Understanding Diversity, Evolution, and Structure of Small Heat Shock Proteins in Annelida Through in Silico Analyses

Autor: Mercedes de la Fuente, Marta Novo

Publikováno v: Frontiers in Physiology, Vol 13 (2022)

Small heat shock proteins (sHsps) are oligomeric stress proteins characterized by an α-crystallin domain (ACD). These proteins are localized in different subcellular compartments and play critical roles in the stress physiology of tissues, organs, a

Externí odkaz: https://doaj.org/article/0eec492ce155417680c62bcedabaa619

α-Crystallin Domains of Five Human Small Heat Shock Proteins (sHsps) Differ in Dimer Stabilities and Ability to Incorporate Themselves into Oligomers of Full-Length sHsps

Autor: Vladislav M. Shatov, Lydia K. Muranova, Maria A. Zamotina, Nikolai N. Sluchanko, Nikolai B. Gusev

Publikováno v: International Journal of Molecular Sciences; Volume 24; Issue 2; Pages: 1085

The α-crystallin domain (ACD) is the hallmark of a diverse family of small heat shock proteins (sHsps). We investigated some of the ACD properties of five human sHsps as well as their interactions with different full-length sHsps. According to size-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ec585c355165749a9bbf89a9d301a0f

The α-Crystallin Domain Containing Genes: Identification, Phylogeny and Expression Profiling in Abiotic Stress, Phytohormone Response and Development in Tomato (Solanum lycopersicum)

Autor: Asosii ePaul, Sombir eRao, Saloni eMathur

Publikováno v: Frontiers in Plant Science, Vol 7 (2016)

The α-crystallin domain (ACD) is an ancient domain conserved among all kingdoms. Plant ACD proteins have roles in abiotic stresses, transcriptional regulation, inhibiting virus movement and DNA demethylation. An exhaustive in-silico analysis using H

Externí odkaz: https://doaj.org/article/5201d3b2f33748469b24d6f0c1d384f3

Terminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3

Autor: Wilbert C. Boelens, Frances D.L. Kondrat, Nicholas J. Ray, Nicholas H. Keep, Ambrose R. Cole, Gillian R. Hilton, Christine Slingsby, Wilma Vree Egberts, Alice R. Clark, John A. Carver, Justin L. P. Benesch

Publikováno v: Journal of Molecular Biology, 430, 3297-3310
'Journal of Molecular Biology ', vol: 430, pages: 3297-3310 (2018)
Journal of Molecular Biology
Journal of Molecular Biology, 430, 18, pp. 3297-3310

Heterogeneity in small heat shock proteins (sHsps) spans multiple spatiotemporal regimes—from fast fluctuations of part of the protein, to conformational variability of tertiary structure, plasticity of the interfaces, and polydispersity of the int

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7eb6bb4ad1717ba7769b716c6c542818
https://doi.org/10.1016/j.jmb.2018.06.047

The MBD7 complex promotes expression of methylated transgenes without significantly altering their methylation status

Autor: Julie A. Law, Brandon H. Le, Dongming Li, Lei Gao, Ying Feng, Shengben Li, Jinyuan Liu, Beixin Mo, Li Liu, Xigang Liu, Ana Marie S. Palanca, Xiuyun Wu, Ajay A. Vashisht, So Youn Won, Guodong Yang, James A. Wohlschlegel, Yun Ju Kim, Shaofang Li, Xuemei Chen, Hongwei Guo, Yuanyuan Zhao

Publikováno v: eLife
eLife, Vol 6 (2017)

DNA methylation is associated with gene silencing in eukaryotic organisms. Although pathways controlling the establishment, maintenance and removal of DNA methylation are known, relatively little is understood about how DNA methylation influences gen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab9f8fcf9bf7b7af2e89cb127681e451
http://europepmc.org/articles/PMC5462541