Research graph
References from D90N and D90K mutations in the chaperonin OBP reduce its ability to induce fibrillation of the prion protein by decreasing ATPase activity. Local targets link to admitted publications; unresolved targets remain external evidence.
Molecular chaperonin HSP60: current understanding and future prospects
10.3390/ijms25105483 · 2024 · External reference
Chaperonin mechanisms: multiple and (mis)understood?
10.1146/annurev-biophys-082521-113418 · 2022 · External reference
Chaperonin-assisted protein folding: a chronologue
10.1017/s0033583519000143 · 2020 · External reference
Molecular chaperones in the cytosol: from nascent chain to folded protein
10.1126/science.1068408 · 2002 · External reference
The molecular chaperone CCT/TRiC: an essential component of proteostasis and a potential modulator of protein aggregation
10.3389/fgene.2020.00172 · 2020 · External reference
Chaperonin-mediated protein folding
10.1146/annurev.biophys.30.1.245 · 2001 · External reference
Genome comparison of Pseudomonas aeruginosa large Phages
10.1016/j.jmb.2005.08.075 · 2005 · External reference
Complete genome sequence of the Giant virus OBP and comparative genome analysis of the diverse ϕKZ-related Phages
10.1128/jvi.06330-11 · 2012 · External reference
The genome of AR9, a giant transducing Bacillus phage encoding two multisubunit RNA polymerases
10.1016/j.virol.2016.04.030 · 2016 · External reference
Comparative genomics of three novel jumbo bacteriophages infecting Staphylococcus aureus
10.1128/jvi.02391-20 · 2021 · External reference
Structural and functional diversity of novel and known bacteriophage-encoded chaperonins
10.1016/j.ijbiomac.2020.04.189 · 2020 · External reference
Structural and functional features of viral chaperonins
10.1134/s0006297922010011 · 2022 · External reference
Cryo-EM reveals an asymmetry in a novel single-ring viral chaperonin
10.1016/j.jsb.2019.107439 · 2020 · External reference
Residues in chaperonin GroEL required for polypeptide binding and release
10.1038/371614a0 · 1994 · External reference
A mutant at position 87 of the GroEL chaperonin is affected in protein binding and ATP hydrolysis
10.1074/jbc.270.23.13956 · 1995 · External reference
New GroEL-like chaperonin of bacteriophage OBP Pseudomonas fluorescens suppresses thermal protein aggregation in an ATP-dependent manner
10.1042/bcj20160367 · 2016 · External reference
Bacteriophage-encoded chaperonins stimulate prion protein fibrillation in an ATP-dependent manner
10.1016/j.bbapap.2023.140965 · 2024 · External reference
Interaction of phage chaperonin OBP domains with amyloidogenic proteins
10.1016/j.abb.2025.110493 · 2025 · External reference
Expression and functional characterization of the first bacteriophage-encoded chaperonin
10.1128/jvi.00940-12 · 2012 · External reference
Molecular chaperones: a double-edged sword in neurodegenerative diseases
10.3389/fnagi.2020.581374 · 2020 · External reference
Factors affecting pathological amyloid protein transformation: from post-translational modifications to chaperones
10.1134/s0006297924604003 · 2025 · External reference
Cleavage of structural proteins during the assembly of the head of bacteriophage T4
10.1038/227680a0 · 1970 · External reference
High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility
2000 · External reference
A malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay
10.1016/0003-2697(88)90484-8 · 1988 · External reference
A three-stage kinetic model of amyloid fibrillation
10.1529/biophysj.106.098608 · 2007 · External reference
Cryo-EM structure and molecular dynamic simulations explain the enhanced stability and ATP activity of the pathological chaperonin mutant
10.1016/j.str.2024.02.001 · 2024 · External reference
Structural and computational study of the GroEL–prion protein complex
10.3390/biomedicines9111649 · 2021 · External reference
Annealing prion protein amyloid fibrils at high temperature results in extension of a proteinase K-resistant core
10.1074/jbc.m510840200 · 2006 · External reference
GroE facilitates refolding of citrate synthase by suppressing aggregation
10.1021/bi00220a020 · 1991 · External reference
Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of alpha-glucosidase from yeast
10.1021/bi00114a001 · 1991 · External reference
Inhibition of chaperonin GroEL by a monomer of ovine prion protein and its oligomeric forms
10.1134/s0006297916100199 · 2016 · External reference
Molecular mechanisms of chaperonin GroEL−GroES function
10.1021/bi011393x · 2002 · External reference
Amyloid disassembly: what can we learn from chaperones?
10.3390/biomedicines10123276 · 2022 · External reference
Amyloid inhibition by molecular chaperones in vitro can be translated to Alzheimer’s pathology in vivo
10.1039/d3md00040k · 2023 · External reference
