scholarly journals Gamma radiation induced changes in expression of Heat Shock Proteins (Hsc70 and Hsp83) in the dengue vector -Aedes aegypti (L.)

2022 ◽  
Vol 0 (0) ◽  
pp. 0
Author(s):  
NJ Shetty ◽  
Vinaya Shetty ◽  
SK Jha ◽  
RC Chaubey
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Aedes Aegypti ◽  
Gamma Radiation ◽  
Dengue Vector ◽  
Radiation Induced ◽  
Shock Proteins ◽  
Induced Changes

pH-induced changes of the structure of small heat shock proteins with molecular mass 24/27kDa (HspB1)

2004 ◽  
Vol 324 (4) ◽  
pp. 1199-1203 ◽  
Author(s):  
Ivan S. Chernik ◽  
Olesya O. Panasenko ◽  
Yi Li ◽  
Steven B. Marston ◽  
Nikolai B. Gusev
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Mass ◽  
Small Heat Shock Proteins ◽  
Shock Proteins ◽  
Induced Changes

scholarly journals The Role of the Arginine in the Conserved N-Terminal Domain RLFDQxFG Motif of Human Small Heat Shock Proteins HspB1, HspB4, HspB5, HspB6, and HspB8

2018 ◽  
Vol 19 (7) ◽  
pp. 2112 ◽  
Author(s):  
Vladislav Shatov ◽  
Stephen Weeks ◽  
Sergei Strelkov ◽  
Nikolai Gusev
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Evolutionary Relationship ◽  
Small Heat Shock Proteins ◽  
Core Motif ◽  
Terminal Domain ◽  
Shock Proteins ◽  
Induced Changes ◽  
Relationship Of

Although the N-terminal domain of vertebrate small heat shock proteins (sHsp) is poorly conserved, it contains a core motif preserved in many members of the sHsp family. The role of this RLFDQxFG motif remains elusive. We analyzed the specific role of the first arginine residue of this conserved octet sequence in five human sHsps (HspB1, HspB4, HspB5, HspB6, and HspB8). Substitution of this arginine with an alanine induced changes in thermal stability and/or intrinsic fluorescence of the related HspB1 and HspB8, but yielded only modest changes in the same biophysical properties of HspB4, HspB5, and HspB6 which together belong to another clade of vertebrate sHsps. Removal of the positively charged Arg side chain resulted in destabilization of the large oligomers of HspB1 and formation of smaller size oligomers of HspB5. The mutation induced only minor changes in the structure of HspB4 and HspB6. In contrast, the mutation in HspB8 was accompanied by shifting the equilibrium from dimers towards the formation of larger oligomers. We conclude that the RLFDQxFG motif plays distinct roles in the structure of several sHsp orthologs. This role correlates with the evolutionary relationship of the respective sHsps, but ultimately, it reflects the sequence context of this motif.

Expression of heat shock proteins (HSPs) in Aedes aegypti (L) and Aedes albopictus (Skuse) (Diptera: Culicidae) larvae in response to thermal stress

Acta Tropica ◽  
2017 ◽  
Vol 167 ◽  
pp. 121-127 ◽  
Author(s):  
Arun Sivan ◽  
Ananganallur Nagarajan Shriram ◽  
Nagarajan Muruganandam ◽  
Ramanathan Thamizhmani
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Aedes Aegypti ◽  
Aedes Albopictus ◽  
Shock Proteins

scholarly journals Heat stress-induced changes in skeletal muscle: Heat shock proteins and cell signaling transduction

2012 ◽  
Vol 1 (1) ◽  
pp. 125-131 ◽  
Author(s):  
Hisashi Naito ◽  
Toshinori Yoshihara ◽  
Ryo Kakigi ◽  
Noriko Ichinoseki-Sekine ◽  
Takamasa Tsuzuki
Keyword(s):  
Skeletal Muscle ◽  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Signaling ◽  
Signaling Transduction ◽  
Shock Proteins ◽  
Induced Changes
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