Results 61 to 70 of about 55,389 (309)

Heat shock-induced chaperoning by Hsp70 is enabled in-cell.

PLoS ONE, 2019
Recent work has shown that weak protein-protein interactions are susceptible to the cellular milieu. One case in point is the binding of heat shock proteins (Hsps) to substrate proteins in cells under stress. Upregulation of the Hsp70 chaperone machinery
Drishti Guin, Hannah Gelman, Yuhan Wang, Martin Gruebele   +3 more
doaj   +1 more source

Cytoplasmic protein misfolding titrates Hsp70 to activate nuclear Hsf1

eLife, 2019
Hsf1 is an ancient transcription factor that responds to protein folding stress by inducing the heat-shock response (HSR) that restore perturbed proteostasis. Hsp70 chaperones negatively regulate the activity of Hsf1 via stress-responsive mechanisms that
Anna E Masser, Wenjing Kang, Joydeep Roy, Jayasankar Mohanakrishnan Kaimal, Jany Quintana-Cordero, Marc R Friedländer, Claes Andréasson   +6 more
doaj   +1 more source

BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins [PDF]

Journal of Molecular Biology, 2017
Small heat shock proteins (sHsps) are a family of ATP-independent molecular chaperones that are important for binding and stabilizing unfolded proteins. In this task, the sHsps have been proposed to coordinate with ATP-dependent chaperones, including heat shock protein 70 (Hsp70).
Rauch, Jennifer N, Tse, Eric, Freilich, Rebecca, Mok, Sue-Ann, Makley, Leah N, Southworth, Daniel R, Gestwicki, Jason E   +6 more
openaire   +4 more sources

Stress-Induced PARP Activation Mediates Recruitment of Drosophila Mi-2 to Promote Heat Shock Gene Expression [PDF]

, 2011
Eukaryotic cells respond to genomic and environmental stresses, such as DNA damage and heat shock (HS), with the synthesis of poly-ADP-ribose] (PAR) at specific chromatin regions, such as DNA breaks or HS genes, by PAR polymerases (PARP). Little is known
Renate Renkawitz-Pohl, Hassler Markus, Murawska, Magdalena, Ladurner Andreas, Brehm Alexander, Andreas Ladurner, Renkawitz-Pohl, Renate, Brehm, Alexander, Ladurner, Andreas, Magdalena Murawska, Murawska Magdalena, Markus Hassler, Hassler, Markus, Alexander Brehm, Renkawitz-Pohl Renate   +14 more
core   +1 more source

SIRT6‐Mediated Deacetylation of ATF3 Promotes Silica‐Induced Lung Fibrosis by Enhancing its Nuclear Import via Binding to Importin α

Advanced Science, EarlyView.
SIRT6‐mediated ATF3 acetylation drives MGARP transcription and mitochondrial dysfunction in macrophages, promoting macrophage senescence and pulmonary fibrosis. Mechanistically, HSP70/Importin α competitively binds to ATF3, modulating its nuclear translocation.
Demin Cheng, Wenxia Bu, Fengxu Wang, Yueyuan Jin, Rongzhu Liu, Rui Zhao, Xuehai Wang, Mengna Jiang, Jinping Shen, Xinhang Cheng, Zuming Chen, Li Zhu, Jinlong Li, Zhenzhong Ge, Shichen Miao, Haotian Xu, Xiaoyu Zhou, Dongming Wang, Xinyuan Zhao   +18 more
wiley   +1 more source

Heat shock protein 70 protects the lungs from hyperoxic injury in a neonatal rat model of bronchopulmonary dysplasia.

PLoS ONE, 2023
Hyperoxia plays a significant role in the pathogenesis of lung injury, such as bronchopulmonary dysplasia (BPD), in premature infants or newborns. BPD management aims to minimize further injury, provide an optimal environment to support growth and ...
Cheng-Han Lee, Tzu-Cheng Su, Ming-Sheng Lee, Chien-Sheng Hsu, Rei-Cheng Yang, Jun-Kai Kao   +5 more
doaj   +1 more source

Bacterial Infection Elicits Heat Shock Protein 72 Release from Pleural Mesothelial Cells [PDF]

, 2013
Heat shock protein 70 (HSP70) has been implicated in infection-related processes and has been found in body fluids during infection. This study aimed to determine whether pleural mesothelial cells release HSP70 in response to bacterial infection in vitro
Porcel, JM, Bielsa, S, Brown, JS, della Vergiliana, JFV, Temple, SEL, Waterer, GW, Lee, YCG, Lansley, SM, Creaney, J   +8 more
core  

Heat Shock Protein 90: From Molecular Chaperone Function to Therapeutic Targeting in Malignancies

Advanced Science, EarlyView.
In this review, an integrated conceptual framework linking HSP90's molecular chaperone functions to its pathological roles in cancer is proposed. HSP90 serves as a central node that integrates oncogenic signaling, buffers proteotoxic stress, maintains cancer stem cell plasticity, and shapes tumor‐immune interactions, all of which converge to drive ...
Beibei Zhang, Xinxin Zou, Jiansong Zhou, Qinmiao Sun, Dahua Chen   +4 more
wiley   +1 more source

Human heat shock protein 70 (Hsp70) as a peripheral membrane protein

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2014
While a significant fraction of heat shock protein 70 (Hsp70) is membrane associated in lysosomes, mitochondria, and the outer surface of cancer cells, the mechanisms of interaction have remained elusive, with no conclusive demonstration of a protein receptor. Hsp70 contains two Trps, W90 and W580, in its N-terminal nucleotide binding domain (NBD), and
Mahalka, Ajay K., Kirkegaard, Thomas, Jukola, Laura T.I., Jaattela, Marja, Kinnunen, Paavo, K.J.   +5 more
openaire   +4 more sources

Lesion Site‐Targeted Microspheres Modulate Nav1.7‐Related Signaling for Osteoarthritis Treatment

Advanced Science, EarlyView.
Cartilage‐targeted carbamazepine‐loaded WYRGRL‐modified composite microspheres (CBZ/WCOM) anchor to exposed type II collagen in osteoarthritic lesions and release carbamazepine under acidic conditions. This bind‐then‐release platform modulates Nav1.7‐related sodium signaling, Na⁺/Ca²⁺ exchanger‐associated Ca2+ dynamics, and heat shock protein 70 ...
Cheng Chen, Jiaying Li, Jinjin Ma, Xiaonan Yuan, Yao Xiao, Yang Zhang, Yuan Chen, Hao Jiang, Hui He, Jie Hu, Qianglong Chen, Jinniu Zhang, Bin Li, Yun Zhou, Fengxuan Han, Yong Wang   +15 more
wiley   +1 more source