2P031 A worm model describing propagation of protein aggregates in neurodegenerative diseases(01B. Protein: Structure & Function,Poster)

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S164
Author(s):  
Mariko Ogawa ◽  
Hisashi Shidara ◽  
Kotaro Oka ◽  
Yoshiaki Furukawa
Keyword(s):  
Protein Structure ◽  
Neurodegenerative Diseases ◽  
Structure Function ◽  
Protein Aggregates ◽  
Worm Model

scholarly journals BECLIN1: Protein Structure, Function and Regulation

Cells ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1522
Author(s):  
Sharon Tran ◽  
W. Douglas Fairlie ◽  
Erinna F. Lee
Keyword(s):  
Protein Structure ◽  
Structure Function ◽  
Membrane Trafficking ◽  
Biochemical Properties ◽  
Class Iii ◽  
Form Class ◽  
Protein Interactome ◽  
Protein Functions ◽  
Phosphoinositide 3 Kinase ◽  
Shed Light

BECLIN1 is a well-established regulator of autophagy, a process essential for mammalian survival. It functions in conjunction with other proteins to form Class III Phosphoinositide 3-Kinase (PI3K) complexes to generate phosphorylated phosphatidylinositol (PtdIns), lipids essential for not only autophagy but other membrane trafficking processes. Over the years, studies have elucidated the structural, biophysical, and biochemical properties of BECLIN1, which have shed light on how this protein functions to allosterically regulate these critical processes of autophagy and membrane trafficking. Here, we review these findings and how BECLIN1’s diverse protein interactome regulates it, as well as its impact on organismal physiology.

New developments in protein structure-function analysis by MS and use of hydrogen-deuterium exchange microfluidics

FEBS Journal ◽  
2011 ◽  
Vol 278 (20) ◽  
pp. 3815-3821 ◽  
Author(s):  
Michael Landreh ◽  
Juan Astorga-Wells ◽  
Jan Johansson ◽  
Tomas Bergman ◽  
Hans Jörnvall
Keyword(s):  
Protein Structure ◽  
Structure Function ◽  
Function Analysis ◽  
Deuterium Exchange ◽  
Hydrogen Deuterium Exchange ◽  
New Developments ◽  
Hydrogen Deuterium
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