Results 51 to 60 of about 3,554,815 (299)
Frontiers in Plant Science, 2022 The effects of the climate change including an increase in the average global temperatures, and abnormal weather events such as frequent and severe heatwaves are emerging as a worldwide ecological concern due to their impacts on plant vegetation and crop
Yeeun Kang +4 more
doaj +1 more source
Heat shock proteins and the cellular response to osmotic stress [PDF]
, 2000 In antidiuresis, the intrarenal distribution of HSP25/27, alpha beta -crystallin, HSP72, OSP94 and HSP110 corresponds to the osmotic gradient between cortex and papilla: low amounts in the cortex and high values in the inner medulla and papilla.
Lugmayr, Karin +3 more
core +1 more source
FEBS Letters, EarlyView.The process of internalization of the Shiga toxin A subunit via formation of a complex with the Shiga toxin B subunit, which specifically binds to the Gb3 receptor. The peptide is designed to act as a carrier of drugs into cancer cells. Here, we explored the potential of peptides derived from the catalytic A subunit of Shiga toxin (STxA) to be drug ...
Giulia Opassi +6 more
wiley +1 more source
The Development of ELISA and SPR-Based Immunoassays for the Detection of Heat Shock Proteins. [PDF]
, 2009 Heat shock proteins (Hsps) are highly conserved molecules in all eukaryotes and prokaryotes. They are named on the basis of their molecular weight and their synthesis is up-regulated by stress conditions such as inflammation, oxidative stress and ...
Gong, Bei
core
Conserved binding mode but diverse interfaces of MreC‐PBP2 interactions
FEBS Letters, EarlyView.The crystal structure of abMreC reveals a conserved two β‐barrel architecture and provides structural insights into its role within the bacterial elongasome. The abMreC–abPBP2 complex model identifies the molecular basis of MreC‐mediated PBP2 recognition, contributing to the regulation of peptidoglycan synthesis.
Hyunseok Jang +4 more
wiley +1 more source
Journal of Hematology & OncologyHeat shock proteins are essential molecular chaperones that play crucial roles in stabilizing protein structures, facilitating the repair or degradation of damaged proteins, and maintaining proteostasis and cellular functions.
Wei-Fang Zuo +7 more
doaj +1 more source
Frontiers in Molecular Biosciences, 2022 Small heat shock proteins (sHsp) are a ubiquitous group of ATP-independent chaperones found in all three domains of life. Although sHsps in bacteria and eukaryotes have been studied extensively, little information was available on their archaeal homologs
Mousam Roy +2 more
doaj +1 more source
Proteomic analysis of the heat shock and acclimation responses of Cyanobacteria [PDF]
, 2005 The cyanobacterium Synechocystis sp. PCC 6803 is a model experimental organism for proteomic research because its entire genomic sequence is available and cyanobacteria have high adaptive potential towards a variety of environmental stresses.
Hall, John James
core
Hsp70 in mitochondrial biogenesis [PDF]
, 1994 The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and diverse role in cellular physiology, Hsp70 proteins appear to elicit their effects by interacting with polypeptides that present domains which exhibit non ...
Stuart, Rosemary A. +2 more
core +1 more source
Heat shock proteins in bacilli [PDF]
Journal of Bacteriology, 1985 Five strains of bacilli, including a nonsporulating strain, when heat shocked, accelerated the synthesis of a specific subset of proteins. The major heat shock protein in all bacilli had a molecular weight of 66,000. The response persisted for at least 40 min and could be eliminated upon a shift down to 37 degrees C.
U N, Streips, F W, Polio
openaire +2 more sources