Elevated chaperone proteins are a feature of winter freeze avoidance by larvae of the goldenrod gall moth, Epiblema scudderiana

2018 ◽  
Vol 106 ◽  
pp. 106-113 ◽  
Author(s):  
Guijun Zhang ◽  
Janet M. Storey ◽  
Kenneth B. Storey
Keyword(s):  
Chaperone Proteins ◽  
Freeze Avoidance ◽  
Epiblema Scudderiana

Epigenetic underpinnings of freeze avoidance in the goldenrod gall moth, Epiblema scudderiana

2021 ◽  
Vol 134 ◽  
pp. 104298
Author(s):  
Sam M. Williamson ◽  
W. Aline Ingelson-Filpula ◽  
Hanane Hadj-Moussa ◽  
Kenneth B. Storey
Keyword(s):  
Freeze Avoidance ◽  
Epiblema Scudderiana

scholarly journals Human Hsp70 and Hsp40 Chaperone Proteins Facilitate Human Papillomavirus-11 E1 Protein Binding to the Origin and Stimulate Cell-free DNA Replication

1998 ◽  
Vol 273 (46) ◽  
pp. 30704-30712 ◽  
Author(s):  
Jen-Sing Liu ◽  
Shu-Ru Kuo ◽  
Alexander M. Makhov ◽  
Douglas M. Cyr ◽  
Jack D. Griffith ◽  
...  
Keyword(s):  
Human Papillomavirus ◽  
Dna Replication ◽  
Protein Binding ◽  
Chaperone Proteins ◽  
Cell Free Dna ◽  
E1 Protein ◽  
Free Dna ◽  
Stimulate Cell ◽  
Human Hsp70

Principles of chaperone-mediated protein folding

1995 ◽  
Vol 348 (1323) ◽  
pp. 107-112 ◽  
Keyword(s):  
Protein Folding ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Cellular Protein ◽  
Chaperone Proteins ◽  
Shock Proteins ◽  
Polypeptide Chains

The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo . Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding.

Chaperone proteins and winter survival by a freeze tolerant insect

2011 ◽  
Vol 57 (8) ◽  
pp. 1115-1122 ◽  
Author(s):  
Guijun Zhang ◽  
Janet M. Storey ◽  
Kenneth B. Storey
Keyword(s):  
Winter Survival ◽  
Chaperone Proteins ◽  
Freeze Tolerant

Adaptive mechanisms of freeze avoidance in plants: A brief update

2014 ◽  
Vol 99 ◽  
pp. 133-140 ◽  
Author(s):  
Michael Wisniewski ◽  
Lawrence Gusta ◽  
Gilbert Neuner
Keyword(s):  
Freeze Avoidance ◽  
Adaptive Mechanisms

The freeze-avoidance response of smelt Osmerus mordax

2002 ◽  
Vol 205 (10) ◽  
pp. 1419-1427 ◽  
Author(s):  
Jason R. Treberg ◽  
Connie E. Wilson ◽  
Robert C. Richards ◽  
K. Vanya Ewart ◽  
William R. Driedzic
Keyword(s):  
Avoidance Response ◽  
Liver Enzymes ◽  
Thermal Hysteresis ◽  
Early Spring ◽  
Osmerus Mordax ◽  
Mrna Levels ◽  
Ambient Conditions ◽  
Freeze Avoidance ◽  
Urea Content ◽  
Trimethylamine Oxide

SUMMARY Smelt (Osmerus mordax) were maintained at either ambient water temperature or approximately 5°C and various aspects of their freeze-avoidance response were examined from early winter until early spring. Plasma levels of glycerol, trimethylamine oxide (TMAO) and urea were elevated by December 15 and continued to increase in fish held in ambient conditions. In contrast, fish held under warm conditions exhibited decreased glycerol and urea content in plasma, muscle and liver. Plasma and liver TMAO levels also decreased in these fish while muscle TMAO did not vary from the initial values. The activity of liver enzymes involved with the production of glycerol did not differ significantly between groups and had decreased by the end of the study. Antifreeze protein (AFP) expression increased over the duration of the experiment. In January samples, AFP activity (thermal hysteresis) did not vary significantly between groups but mRNA levels were significantly lower in the smelt held at warm temperatures.

Chaperone Proteins and Chaperonopathies

2007 ◽  
pp. 438-444
Author(s):  
A.J.L. Macario ◽  
E. Conway de Macario
Keyword(s):  
Chaperone Proteins
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