scholarly journals The Role of NLRP1, NLRP3, and AIM2 Inflammasomes in Psoriasis: Review

2021 ◽  
Vol 22 (11) ◽  
pp. 5898
Author(s):  
Magdalena Ciążyńska ◽  
Irmina Olejniczak-Staruch ◽  
Dorota Sobolewska-Sztychny ◽  
Joanna Narbutt ◽  
Małgorzata Skibińska ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Systemic Review ◽  
Molecular Weight Protein ◽  
Susceptibility Loci ◽  
Interleukin 18 ◽  
High Molecular Weight Protein ◽  
Autoimmune Condition ◽  
Weight Protein ◽  
Made In

Inflammasomes are high-molecular-weight protein complexes that may cleave the two main proinflammatory cytokines, pro-interleukin-1β and pro-interleukin-18, into active forms, and contribute to psoriasis. Despite recent advances made in the pathogenesis of psoriasis, mainly studied as an autoimmune condition, activation of immune response triggers of psoriasis is still not completely understood. Recently, focus was placed on the role of inflammasomes in the pathogenesis of psoriasis. Multiple types of inhibitors and activators of various inflammasomes, inflammasome-related genes, and genetic susceptibility loci were recognized in psoriasis. In this systemic review, we collect recent and comprehensive evidence from the inflammasomes, NLRP1, NLRP3, and AIM2, in pathogenesis of psoriasis.

scholarly journals Crystal structure of theThermoplasma acidophilumprotein Ta1207

2017 ◽  
Vol 73 (6) ◽  
pp. 328-335
Author(s):  
Ganesh Ramnath Pathare ◽  
István Nagy ◽  
Ágnes Hubert ◽  
Dennis R. Thomas ◽  
Andreas Bracher
Keyword(s):  
Crystal Structure ◽  
Molecular Weight ◽  
Calcium Ions ◽  
Protein Complexes ◽  
Molecular Weight Protein ◽  
High Molecular Weight Protein ◽  
Thermoplasma Acidophilum ◽  
Intracellular Receptor ◽  
Weight Protein ◽  
Charged Group

The crystal structure of the Ta1207 protein fromThermoplasma acidophilumis reported. Ta1207 was identified in a screen for high-molecular-weight protein complexes inT. acidophilum. In solution, Ta1207 forms homopentamers of 188 kDa. The crystal structure of recombinant Ta1207 solved by Se-MAD at 2.4 Å resolution revealed a complex with fivefold symmetry. In the crystal lattice, calcium ions induce the formation of a nanocage from two pentamers. The Ta1207 protomers comprise two domains with the same novel α/β topology. A deep pocket with a binding site for a negatively charged group suggests that Ta1207 functions as an intracellular receptor for an unknown ligand. Homologues of Ta1207 occur only in Thermoplasmatales and its function might be related to the extreme lifestyle of these archaea. The thermostable Ta1207 complex might provide a useful fivefold-symmetric scaffold for future nanotechnological applications.

scholarly journals A high molecular weight protein in axoplasm underlying excitable membrane of squid giant axon

1983 ◽  
Vol 4 (6) ◽  
pp. 615-618 ◽  
Author(s):  
SHOICHIRO TSUKITA ◽  
SACHIKO TSUKITA ◽  
TAKAAKI KOBAYASHI ◽  
GEN MATSUMOTO
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Excitable Membrane ◽  
Molecular Weight Protein ◽  
High Molecular Weight Protein ◽  
Weight Protein
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