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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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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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
Confinement Effects on the Kinetics and Thermodynamics of Protein Dimerization
, 2009 In the cell, protein complexes form relying on specific interactions between their monomers. Excluded volume effects due to molecular crowding would lead to correlations between molecules even without specific interactions. What is the interplay of these
Breg +25 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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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
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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Characteristics of the tomato chromoplast revealed by proteomic analysis [PDF]
, 2010 Chromoplasts are non-photosynthetic specialized plastids that are important in ripening tomato fruit (Solanum lycopersicum) since, among other functions, they are the site of accumulation of coloured compounds.
Barsan, Cristina +9 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
Mammalian 60-kDa Stress Protein (Chaperonin Homolog). [PDF]
Journal of Biological Chemistry, 1995 Hideaki Itoh +11 more
openaire +1 more source