Analysis of the role of mitochondrial and endoplasmic reticulum localized small heat shock proteins in tomato

2010 ◽  
Vol 54 (4) ◽  
pp. 715-719 ◽  
Author(s):  
P. C. Nautiyal ◽  
M. Shono
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

Abstract 2257: Role of Survivin and small heat shock proteins in the chemoresistance of retinoblastoma

2012 ◽  
Author(s):  
Margaret Koch ◽  
Jeffery A. Bowen ◽  
Allison Galanis ◽  
Meredith Gregory ◽  
Bruce R. Ksander ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

Role of the Small Heat Shock Proteins in Regulating Vascular Smooth Muscle Tone

2005 ◽  
Vol 201 (1) ◽  
pp. 30-36 ◽  
Author(s):  
Elisabeth C. McLemore ◽  
Deron J. Tessier ◽  
Jeffrey Thresher ◽  
Padmini Komalavilas ◽  
Colleen M. Brophy
Keyword(s):  
Smooth Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Vascular Smooth Muscle ◽  
Muscle Tone ◽  
Small Heat Shock Proteins ◽  
Smooth Muscle Tone ◽  
Shock Proteins ◽  
Vascular Smooth Muscle Tone

The potential role of small heat shock proteins in mitochondria

2013 ◽  
Vol 25 (11) ◽  
pp. 2312-2319 ◽  
Author(s):  
Liuwang Zeng ◽  
Jieqiong Tan ◽  
Wei Lu ◽  
Tonglin Lu ◽  
Zhiping Hu
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Potential Role ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

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.

scholarly journals The pivotal role of the β7 strand in the intersubunit contacts of different human small heat shock proteins

2009 ◽  
Vol 15 (4) ◽  
pp. 365-377 ◽  
Author(s):  
Evgeny V. Mymrikov ◽  
Olesya V. Bukach ◽  
Alim S. Seit-Nebi ◽  
Nikolai B. Gusev
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Pivotal Role ◽  
Shock Proteins
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