TRiC controls transcription resumption after UV damage by regulating Cockayne syndrome protein A [PDF]
, 2018 Transcription-blocking DNA lesions are removed by transcription-coupled nucleotide excision repair (TC-NER) to preserve cell viability. TC-NER is triggered by the stalling of RNA polymerase II at DNA lesions, leading to the recruitment of TC-NER-specific
Attikum, H. (Haico) van +14 more
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Chaperonopathies and Chaperonotherapy. Hsp60 as Therapeutic Target in Cancer: Potential Benefits and Risks. [PDF]
, 2013 In this minireview we focus on Hsp60 as a target for anticancer therapy. We discuss the new concepts of chaperonopathies and chaperonotherapy and present information on Hsp60 localization in the cell membrane of human tumor cells.
Angileri, Francesca +3 more
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Protein folding tames chaos [PDF]
, 2013 Protein folding produces characteristic and functional three-dimensional structures from unfolded polypeptides or disordered coils. The emergence of extraordinary complexity in the protein folding process poses astonishing challenges to theoretical ...
Wei, Guo-Wei, Xia, Kelin
core
Systematic interaction network filtering identifies CRMP1 as a novel suppressor of huntingtin misfolding and neurotoxicity [PDF]
, 2015 Assemblies of huntingtin (HTT) fragments with expanded polyglutamine (polyQ) tracts are a pathological hallmark of Huntington's disease (HD). The molecular mechanisms by which these structures are formed and cause neuronal dysfunction and toxicity are ...
Andrade-Navarro, Miguel A. +24 more
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Pathogenic mutation impairs functional dynamics of Hsp60 in mono- and oligomeric states
Nature CommunicationsMitochondrial chaperonin Heat Shock Protein 60 kDa (Hsp60) oversees the correct folding of client proteins in cooperation with Hsp10. Hsp60 monomers M first form 7-meric Single rings (S), which then pair into 14-meric Double rings (D) that accommodate ...
Luca Torielli +5 more
doaj +1 more source
Beyond Folding: The Dual Life of Hsp60 in Tissue Homeostasis and Pathophysiology
Applied BiosciencesThe heat shock protein 60 (Hsp60) is a highly conserved molecular chaperonin belonging to the chaperone system, a complex network that maintains proteostasis and regulates numerous cellular processes beyond protein folding.
Giuseppa D’Amico +4 more
doaj +1 more source
Ordered Nanostructures Made Using Chaperonin Polypeptides [PDF]
A recently invented method of fabricating periodic or otherwise ordered nanostructures involves the use of chaperonin polypeptides. The method is intended to serve as a potentially superior and less expensive alternative to conventional lithographic ...
Kagawa, Hiromi +4 more
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RNA interference approaches for treatment of HIV-1 infection. [PDF]
, 2015 HIV/AIDS is a chronic and debilitating disease that cannot be cured with current antiretroviral drugs. While combinatorial antiretroviral therapy (cART) can potently suppress HIV-1 replication and delay the onset of AIDS, viral mutagenesis often leads to
Bobbin, Maggie L +2 more
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Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring.
Journal of Biological Chemistry, 1992 Chaperonins are thought to participate in the process of protein folding in bacteria and in eukaryotic mitochondria and chloroplasts. While some chaperonins are relatively well characterized, the structures of the mammalian chaperonins are unknown.
P V, Viitanen +6 more
openaire +2 more sources
Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA [PDF]
, 1994 Mitochondrial heat shock protein 70 (mt-Hsp70) has been shown to play an important role in facilitating import into, as well as folding and assembly of nuclear-encoded proteins in the mitochondrial matrix.
Craig, Elisabeth A. +3 more
core +4 more sources