An Experimental Platform for Real-Time Students Engagement Measurements from Video in STEM Classrooms.

The ability to measure students' engagement in an educational setting may facilitate timely intervention in both the learning and the teaching process in a variety of classroom settings. In this paper, a real-time automatic student engagement measure is proposed through investigating two of the main components of engagement: the behavioral engagement and the emotional engagement. A biometric sensor network (BSN) consisting of web cameras, a wall-mounted camera and a high-performance computing machine was designed to capture students' head poses, eye gaze, body movements, and facial emotions.

The N-terminus of Sec61p plays key roles in ER protein import and ERAD.

Sec61p is the channel-forming subunit of the heterotrimeric Sec61 complex that mediates co-translational protein import into the endoplasmic reticulum (ER). In yeast, proteins can also be post-translationally translocated by the hetero-heptameric Sec complex, composed of the Sec61 and the Sec63 complexes. The Sec61 channel is also a candidate for the dislocation channel for misfolded proteins from the ER to the cytosol during ER-associated degradation (ERAD).

ERAD and protein import defects in a sec61 mutant lacking ER-lumenal loop 7.

Background: The Sec61 channel mediates protein translocation across the endoplasmic reticulum (ER) membrane during secretory protein biogenesis, and likely also during export of misfolded proteins for ER-associated degradation (ERAD). The mechanisms of channel opening for the different modes of translocation are not understood so far, but the position of the large ER-lumenal loop 7 of Sec61p suggests a decisive role.

Results: We show here that the Y345H mutation in L7 which causes diabetes in the mouse displays no ER import defects in yeast, but a delay in misfolded protein export.

N-acetylation and phosphorylation of Sec complex subunits in the ER membrane.

Background: Covalent modifications of proteins provide a mechanism to control protein function. Here, we have investigated modifications of the heptameric Sec complex which is responsible for post-translational protein import into the endoplasmic reticulum (ER). It consists of the Sec61 complex (Sec61p, Sbh1p, Sss1p) which on its own mediates cotranslational protein import into the ER and the Sec63 complex (Sec63p, Sec62p, Sec71p, Sec72p).