Results 161 to 170 of about 20,108 (219)

High-Throughput Detection of Cyanobacterial Form I Rubisco Assembly. [PDF]

ACS Synth Biol
Wysocki JW, Lee B, Wang T.
europepmc   +1 more source

Dual-calibration RT-qPCR reveals distinct dnaK1/2/3 and groEL1/2 expression dynamics under heat and acid stress in the sinefungin producer Streptomyces incarnatus. [PDF]

Sci Rep
Xiao-Hui Z, Kubo M, Yamagata H, Nakashima Y, Hasunuma T, Kanao T, Tamura T.   +6 more
europepmc   +1 more source

An outmoded in vitro-inferred mechanism for chaperonin-accelerated protein refolding is confirmed in cells by cryo-electron tomography. [PDF]

Cell Stress Chaperones
De Los Rios P, Rebeaud ME, Goloubinoff P.   +2 more
europepmc   +1 more source

TRiC Is a Structural Component of Mammalian Sperm Axonemes. [PDF]

Cytoskeleton (Hoboken)
Brown A, Leung MR, Zeev-Ben-Mordehai T, Zhang R.   +3 more
europepmc   +1 more source

Origin of chaperone dependence and assembly complexity in Rubisco’s biogenesis

Ng JZY, Wiens D, Schulz L, Hergenröder A, Küffner AM, Geil C, Erb TJ, Hochberg GKA.   +7 more
europepmc   +1 more source

Pathway of Actin Folding Directed by the Eukaryotic Chaperonin TRiC [PDF]

Cell, 2018
The hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein actin. The simpler bacterial chaperonin system, GroEL/GroES, is unable to mediate actin folding.
David Balchin, Mike Strauss, Manajit Hayer-Hartl   +2 more
exaly   +2 more sources

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The first chaperonin

Nature Reviews Molecular Cell Biology, 2013
F Ulrich Hartl, Manajit Hayer-Hartl, Hartl F Ulrich   +2 more
exaly   +4 more sources

Purification of chaperonins

Journal of Chromatography B: Biomedical Sciences and Applications, 1999
The availability of protein samples of sufficient quality and in sufficient quantity is a driving force in biology and biotechnology. Protein samples that are free of critical contaminants are required for specific assays. Large amounts of highly homogeneous and reproducible material are needed for crystallography and nuclear magnetic resonance studies
E, Quaite-Randall, A, Joachimiak
openaire   +2 more sources

On the oligomeric state of chloroplast chaperonin 10 and chaperonin 20

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003
Type I chaperonins are fundamental protein folding machineries that function in eubacteria, mitochondria and chloroplasts. Eubacteria and mitochondria contain chaperonin systems comprised of homo-oligomeric chaperonin 60 tetradecamers and co-chaperonin 10 heptamers.
Rajach, Sharkia, Anat L, Bonshtien, Itzhak, Mizrahi, Celeste, Weiss, Adina, Niv, Ariel, Lustig, Paul V, Viitanen, Abdussalam, Azem   +7 more
openaire   +2 more sources