Development of Virtual Metrology Using Plasma Information Variables to Predict Si Etch Profile Processed by SF6/O2/Ar Capacitively Coupled Plasma.

In the semiconductor etch process, as the critical dimension (CD) decreases and the difficulty of the process control increases, in-situ and real-time etch profile monitoring becomes important. It leads to the development of virtual metrology (VM) technology, one of the measurement and inspection (MI) technology that predicts the etch profile during the process. Recently, VM to predict the etch depth using plasma information (PI) variables and the etch process data based on the statistical regression method had been developed and demonstrated high performance. In this study, VM using PI variables, named PI-VM, was extended to monitor the etch profile and investigated the role of PI variables and features of PI-VM. PI variables are obtained through analysis on optical emission spectrum data. The features in PI-VM are investigated in terms of plasma physics and etch kinetics. The PI-VM is developed to monitor the etch depth, bowing CD, etch depth times bowing CD (rectangular model), and etch area model (non-rectangular model). PI-VM for etch depth and bowing CD showed high prediction accuracy of R-square value (R2) 0.8 or higher. The rectangular and non-rectangular etch area model PI-VM showed prediction accuracy R2 of 0.78 and 0.49, respectively. The first trial of virtual metrology to monitor the etch profile will contribute to the development of the etch profile control technology.

IκB kinase γ/nuclear factor-κB-essential modulator (IKKγ/NEMO) facilitates RhoA GTPase activation, which, in turn, activates Rho-associated KINASE (ROCK) to phosphorylate IKKß in response to transforming growth factor (TGF)-ß1.

Transforming growth factor (TGF)-ß1 plays several roles in a variety of cellular functions. TGF-ß1 transmits its signal through Smad transcription factor-dependent and -independent pathways. It was reported that TGF-ß1 activates NF-κB and RhoA, and RhoA activates NF-κB in several kinds of cells in a Smad-independent pathway. However, the activation molecular mechanism of NF-κB by RhoA upon TGF-ß1 has not been clearly elucidated. We observed that RhoA-GTP level was increased by TGF-ß1 in RAW264.7 cells. RhoA-GDP and RhoGDI were bound to N- and C-terminal domains of IKKγ, respectively. Purified IKKγ facilitated GTP binding to RhoA complexed with RhoGDI. Furthermore, Dbs, a guanine nucletotide exchange factor of RhoA much more enhanced GTP binding to RhoA complexed with RhoGDI in the presence of IKKγ. Indeed, si-IKKγ abolished RhoA activation in response to TGF-ß1 in cells. However, TGF-ß1 stimulated the release of RhoA-GTP from IKKγ and Rho-associated kinase (ROCK), an active RhoA effector protein, directly phosphorylated IKKß in vitro, whereas TGF-ß1-activated kinase 1 activated RhoA upon TGF-ß1 stimulation. Taken together, our data indicate that IKKγ facilitates RhoA activation via a guanine nucletotide exchange factor, which in turn activates ROCK to phosphorylate IKKß, leading to NF-κB activation that induced the chemokine expression and cell migration upon TGF-ß1.