Results 11 to 20 of about 28,092 (189)

CCT4 promotes tunneling nanotube formation. [PDF]

FEBS Lett
Tunneling nanotubes (TNTs) are membranous tunnel‐like structures that transport molecules and organelles between cells. They vary in thickness, and thick nanotubes often contain microtubules in addition to actin fibers. We found that cells expressing monomeric CCT4 generate many thick TNTs with tubulin.
Enomoto M, Asada A, Saito T, Ando K.
europepmc   +2 more sources

Heat shock protein 10 as a chaperone modulating α-synuclein amyloid fibril formation. [PDF]

Protein Sci
Abstract HSP10 is a well‐known human co‐chaperone that interacts with HSP60 to comprise the HSP60/10 chaperonin complex which upholds mitochondrial proteostasis. HSP10 also demonstrates independent roles in binding to misfolded proteins and interacts with several amyloidogenic client proteins.
Larsson JNK, Kumar R, Buratti FA, Nyström S, Wittung-Stafshede P, Hammarström P.   +5 more
europepmc   +2 more sources

DCAF12 Ubiquitin Ligase Promotes Lung Cancer Metastasis by Modulating the TRiC/CCT Chaperonin Complex. [PDF]

Adv Sci (Weinh)
This study elucidates how DCAF12 facilitates non‐degradative ubiquitination to stabilize TRiC/CCT, thereby enhancing the folding capacity of chaperonins. This mechanism promotes the maturation of cytoskeletal proteins and activates key oncogenic drivers, including YAP, STAT3, and mTOR, ultimately driving metastatic progression in lung cancer.
Wang Z, Huang H, Huang K, Cui X, Wu L, Lin R, Zhao Z, Chen H, Zheng C, Jin W, Chen S, Chen J, Xu Y, Wei D.   +13 more
europepmc   +2 more sources

Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60 [PDF]

Proceedings of the National Academy of Sciences, 1997
Chaperonins are essential for the folding of proteins in bacteria, mitochondria, and chloroplasts. We have functionally characterized the yeast mitochondrial chaperonins hsp60 and hsp10. In the presence of ADP, one molecule of hsp10 binds to hsp60 with an apparent K d of 0.9 nM and a second molecule of ...
Y, Dubaquié, R, Looser, S, Rospert
openaire   +2 more sources

Identification of a chaperonin‐10 homologue in plant mitochondria [PDF]

FEBS Letters, 1994
Chaperonin‐60 and chaperonin‐10 form stable binary complexes in the presence of ATP. This phenomenon has been used as the basis for the identification of a chaperonin‐10 homologue in potato (Solanum tuberosum L.) mitochondria. ATP‐dependent binary complexes formed between chaperonin‐60 and chaperonin‐10 in potato mitochondrial extracts were isolated by
Burt, W.J.E., Leaver, C.J.
openaire   +2 more sources

Disease-associated mutations in the HSPD1 gene encoding the large subunit of the mitochondrial HSP60/HSP10 chaperonin complex

Frontiers in Molecular Biosciences, 2016
Heat shock protein 60 (HSP60) forms together with heat shock protein 10 (HSP10) double-barrel chaperonin complexes that are essential for folding to the native state of proteins in the mitochondrial matrix space.
Peter Bross, Paula Fernandez-Guerra
doaj   +1 more source

DNA vaccines against dengue virus type 2 based on truncate envelope protein or its domain III. [PDF]

PLoS ONE, 2011
Two DNA vaccines were constructed encoding the ectodomain (domains I, II and III) of the DENV2 envelope protein (pE1D2) or only its domain III (pE2D2), fused to the human tissue plasminogen activator signal peptide (t-PA). The expression and secretion of
Adriana S Azevedo, Anna M Y Yamamura, Marcos S Freire, Gisela F Trindade, Myrna Bonaldo, Ricardo Galler, Ada M B Alves   +6 more
doaj   +1 more source

Myelin pathology: Involvement of molecular chaperones and the promise of chaperonotherapy [PDF]

, 2019
The process of axon myelination involves various proteins including molecular chaperones. Myelin alteration is a common feature in neurological diseases due to structural and functional abnormalities of one or more myelin proteins.
Cappello F., Conway De Macario E., Macario A. J. L., Marino Gammazza A., Scalia F.   +4 more
core   +1 more source

Toward Developing Chemical Modulators of Hsp60 as Potential Therapeutics

Frontiers in Molecular Biosciences, 2018
The 60 kDa heat shock protein (Hsp60) is classically known as a mitochondrial chaperonin protein working together with co-chaperonin 10 kDa heat shock protein (Hsp10).
Qianli Meng, Bingbing X. Li, Xiangshu Xiao   +2 more
doaj   +1 more source

Formation of the chaperonin complex studied by 2D NMR spectroscopy. [PDF]

PLoS ONE, 2017
We studied the interaction between GroES and a single-ring mutant (SR1) of GroEL by the NMR titration of 15N-labeled GroES with SR1 at three different temperatures (20, 25 and 30°C) in the presence of 3 mM ADP in 100 mM KCl and 10 mM MgCl2 at pH 7.5.
Toshio Takenaka, Takashi Nakamura, Saeko Yanaka, Maho Yagi-Utsumi, Mahesh S Chandak, Kazunobu Takahashi, Subhankar Paul, Koki Makabe, Munehito Arai, Koichi Kato, Kunihiro Kuwajima   +10 more
doaj   +1 more source