Results 31 to 40 of about 216,912 (262)
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
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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
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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
Molecular Oncology, EarlyView.BCL9 and BCL9L drive bladder cancer progression by enhancing β‐catenin signaling, promoting proliferation, migration, invasion, and organoid growth. Genetic depletion of BCL9(L) suppresses malignant phenotypes, while pharmacological disruption of the β‐catenin/BCL9(L) complex with ZW4864 inhibits canonical Wnt signaling and tumor‐associated cellular ...
Roland Kotolloshi +11 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
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Expression of Hsp72 in Lymphocytes in Patients with Febrile Convulsion
Kaohsiung Journal of Medical Sciences, 2005 The pathophysiology of febrile convulsion, the most common childhood neurologic disease, remains unclear. In this study, we investigated what role a heat shock protein plays in this disease.
Lung-Chang Lin
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Molecular Oncology, EarlyView.Interferon type 1 (IFN‐1) production and signaling is associated with the acquisition of therapy resistance, following chronic DNA damage, via Interferon‐related DNA damage resistance signature (IRDS) gene expression. An alternative, DNA damage‐independent role of sustained IFN‐1 mediated resistance was identified and characterized by the emergence of ...
Ashlyn Conant +11 more
wiley +1 more source
FEBS Open Bio, EarlyView.The MRP4 transporter exports several drugs and signaling molecules. Here, we identified key promoter elements regulating basal MRP4 expression. Using reporter assays, we defined a conserved region with essential Sp1 and contributory Ets sites, which controlled basal MRP4 expression.
Debora Singer +7 more
wiley +1 more source
FEBS Open Bio, EarlyView.In normal (nontolerant) cells, CD14 is crucial for both LPS uptake and LPS signaling. In LPS‐tolerant cells, in which LPS‐induced TNF‐α and IFN‐β production is suppressed, there is a dramatic increase in surface CD14 expression. The overexpressed CD14 in LPS‐tolerant cells is responsible for the enhanced LPS uptake without inducing pro‐inflammatory ...
Saeka Nishihara +3 more
wiley +1 more source