Post-Translational Modifications and Thapsigargin-Induced Localization Effects on Human Endoplasmic Reticulum Mannosidase I

Author

Neil Blok, Western Michigan University

Date of Defense

Spring 4-30-2010

Department

Biological Sciences

First Advisor

David Huffman, Chemistry

Second Advisor

Sherine Obare, Chemistry

Third Advisor

Bruce Bejcek, Biological Sciences

Abstract

A key aspect of globular protein biogenesis is folding. While protein folding is an incompletely understood process, the facts that this is closely monitored by the cell and that this monitoring, under native conditions, helps ensure homeostatic maintenance of the proteome, proteostasis, are becoming increasingly clear. When proteostasis goes awry disease can ensue. A number of diseases are associated with protein misfolding due to various causes Two broad classes of consequences can result. Toxic gain-of-function occurs most often with the formation of aggregates of misfolded proteins which may kill cells or incite the inflammatory response. Examples include Alzheimer's disease and Parkinson's disease.

Comments

Research mentors: Richard N. Sifers, Baylor University ; Shujuan Pan, Baylor University

Neil Blok is double major in Biological Sciences and Chemistry.

Recommended Citation

Blok, Neil, "Post-Translational Modifications and Thapsigargin-Induced Localization Effects on Human Endoplasmic Reticulum Mannosidase I" (2010). Honors Theses. 136.
https://scholarworks.wmich.edu/honors_theses/136

Access Setting

Honors Thesis-Campus Only