Cell Fragment Formation, Migration, and Force Exertion on Extracellular Mimicking Fiber Nanonets

2021 ◽  
pp. 2000592
Author(s):  
Abinash Padhi ◽  
Brooke E. Danielsson ◽  
Deema S. Alabduljabbar ◽  
Ji Wang ◽  
Daniel E. Conway ◽  
...  
Keyword(s):  
Cell Fragment ◽  
Fragment Formation

scholarly journals Cell Fragments: Cell Fragment Formation, Migration, and Force Exertion on Extracellular Mimicking Fiber Nanonets (Adv. Biology 6/2021)

2021 ◽  
Vol 5 (6) ◽  
pp. 2170062
Author(s):  
Abinash Padhi ◽  
Brooke E. Danielsson ◽  
Deema S. Alabduljabbar ◽  
Ji Wang ◽  
Daniel E. Conway ◽  
...  
Keyword(s):  
Cell Fragment ◽  
Fragment Formation ◽  
Cell Fragments

Fragment formation in crushing a brittle medium under hydrostatic compression

1979 ◽  
Vol 15 (3) ◽  
pp. 228-232 ◽  
Author(s):  
V. M. Tsvetkov ◽  
B. G. Lukishov ◽  
L. D. Livshits
Keyword(s):  
Hydrostatic Compression ◽  
Fragment Formation

Monitoring of epithelial cell caspase activation via detection of durable keratin fragment formation

2008 ◽  
Vol 215 (2) ◽  
pp. 164-174 ◽  
Author(s):  
G-Z Tao ◽  
DH Li ◽  
Q Zhou ◽  
DM Toivola ◽  
P Strnad ◽  
...  
Keyword(s):  
Epithelial Cell ◽  
Caspase Activation ◽  
Fragment Formation

Studies on the timescale of fragment formation in heavy ion collisions

1996 ◽  
pp. 251-259
Author(s):  
Rajeev K. Puri ◽  
P. B. Gossiaux ◽  
Ch. Hartnack ◽  
J. Aichelin
Keyword(s):  
Heavy Ion Collisions ◽  
Heavy Ion ◽  
Ion Collisions ◽  
Fragment Formation

Nucleon-induced fragment formation with antisymmetrized molecular dynamics

1999 ◽  
Vol 60 (6) ◽  
Author(s):  
Yoshiharu Tosaka ◽  
Akira Ono ◽  
Hisashi Horiuchi
Keyword(s):  
Molecular Dynamics ◽  
Fragment Formation

Microfiltration of cutinase and Escherichia coli cell fragment suspensions

2002 ◽  
Vol 207 (2) ◽  
pp. 171-187 ◽  
Author(s):  
A. Cláudia Sousa ◽  
Joaquim M.S. Cabral ◽  
Marı́lia Mateus
Keyword(s):  
Escherichia Coli ◽  
Coli Cell ◽  
Cell Fragment

Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1

2005 ◽  
Vol 386 (12) ◽  
pp. 1307-1317 ◽  
Author(s):  
Birgit von Janowsky ◽  
Karin Knapp ◽  
Tamara Major ◽  
Martin Krayl ◽  
Bernard Guiard ◽  
...  
Keyword(s):  
Structural Properties ◽  
Major Effect ◽  
Terminal Segment ◽  
Mitochondrial Matrix ◽  
Amino Terminal ◽  
In Organello ◽  
Fragment Formation ◽  
Folded Proteins ◽  
Substrate Proteins ◽  
Folding State

Abstract The protease Pim1/LON, a member of the AAA+ family of homo-oligomeric ATP-dependent proteases, is responsible for the degradation of soluble proteins in the mitochondrial matrix. To establish the molecular parameters required for the specific recognition and proteolysis of substrate proteins by Pim1, we analyzed the in organello degradation of imported reporter proteins containing different structural properties. The amino acid composition at the amino-terminal end had no major effect on the proteolysis reaction. However, proteins with an amino-terminal extension of less than 60 amino acids in front of a stably folded reporter domain were completely resistant to proteolysis by Pim1. Substrate proteins with a longer amino-terminal extension showed incomplete proteolysis, resulting in the generation of a defined degradation fragment. We conclude that Pim1-mediated protein degradation is processive and is initiated from an unstructured amino-terminal segment. Resistance to degradation and fragment formation was abolished if the folding state of the reporter domain was destabilized, indicating that Pim1 is not able to unravel folded proteins for proteolysis. We propose that the requirement for an exposed, large, non-native protein segment, in combination with a limited unfolding capability, accounts for the selectivity of the protease Pim1 for damaged or misfolded polypeptides.

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