scholarly journals Physical models have gender-specific effects on student understanding of protein structure-function relationships

2016 ◽  
Vol 44 (4) ◽  
pp. 326-335 ◽  
Author(s):  
Robin M. Forbes-Lorman ◽  
Michelle A. Harris ◽  
Wesley S. Chang ◽  
Erik W. Dent ◽  
Erik V. Nordheim ◽  
...  
2006 ◽  
Vol 34 (4) ◽  
pp. 247-254 ◽  
Author(s):  
Tim Herman ◽  
Jennifer Morris ◽  
Shannon Colton ◽  
Ann Batiza ◽  
Michael Patrick ◽  
...  

2020 ◽  
Vol 48 (4) ◽  
pp. 356-368
Author(s):  
Michelle E. Howell ◽  
Christine S. Booth ◽  
Sharmin M. Sikich ◽  
Tomáš Helikar ◽  
Karin Dijk ◽  
...  

Diabetes ◽  
2020 ◽  
Vol 69 (Supplement 1) ◽  
pp. 312-OR
Author(s):  
AHMAD AL-MRABEH ◽  
SHADEN MELHEM ◽  
SVIATLANA V. ZHYZHNEUSKAYA ◽  
CARL PETERS ◽  
ALISON C. BARNES ◽  
...  

Cells ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1522
Author(s):  
Sharon Tran ◽  
W. Douglas Fairlie ◽  
Erinna F. Lee

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.


PLoS ONE ◽  
2016 ◽  
Vol 11 (10) ◽  
pp. e0165289 ◽  
Author(s):  
Tina Strombach ◽  
Zsofia Margittai ◽  
Barbara Gorczyca ◽  
Tobias Kalenscher

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