-2 receptor (IL-2R) beta chain (p75) and does not inhibit IL-2-binding to IL-2R beta.
Stauber et al. (2006)IL-2RIL-2The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
Suzuki et al. (1989)p75IL-2IL-2 receptor subunit, p75: direct demonstration of its IL-2 binding ability by using a novel monoclonal antibody.
Caligiuri et al. (1993)IL-2RIL-2Further activation of NK cytolytic activity can also be achieved in vivo, but it requires concentrations of IL-2 that bind intermediate affinity IL-2R p75.
Johnson and Smith (1990)p75IL-2Moreover, the effect of cAMP on IL-2 binding to p75 subunits is post-transcriptional, because the steady state levels of p75 mRNA expression are not altered within a time interval that produced nearly a 50% reduction in p75 binding.
Waters et al. (1990)p75 subunitDAB486-IL 2We also demonstrate that an alteration in the binding of DAB486-IL 2 to the p75 subunit of the IL 2R may account for the selective cytotoxicity of DAB486-IL 2 for cells bearing the heterodimeric high-affinity IL 2R.
Osawa and Diamantstein (1989)p75IL-2Both mAbs inhibited the high-affinity binding and crosslinking of IL-2 to the p55 + p75 heterodimeric complex on forskolin-treated YT cells.
Stauber et al. (2006)IL-2RIL-2Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
Audrain et al. (1991)p75 chainIL-2Both antibody were found to synergize on 4AS cells, as a result of a cooperative mechanism in which 33B3.1 blocks the formation of the high affinity complex hence allowing TU27 to bind with higher affinity, and TU27 blocks IL-2 binding to the p75 chain.
Kanakura et al. (1993)IL-2RIL-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).
Kanakura et al. (1993)IL-2RIL-2The expression of IL-2R beta on M07E cells was detectable with 125I-IL-2 binding and affinity cross-linking analyses and with a monoclonal antibody against IL-2R beta, Mik-beta 1.
Kasinrerk et al. (1994)IL-2RIL-2The enhancing effect of anti-IL-2R alpha antibody, observed in both murine and human systems, reinforces the possibility that binding of IL-2 to the IL-2R alpha chain plays a negative regulatory role in signal transduction.
Minamoto et al. (1990)IL-2RIL-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.
Eckenberg et al. (1997)IL-2RIL-2Interleukin 2 (IL-2) interacts with a receptor (IL-2R) composed of three subunits (IL-2R alpha, IL-2R beta and IL-2R gamma).
Harvill and Morrison (1995)IL-2RIgG3-IL2In contrast, IgG3-IL2 shows a greater affinity than hrIL-2 for the high affinity IL-2R, consisting of alpha, beta and gamma subunits.
Harvill and Morrison (1995)IL-2RIgG3-IL2Competition studies show that IgG3-IL2 binds the intermediate affinity form of the IL-2 receptor (IL-2R), consisting of the beta and gamma subunits, with an affinity slightly less than that of hrIL-2.
Kuhn et al. (2003)IL-2RIL-2The beta and gamma chains of IL-2R have intermediate binding affinity for IL-2 and are responsible for the intracellular signaling cascades after IL-2 stimulation.
Sugie et al. (1990)IL-2RIL-2Rp75Pre-incubation of YT cells with 20 micrograms/ml YTA-1 mAb accelerated the internalization of IL-2Rp75 but did not accelerate that of IL-2Rp55, indicating that YTA-1-induced down-regulation of IL-2R is associated with the internalization of IL-2Rp75.
Niguma et al. (1991)p75IL-2Recent chemical linking studies have demonstrated that the human high-affinity IL-2 receptor is a membrane complex composed of at least two distinct subunits, which are the p55 (alpha-chain) and p75 (beta-chain) subunits.
Plaisance et al. (1993)IL-2RIL-2These chains are able to specifically bind IL-2 and to form high-affinity heterodimers (IL-2R alpha beta).
Rebollo and Silva (1993)IL-2RIL-2Taken together, our results strongly suggest that human and murine IL-2R beta molecules are different since interaction of IL-2 with human p70 IL-2R is sufficient for transduction of proliferative signals in the absence of p55 IL-2R or, alternatively, that over-expression of the IL-2R beta chain renders cells responsive to IL-2.
Lin et al. (1988)IL-2RIL-2-LIn addition, biotinylated IL-2-L was capable of simultaneously binding to cell surface IL-2R and streptavidin.
Saito and Honjo (1990)IL-2RIL-2Kinetic studies on the IL-2 binding to the high-affinity IL-2R have shown that the association of IL-2 to the L chain is the first step of the ternary complex formation and that expression of a larger number of L chains accelerates the association of IL-2 to the high-affinity IL-2R in agreement with the stepwise binding/affinity conversion model.
Adachi et al. (1997)IL-2RIL-2Coupling of interleukin-2 (IL-2) to the IL-2 receptor (IL-2R) induces rapid increase in tyrosine phosphorylation of cellular substrates through activation of non-receptor protein tyrosine kinases.
de Jong et al. (1996)IL-2RIL-2This study was designed to compare the interactions of IL-2 and IL-15 with the IL-2R beta and IL-2R gamma c subunits, as differences in receptor interactions between IL-2 and IL-15 might contribute to the functional differences between these two cytokines.
Smart et al. (1990)IL-2Rinterleukin-2We have developed a ligand-affinity method for the medium-scale purification of these two soluble forms of the IL-2R, based on the biochemical interactions between the matrix-bound ligand (interleukin-2) and its soluble receptor.
Arima et al. (1992)IL-2RIL-2Using electrophoretic mobility shift assays and DNA-protein cross-linking techniques, we demonstrate that IL-2 binding to functional forms of the human IL-2R activates nuclear expression of the eukaryotic transcription factor NF-kappa B.
Collins (1989)p75IL 2These data suggest that the amino terminal region of the IL 2 molecule interacts with the p75 chain of the IL 2 receptor.
Takeshita et al. (1992)IL-2RIL-2The IL-2R on murine fibroblastoid cells can be internalized after binding IL-2 only if the gamma chain is present; alpha and beta are insufficient for internalization.
Okamoto et al. (1990)IL-2RIL-2When the cDNA was expressed in a human oligodendroglioma cell line, ONS-21, the IL-2R beta bound IL-2 with an affinity similar to that in lymphoid cells (Kd, approximately 2 nM).
García-Tuñnón et al. (2004)IL-2RIL-2The correlation (r) between the immunoexpression intensity of IL-2 and each receptor chain was as follows: IL-2/IL-2R?
Liang et al. (1988)IL-2RIL-2These results suggest that binding of IL-2 and mutant proteins to the IL-2R beta component of the high-affinity receptor is essential for the induction of biological effects.
Takeshita et al. (1992)IL-2RIL-2Two subclones, MOLT beta-11 and MOLT beta-12, of an IL-2R beta cDNA-transfected MOLT4 clone expressed similar numbers of IL-2R beta molecules on cell surfaces and bound to IL-2 with intermediate affinity.
Takeshita et al. (1992)IL-2RIL-2Two functional parameters associated with IL-2R, IL-2 binding ability and association of p64 with the beta-chain, were examined.
Grant et al. (1992)IL-2RIL-2The 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.
Grant et al. (1992)IL-2RIL-2Med. 168, 1563-1572] that predicted an ordered sequence of events in which IL-2 must first bind to IL-2R alpha before its interaction with IL-2R beta.
Grant et al. (1992)IL-2RIL-2The IL-2R alpha-mediated augmentation of IL-2R beta functions involves affinity conversion of IL-2R beta, increasing its affinity for IL-2, and may involve facilitation of Il-2-mediated signaling after binding of IL-2 to this IL-2R beta.
Vitte-Mony et al. (1994)IL-2RIL-2Furthermore, dose response experiments, and blocking studies performed with anti-IL-2R alpha antibodies, indicated that binding of IL-2 to the IL-2R beta chain was sufficient to produce these modifications of p56lck.
Grant et al. (1992)IL-2RIL-2Furthermore, we used two forms of IL-2, recombinant native IL-2 and F42A, an IL-2 analog (Phe-42----Ala substitution) that binds only to IL-2R beta.
Grant et al. (1992)IL-2RIL-2Previously with the reagents available it was difficult to define functional interactions between these two IL-2R subunits involved in IL-2 binding and signal transduction.
Takeshita et al. (1989)IL-2RIL-2TU27 mAb completely blocked IL-2 binding to IL-2Rp75 and to the high-affinity IL-2R but not to IL-2Rp55 composing the low-affinity IL-2R.
Heaton et al. (1994)IL-2RIL-2METHODS: Human PBMCs were stimulated with 1 nM wild-type recombinant IL-2 (rIL-2) or IL-2 analogs (R38A or F42K) that preferentially bind to the intermediate affinity IL-2 receptor (IL-2R).
Heaton et al. (1994)IL-2RIL-2CONCLUSIONS: IL-2 analogs that preferentially bind the intermediate-affinity IL-2R retain the capacity to induce substantial LAK activity despite a greatly reduced secondary cytokine production.
Fujii et al. (1988)IL-2RIL-2These results support a supposition that the high affinity IL-2R is generated by assembly of the alpha and beta chains, and suggest that the IL-2 binding to IL-2R alpha and beta chains could induce stable constitution of the high-affinity state of IL-2R, but these affinity modulating reagents could perturb the optimum association between alpha and beta chains to generate the high-affinity IL-2R.
Dionyssopoulou et al. (2000)IL-2RIL-2One approach is the synthesis of peptides that interfere with the binding of interleukin-2 (IL-2) to its high affinity receptor (IL-2R).
Kierszenbaum et al. (1989)IL-2RIL-2The Kd for IL-2 binding to the fewer IL-2R expressed on PBMC exposed to T. cruzi was not significantly different from that of IL-2R on nonsuppressed PBMC.
Fujii et al. (1988)IL-2RIL-2On treatment with the reagents, the IL-2 binding to both IL-2R alpha and beta chains was inhibited and these inhibitory effects were seen only when the reagents were added before IL-2 addition, like their high-affinity reducing effects.
Warren et al. (1996)IL-2RIL-2IFN-gamma was secreted in cultures containing rIL-12, whereas IL-5 secretion was dependent upon interaction of IL-2 with the high affinity IL-2R.
Mentz et al. (1994)IL-2RIL-2The ligation of IL-2R by IL-2 rescued T-ALL cells from death and promoted their progression toward more mature cells expressing extracellular CD3/TCR alpha beta complexes.