Two tetratricopeptide repeat proteins facilitate human aryl hydrocarbon receptor signalling in yeast

2002 ◽  
Vol 14 (7) ◽  
pp. 615-623 ◽  
Author(s):  
Charles A. Miller
Keyword(s):  
Aryl Hydrocarbon Receptor ◽  
Tetratricopeptide Repeat ◽  
Receptor Signalling ◽  
Aryl Hydrocarbon ◽  
Repeat Proteins ◽  
Tetratricopeptide Repeat Proteins

Inhibition of eukaryotic translation by tetratricopeptide-repeat proteins of Orientia tsutsugamushi

2016 ◽  
Vol 54 (2) ◽  
pp. 136-144 ◽  
Author(s):  
Sunyoung Bang ◽  
Chan-Ki Min ◽  
Na-Young Ha ◽  
Myung-Sik Choi ◽  
Ik-Sang Kim ◽  
...  
Keyword(s):  
Tetratricopeptide Repeat ◽  
Orientia Tsutsugamushi ◽  
Eukaryotic Translation ◽  
Repeat Proteins ◽  
Tetratricopeptide Repeat Proteins

1‐Hydroxypyrene mediates renal fibrosis through aryl hydrocarbon receptor signalling pathway

2021 ◽  
Author(s):  
Hua Miao ◽  
Xia‐Qing Wu ◽  
Yan‐Ni Wang ◽  
Dan‐Qian Chen ◽  
Lin Chen ◽  
...  
Keyword(s):  
Aryl Hydrocarbon Receptor ◽  
Renal Fibrosis ◽  
Signalling Pathway ◽  
Receptor Signalling ◽  
Aryl Hydrocarbon

scholarly journals Molecular Dynamics Simulations of Consensus Tetratricopeptide Repeat Proteins

2010 ◽  
Vol 98 (3) ◽  
pp. 636a-637a
Author(s):  
Rudesh D. Toofanny ◽  
Aitziber L. Cortajarena ◽  
Lynne Regan ◽  
Valerie Daggett
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Tetratricopeptide Repeat ◽  
Repeat Proteins ◽  
Tetratricopeptide Repeat Proteins ◽  
Dynamics Simulations

scholarly journals What Curves α-Solenoids?

2002 ◽  
Vol 277 (51) ◽  
pp. 49791-49798 ◽  
Author(s):  
Andrey V. Kajava
Keyword(s):  
Structural Model ◽  
Quaternary Structure ◽  
Tetratricopeptide Repeat ◽  
Protein Substrates ◽  
Unfolded Protein ◽  
Curved Structures ◽  
Repeat Proteins ◽  
Pattern Characteristic ◽  
The Common ◽  
Tetratricopeptide Repeat Proteins

The α-helical solenoid proteins adopt a variety of elongated curved structures. They have been examined to identify the interactions that determine their curvature. A sequence pattern characteristic for strongly curved α-helical solenoids has been constructed and was found to match protein sequences containing the proteasome/cyclosome repeats. Based on this, a structural model of the repeat-containing domains of the Rpn1/S2 and Rpn2/S1 proteins, which represent the largest subunits of the 26 S proteasome, has been proposed. The model has a novel architecture resembling an α-helical toroid. Molecular modeling shows that these toroids have a central pore that would allow passage of an unfolded protein substrate through it. This implies that the Rpn1 and Rpn2 toroids are aligned along the common axial pores of the ATPase hexamer and form an “antechamber” of the 26 S proteasome. The proposed quaternary structure agrees with the available experimental data. It is suggested that the function of this antechamber is assistance to the ATPases in the unfolding of protein substrates prior to proteolysis. An evolutionary link between the PC repeat-containing proteins and tetratricopeptide repeat proteins is proposed.

scholarly journals Altered aryl-hydrocarbon-receptor signalling affects regulatory and effector cell immunity in autoimmune hepatitis

2021 ◽  
Vol 74 (1) ◽  
pp. 48-57
Author(s):  
Marta Vuerich ◽  
Rasika Harshe ◽  
Luiza Abrahão Frank ◽  
Samiran Mukherjee ◽  
Barbora Gromova ◽  
...  
Keyword(s):  
Autoimmune Hepatitis ◽  
Aryl Hydrocarbon Receptor ◽  
Effector Cell ◽  
Receptor Signalling ◽  
Aryl Hydrocarbon ◽  
Cell Immunity
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