Results 41 to 50 of about 3,554,762 (254)
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
Emerging experimental and computational methods for studying redox‐regulated structural transitions
FEBS Letters, EarlyView.Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass +2 more
wiley +1 more source
Frontiers in Molecular BiosciencesHeat shock proteins are molecular chaperones that play crucial roles in the folding and unfolding of complex polypeptides within the cellular system. These molecules are involved in various processes, including vesicular transport, prevention of protein ...
Xolani Henry Makhoba
doaj +1 more source
Enhanced levels of cold shock proteins in Listeria monocytogenes LO28 upon exposure to low temperature and high hydrostatic pressure [PDF]
, 2002 Listeria monocytogenes is a psychrotrophic food-borne pathogen that is problematic for the food industry because of its ubiquitous distribution in nature and its ability to grow at low temperatures and in the presence of high salt concentrations.
Karatzas, Andreas K. +7 more
core +1 more source
FEBS Letters, EarlyView.Encapsulins are protein nanocompartments that play an important role in iron storage. In the Myxococcus xanthus encapsulin system, two cargo proteins called EncB and EncC contribute to iron mineralization. Here, we show that EncB and EncC generate iron‐containing minerals with distinct chemical compositions, suggesting that the composition of stored ...
Harry B. McDowell +2 more
wiley +1 more source