Results 51 to 60 of about 37,307 (249)

Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly

Nature Communications, 2019
The mechanistic target of rapamycin (mTOR) kinase forms two multi-protein signaling complexes, mTORC1 and mTORC2, which are master regulators of cell growth, metabolism, survival and autophagy. Two of the subunits of these complexes are mLST8 and Raptor,
J. Cuéllar, W. Ludlam, Nicole C Tensmeyer, Takuma Aoba, Madhura Dhavale, César Santiago, M. Bueno-Carrasco, Michael J Mann, Rebecca L. Plimpton, Aman Makaju, S. Franklin, B. Willardson, J. Valpuesta   +12 more
semanticscholar   +1 more source

The Molecular Chaperone CCT/TRiC: An Essential Component of Proteostasis and a Potential Modulator of Protein Aggregation

Frontiers in Genetics, 2020
Chaperonin containing tailless complex polypeptide 1 (CCT) or tailless complex polypeptide 1 ring complex (TRiC) is an essential eukaryotic molecular chaperone. It is a multi-subunit oligomer of two rings of eight individual protein subunits.
Julie Grantham
doaj   +1 more source

The Functional Differences between the GroEL Chaperonin of Escherichia coli and the HtpB Chaperonin of Legionella pneumophila Can Be Mapped to Specific Amino Acid Residues

Biomolecules, 2021
Group I chaperonins are a highly conserved family of essential proteins that self-assemble into molecular nanoboxes that mediate the folding of cytoplasmic proteins in bacteria and organelles.
Karla N. Valenzuela-Valderas, Gabriel Moreno-Hagelsieb, John R. Rohde, Rafael A. Garduño   +3 more
doaj   +1 more source

Reconstitution of Pure Chaperonin Hetero-Oligomer Preparations in Vitro by Temperature Modulation

Frontiers in Molecular Biosciences, 2018
Chaperonins are large, essential, oligomers that facilitate protein folding in chloroplasts, mitochondria, and eubacteria. Plant chloroplast chaperonins are comprised of multiple homologous subunits that exhibit unique properties.
Anna Vitlin Gruber, Milena Vugman, Abdussalam Azem, Celeste E. Weiss   +3 more
doaj   +1 more source

GroEL—A Versatile Chaperone for Engineering and a Plethora of Applications

Biomolecules, 2022
Chaperones play a vital role in the life of cells by facilitating the correct folding of other proteins and maintaining them in a functional state, being themselves, as a rule, more stable than the rest of cell proteins.
Maria S. Yurkova, Alexey N. Fedorov
doaj   +1 more source

Deletion of heat shock protein 60 in adult mouse cardiomyocytes perturbs mitochondrial protein homeostasis and causes heart failure. [PDF]

, 2020
To maintain healthy mitochondrial enzyme content and function, mitochondria possess a complex protein quality control system, which is composed of different endogenous sets of chaperones and proteases.
Chen, Ju, Duan, Yaoyun, Fan, Feifei, Fang, Xi, Huang, Lei, Jia, Nan, Li, Yali, Liu, Jie, Ouyang, Kunfu, Tang, Huayuan, Trexler, Christa, Wang, Gang, Wang, Hong, Yang, Feili   +13 more
core  

Molecular Chaperonin HSP60: Current Understanding and Future Prospects

International Journal of Molecular Sciences
Molecular chaperones are highly conserved across evolution and play a crucial role in preserving protein homeostasis. The 60 kDa heat shock protein (HSP60), also referred to as chaperonin 60 (Cpn60), resides within mitochondria and is involved in ...
Manish Kumar Singh, Yoonhwa Shin, Sunhee Han, J. Ha, P. K. Tiwari, Sung Soo Kim, I. Kang   +6 more
semanticscholar   +1 more source

Visualizing chaperonin function in situ by cryo-electron tomography

Nature
Chaperonins are large barrel-shaped complexes that mediate ATP-dependent protein folding1–3. The bacterial chaperonin GroEL forms juxtaposed rings that bind unfolded protein and the lid-shaped cofactor GroES at their apertures.
Jonathan Wagner, Alonso I Carvajal, A. Bracher, F. Beck, W. Wan, S. Bohn, Roman Körner, Wolfgang Baumeister, R. Fernández-Busnadiego, F. U. Hartl   +9 more
semanticscholar   +1 more source

Shotgun Proteomics Revealed Preferential Degradation of Misfolded In Vivo Obligate GroE Substrates by Lon Protease in Escherichia coli

Molecules, 2022
The Escherichia coli chaperonin GroEL/ES (GroE) is one of the most extensively studied molecular chaperones. So far, ~80 proteins in E. coli are identified as GroE substrates that obligately require GroE for folding in vivo. In GroE-depleted cells, these
Tatsuya Niwa, Yuhei Chadani, Hideki Taguchi   +2 more
doaj   +1 more source

Exposure of Bifidobacterium longum subsp. infantis to Milk Oligosaccharides Increases Adhesion to Epithelial Cells and Induces a Substantial Transcriptional Response [PDF]

, 2013
Devon Kavanaugh is in receipt of a Teagasc Walsh Fellowship. The authors would also like to acknowledge the support of Science Foundation Ireland under Grant No.
Butto, Ludovica F., Clyne, Marguerite, Hickey, Rita M., Joshi, Lokesh, Kane, Marian, Kavanaugh, Devon W., Lane, Jonathan, O'Callaghan, John, Slattery, Helen   +8 more
core   +7 more sources