Results 51 to 60 of about 140,081 (117)

Celastrol regulates the oligomeric state and chaperone activity of αB-crystallin linked with protein homeostasis in the lens

Fundamental Research
Protein misfolding and aggregation are crucial pathogenic factors for cataracts, which are the leading cause of visual impairment worldwide. α-crystallin, as a small molecular chaperone, is involved in preventing protein misfolding and maintaining lens ...
Huaxia Wang, Qing Tian, Ying Zhang, Yibo Xi, Lidan Hu, Ke Yao, Jingyuan Li, Xiangjun Chen   +7 more
doaj   +1 more source

The chaperone DnaK promotes the emergence and accumulation of antibiotic-resistant clones through its ATPase activity in Riemerella anatipestifer

Poultry Science
The rapid emergence of antibiotic-resistant bacteria has become a global concern. In particular, the overuse of antibiotics in the breeding industry has accelerated the emergence of antibiotic-resistant bacteria, but the mechanisms driving this ...
Fang Guo, Chunfeng Shi, Li Huang, Yizhou Yao, Liping Qiao, Dekang Zhu, Mingshu Wang, Renyong Jia, Shun Chen, Xinxin Zhao, Ying Wu, Shaqiu Zhang, Ling Zhang, Yanling Yu, Friedrich Götz, Anchun Cheng, Mafeng Liu   +16 more
doaj   +1 more source

Continuous-exchange cell-free protein synthesis using PCR-generated DNA and an RNase E-deficient extract

BioTechniques, 2008
Though the use of PCR-generated DNA (i.e., linear template) as template DNA is desirable because of its simple preparation, the linear template has not been routinely used in a conventional continuous-exchange cell-free (CECF) protein synthesis system ...
Soo Youn Jun, Sang Hyeon Kang, Kwang-Ho Lee   +2 more
doaj   +1 more source

The Hsp70 co-chaperone Ydj1/HDJ2 regulates ribonucleotide reductase activity.

PLoS Genetics, 2018
Hsp70 is a well-conserved molecular chaperone involved in the folding, stabilization, and eventual degradation of many "client" proteins. Hsp70 is regulated by a suite of co-chaperone molecules that assist in Hsp70-client interaction and stimulate the ...
Isaac T Sluder, Nitika, Laura E Knighton, Andrew W Truman   +3 more
doaj   +1 more source

New Insights into Hsp90 Structural Plasticity Revealed by cryoEM

BioChem
Heat Shock Protein 90 (Hsp90) acts as a crucial molecular chaperone, playing an essential role in activating numerous signaling proteins. The intricate mechanism of Hsp90 involving ATPase-coupled conformational changes and interactions with cochaperone ...
Karine Minari, Vitor Hugo Balasco Serrão, Júlio César Borges   +2 more
doaj   +1 more source

Hsp90: A means to an end

Cell Stress & Chaperones
The Hsp90 molecular chaperone is a key component of the protein homeostasis (proteostasis) system. Hsp90 likely serves as a gatekeeper in a cell’s protein quality control decision tree since this chaperone is linked to nascent polypeptide folding, client
Katie M. Whalen, Brian C. Freeman
doaj   +1 more source

Heat shock proteins (Hsp70 and Hsp90) in neurodegeneration: pathogenic roles and therapeutic potential

Frontiers in Aging Neuroscience
The maintenance of protein homeostasis is essential for neuronal survival and function; however, it progressively declines with age, predisposing the brain to neurodegenerative diseases.
Noureddine Ben Khalaf
doaj   +1 more source

The dynamic triage interplay of Hsp90 with its chaperone cycle and client binding

Nature Communications
Hsp90, a crucial molecular chaperone, regulates diverse client proteins, impacting both normal biology and disease. Central to its function is its conformational plasticity, driven by ATPase activity and client interactions.
Xiaozhan Qu, Simin Wang, Shuo Zhao, Chanjuan Wan, Weiya Xu, Chengdong Huang   +5 more
doaj   +1 more source

Structural basis for LMBD1-dependent trafficking and cobalamin export of ABCD4

Nature Communications
Correct trafficking of lysosomal transporters is essential for intracellular homeostasis. While most lysosomal membrane proteins are directed to the lysosome via sorting motifs, the cobalamin exporter ABCD4 is distinct, instead relying on LMBD1 as a ...
Qiwei Liu, Xingfan Li, Yingjie Wu, Kai Zheng, Mi Zhou, Tao Long   +5 more
doaj   +1 more source

Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function. [PDF]

Essays Biochem, 2023
Backe SJ, Mollapour M, Woodford MR.
europepmc   +1 more source