Viewing affirmative mentions of binding of IL2 (H. sapiens) and Il2rb (M. musculus)

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Document Target Regulator Anatomy Sentence
Rebollo and Silva (1993)p70IL-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.
Kumar et al. (1987)IL-2RIL-2The respective role of IL-2 binding to HA-IL-2R and internalization of the complex has been examined.
Sugamura et al. (1992)IL-2R betaIL-2The comparative study between two subclones of lymphoid MOLT4 transfectant of IL-2R beta cDNA demonstrated that the amount of the gamma chain coprecipitated with IL-2R beta was proportional to numbers of the IL-2 binding sites.
Roessler et al. (1994)IL-2RIL-2This binding pattern is inconsistent with the strict hierarchical affinity-conversion model that mandates an initial binding of IL-2 to IL-2R alpha followed by binding of the IL-2/IL-2R alpha complex to IL-2R beta.
Roessler et al. (1994)IL-2RIL-2In this alternative model, IL-2R alpha and -beta exist in part as preformed complexes in which the affinity of IL-2R beta for IL-2 is altered by the proximity of IL-2R alpha, through mechanisms that do not require the prior binding of IL-2 to IL-2R alpha.
Roessler et al. (1994)IL-2RIL-2We demonstrated that IL-2 F42A, an analog that fails to bind to the isolated IL-2R alpha subunit and would be predicted by the hierarchical affinity-conversion model to have impaired binding to cells expressing both chains, instead readily binds to the IL-2R alpha/beta heterodimer in COS cells.
Mazur and Frydecka (1993)IL-2RInterleukin 2[Interleukin 2 (IL-2) and its receptor (IL-2R) in healthy individuals and with various disease states].
Gaffen (2001)IL-2RIL-2This review focuses on molecular signaling pathways triggered by the IL-2/IL-2R complex, with an emphasis on how the IL-2R physically translates its interaction with IL-2 into a coherent biological outcome.
Goldsmith et al. (1995)IL-2RIL-2Collectively, our findings suggest that the cytoplasmic domain of IL-2R beta produces intrasubunit transmembrane conformational changes in this receptor subunit that promote extracellular IL-2 binding in combination with IL-2R alpha.
Balasubramanian et al. (1995)IL-2RIL-2Studies on the binding of IL-2 to its receptor (IL-2R) have generally been limited to receptors expressed on cell surfaces.
Kuziel and Greene (1990)IL-2RIL-2Also, IL-2R beta appears centrally involved in internalization of IL-2 and signal transduction, functions mediated presumably through its long intracytoplasmic domain.
Allouche et al. (1989)IL-2RIL-2The association of both chains forms high affinity IL-2R, whereas each chain alone binds IL-2 with a low (alpha-chain) or intermediate (beta-chain) affinity.
Johnson et al. (1994)IL-2RIL-2While IL-2R beta and gamma cytoplasmic and transmembrane domains are not essential for interactive binding of IL-2, they may contribute to IL2 binding affinity.
Denis and Huber (2003)IL-2RmoIL-2We show that moIL-2 has high binding affinity for the IL-2 receptor (IL-2R), induces the immediate expression of the IL-2R alpha chain and rapidly activates downstream signaling molecules.
Marino and Preatoni (1991)IL-2Rinterleukin-2The interleukin-2 acts via interaction with high affinity, cell bound receptors (IL-2R).
de Jong et al. (1998)IL-2RbetaIL-2Monoclonal antibody 341, which recognizes IL-2Rbeta but does not inhibit IL-2 binding to the IL-2Rbeta chain, blocks 35.4+/-2.3% of IL-15-stimulated proliferation of PHA blasts, while not affecting the IL-2-stimulated proliferation.
Burdach et al. (1991)IL-2RIL-2Most biologic responses to IL-2 have been attributed to interaction of IL-2 with a high affinity receptor which consists of a heterodimer composed of two distinct IL-2-binding proteins (IL-2R alpha/IL-2R beta).
Lowenthal et al. (2001)IL-2RIL-2This method employs the chemical disuccinimidyl suberate (DSS) to achieve irreversible cross-linking of IL-2 to IL-2R.
de Jong et al. (1998)IL-2RbetaIL-2Some of this difference can be attributed to the role of the IL-2Rbeta chain, in that HuMikbeta1, a monoclonal antibody recognizing the IL-2Rbeta chain, blocks 92.2+/-2.5% (mean+/-SE) of the IL-2 proliferative response by Tf-1beta cells but only inhibits 57.9+/-3.7% of the IL-15 response, indicating that IL-2 and IL-15 may physically utilize the IL-2Rbeta chain differently.
Toribio et al. (1989)IL-2RIL-2Both molecules bind IL-2 independently, with low and intermediate affinity respectively, but only IL-2R beta is thought to mediate IL-2 signal transduction.
Toribio et al. (1989)IL-2RIL-2The IL-2/IL-2R beta interaction on these cells induces the expression of IL-2R alpha, leading to high-affinity IL-2R display and cellular proliferation.
Takaishi et al. (1990)IL-2RIL-2This assay system has good reproducibility, and was found to be specific for soluble IL-2R by examination of the binding of anti-IgM antibody or anti-IL-2R monoclonal antibody (mAb) with IgM or soluble IL-2R and inhibition by IL-2 of the binding of anti-IL-2R mAb to soluble IL-2R.
Zanetta et al. (1996)IL-2RIL-2This lectin activity is preserved after binding of IL-2 to IL-2R beta.
Zanetta et al. (1996)IL-2RIL-2IL-2 behaves as a bifunctional molecule that associates IL-2R beta with specific glycoprotein ligands of the TCR complex including a glycosylated form of CD3.
Ravichandran and Burakoff (1994)IL-2Rinterleukin-2Binding of interleukin-2 (IL-2) to the IL-2 receptor (IL-2R) stimulates Src family kinases, tyrosine phosphorylation of several proteins, conversion of Ras to its active GTP-bound form, and eventually c-fos, c-jun, and c-myc induction.
Pilson et al. (1997)IL-2RIL-2Humanized anti-Tac (HAT) and Mik beta1 (HuMik beta 1) Abs directed at IL-2R alpha and IL-2R beta, respectively, inhibit IL-2 binding and biological activity and together act synergistically in vitro.
Kim et al. (2002)IL-2RIL-2It has a different molecular structure but it functions like IL-2 by binding to the IL-2R beta and gammac chain.
Ferrag et al. (1996)IL-2R betaIL-2Otherwise, Jak1 and Jak3 are involved in IL-2 signaling through heterodimerization of the IL-2 receptor-beta (IL-2R beta) and gamma c-chains.