再论别价：多位点磷酸化和底物再结合的分析
Allovalency revisited: an analysis of multisite phosphorylation and substrate rebinding
摘要：
利用多个磷酸化位点调节生物反应在细胞信号转导中是普遍存在的。如果每个位点都提供了一个额外的、等价的结合位点，那么磷酸化数量增加的一个结果可能是增加了配体在解离后立即与其受体重新结合的概率。这些效应如何影响细胞信号转导系统的研究较少。在这里，一个自洽的配体结合的积分方程形式主义，结合蒙特卡罗模拟，被用来进一步研究多个，等效的结合位点对塑造生物反应的影响。多个制度，定性不同的物理特性，由于不同的流行率的再结合效应的预测。计算表明，当配体再结合的剂量响应显着贡献，一个纯粹的等价模型可以影响结合曲线非线性。该模型还预测，配体再结合本身似乎不足以产生高度合作的生物反应。
英文摘要：
The utilization of multiple phosphorylation sites in regulating a biological response is ubiquitous in cell signaling. If each site contributes an additional, equivalent binding site, then one consequence of an increase in the number of phosphorylations may be to increase the probability that, upon disassociation, a ligand immediately rebinds to its receptor. How such effects may influence cell signaling systems has been less studied. Here, a self-consistent integral equation formalism for ligand rebinding, in conjunction with Monte Carlo simulations, is employed to further investigate the effects of multiple, equivalent binding sites on shaping biological responses. Multiple regimes that characterize qualitatively different physics due to the differential prevalence of rebinding effects are predicted. Calculations suggest that when ligand rebinding contributes significantly to the dose response, a purely allovalent model can influence the binding curves nonlinearly. The model also predicts that ligand rebinding in itself appears insufficient to generative a highly cooperative biological response.
机构、总结、中文摘要均由AI分析而来，可能存在错误，请以论文正文为准。
