A Curriculum Development and Quality Assessment Model Based on the Formation of Professional Identity

2022 ◽  
pp. 189-211
Author(s):  
Michael D. Hamlin

Educators are increasingly urged to improve quality control mechanisms. Improving quality involves more than simply increasing the variety of options for assessments. It calls for a new model of curriculum design focused on the formation of professional competencies students will need in the workplace along with the integration of theory-based learning activities and assessments supported by instructional technologies. This chapter will present a framework that educators can use to guide the integration of learning activities, assessments, and instructional technologies in a manner that guides students in the development of professional competencies for success in the workplace and also provides a stream of quality control data that can be used to measure both educational and organizational effectiveness.

2021 ◽  
pp. 153537022199981
Author(s):  
Chamithi Karunanayake ◽  
Richard C Page

The chaperone heat shock protein 70 (Hsp70) and its network of co-chaperones serve as a central hub of cellular protein quality control mechanisms. Domain organization in Hsp70 dictates ATPase activity, ATP dependent allosteric regulation, client/substrate binding and release, and interactions with co-chaperones. The protein quality control activities of Hsp70 are classified as foldase, holdase, and disaggregase activities. Co-chaperones directly assisting protein refolding included J domain proteins and nucleotide exchange factors. However, co-chaperones can also be grouped and explored based on which domain of Hsp70 they interact. Here we discuss how the network of cytosolic co-chaperones for Hsp70 contributes to the functions of Hsp70 while closely looking at their structural features. Comparison of domain organization and the structures of co-chaperones enables greater understanding of the interactions, mechanisms of action, and roles played in protein quality control.


Author(s):  
H.V. Jagadish ◽  
Julia Stoyanovich ◽  
Bill Howe

The COVID-19 pandemic is compelling us to make crucial data-driven decisions quickly, bringing together diverse and unreliable sources of information without the usual quality control mechanisms we may employ. These decisions are consequential at multiple levels: they can inform local, state and national government policy, be used to schedule access to physical resources such as elevators and workspaces within an organization, and inform contact tracing and quarantine actions for individuals. In all these cases, significant inequities are likely to arise, and to be propagated and reinforced by data-driven decision systems. In this article, we propose a framework, called FIDES, for surfacing and reasoning about data equity in these systems.


Author(s):  
H. R. Adams ◽  
M. A. Channing ◽  
J. E. Divel ◽  
B. B. Dunn ◽  
D. O. Kiesewetter ◽  
...  

1972 ◽  
Vol 18 (3) ◽  
pp. 250-257 ◽  
Author(s):  
J H Riddick ◽  
Roger Flora ◽  
Quentin L Van Meter

Abstract A system of quality-control data analysis by computer is described, in which two-way analysis of variance is used for partitioning sources of laboratory error into day-to-day, within-day, betweenpools and additivity variation. The partition for additivity is described in detail as to its advantages and applications. In addition, control charts based on two-way analysis of variance computations are prepared each month by computer. This computer program is designed to operate with the IBM 1800 or 1130 computers or any computer with a Fortran IV compiler. Examples are presented of use of the control charts and of tables of analysis of variance.


2016 ◽  
Vol 213 (6) ◽  
pp. 693-704 ◽  
Author(s):  
Natalia Sikorska ◽  
Leticia Lemus ◽  
Auxiliadora Aguilera-Romero ◽  
Javier Manzano-Lopez ◽  
Howard Riezman ◽  
...  

Endoplasmic reticulum (ER) quality control mechanisms target terminally misfolded proteins for ER-associated degradation (ERAD). Misfolded glycophosphatidylinositol-anchored proteins (GPI-APs) are, however, generally poor ERAD substrates and are targeted mainly to the vacuole/lysosome for degradation, leading to predictions that a GPI anchor sterically obstructs ERAD. Here we analyzed the degradation of the misfolded GPI-AP Gas1* in yeast. We could efficiently route Gas1* to Hrd1-dependent ERAD and provide evidence that it contains a GPI anchor, ruling out that a GPI anchor obstructs ERAD. Instead, we show that the normally decreased susceptibility of Gas1* to ERAD is caused by canonical remodeling of its GPI anchor, which occurs in all GPI-APs and provides a protein-independent ER export signal. Thus, GPI anchor remodeling is independent of protein folding and leads to efficient ER export of even misfolded species. Our data imply that ER quality control is limited for the entire class of GPI-APs, many of them being clinically relevant.


Molecules ◽  
2018 ◽  
Vol 23 (5) ◽  
pp. 1219 ◽  
Author(s):  
Sophia Wedel ◽  
Maria Manola ◽  
Maria Cavinato ◽  
Ioannis Trougakos ◽  
Pidder Jansen-Dürr

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