2015年9月15日 · We demonstrate the role of molecular switching of TrkA/p75 NTR signaling cascade in organophosphate pesticide-Monocrotophos (MCP) induced neurotoxicity in stem cell derived cholinergic neurons...

2022年3月1日 · The p75 ICD –TrkA (or c29–TrkA) active complex binds NGF through high-affinity ECD sites. Allosteric modulation to the Trk ECD may (i) improve ligand access to D5, (ii) position D1 and D4 appropriately to promote ligand-D5 interaction, and/or (iii) …

2006年9月20日 · Nerve growth factor engages two structurally distinct transmembrane receptors, TrkA and p75, which have been proposed to create a "high-affinity" NGF binding site through formation of a ternary TrkA/NGF/p75 complex.

We found that TrkA kinase activity abrogates p75-CTF oligomerization, promotes p75CTF internalization and inhibits cell death upon γ-secretase inhibition. Collectively, these observations assign a key role to TrkA in the regulation of p75 NTR deadly function. In agreement, our studies in cholinergic neurons show that the inhibition of TrkA ...

2007年1月4日 · Nerve growth factor engages two structurally distinct transmembrane receptors, TrkA and p75, which have been proposed to create a “high-affinity” NGF binding site through formation of a ternary TrkA/NGF/p75 complex.

神经营养蛋白受体 p75 和酪氨酸蛋白激酶受体 A (TrkA) 在神经系统的发育和生存中发挥重要作用。 生化数据表明 p75 和 TrkA 相互调节彼此的活性。 例如，p75能够调节TrkA对较低浓度的神经生长因子（NGF）的反应，并且TrkA以配体依赖性方式通过α-分泌酶促进p75胞外 ...

2008年7月2日 · NTs bind to two distinct classes of glycosylated receptor: the p75 neurotrophin receptor (p75 NTR) and tyrosine kinase receptors (Trks). Whereas p75 NTR binds to all NTs, the Trk subtypes are...

2005年8月5日 · The cellular response to nerve growth factor (NGF) is mediated by two structurally unrelated receptors, TrkA and p75 neurotrophin receptor (p75NTR), which have been shown to interact resulting in reciprocal modulation of function.

Biochemical data suggest that p75 and TrkA reciprocally regulate the activities of each other. For instance, p75 is able to regulate the response of TrkA to lower concentrations of nerve growth factor (NGF), and TrkA promotes shedding of the extracellular domain of p75 by α-secretases in a ligand-dependent manner.

Thirty years ago, it was discovered that p75 neurotrophin receptor and tropomyosin receptor kinase A form a complex and mediate high-affinity ligand binding and survival signaling; however, despite decades of functional and structural research, the mechanism of modulation that yields this high-affinity complex remains unclear.