AbstractThe thermosome, the chaperonin of the archaea, and its homologue from the cytosol of eukaryotes, known as TRiC or CCT, form a distinct subfamily of the chaperonins that does not depend on a co-chaperonin for protein folding activity. Recent structural data obtained by cryo- electron microscopy and X-ray crystallography provide the first insights into a novel mechanism remarkably different from that of the bacterial GroEL-GroES system
The crystal structure of the substrate binding domain of the thermosome, the archaeal group II chape...
The thermosome, a chaperonin from the archaebacterium Thermoplasma acidophilum, consists of two subu...
hat were found to be variable in length and/or amino acid sequence were localized primarily to the e...
AbstractThe thermosome, the chaperonin of the archaea, and its homologue from the cytosol of eukaryo...
The thermosome, the chaperonin of the archaea, and its homologue from the cytosol of eukaryotes, kno...
AbstractWe have determined to 2.6 Å resolution the crystal structure of the thermosome, the archaeal...
AbstractThe crystal structure of the substrate binding domain of the thermosome, the archaeal group ...
In the past decade, the eubacterial group I chaperonin GroEL became the paradigm of a protein foldin...
AbstractChaperonins are large oligomers made up of two superimposed rings, each enclosing a cavity u...
Two classes of chaperonins are known in all groups of organisms to participate in the folding of new...
AbstractChaperonins are double-ring protein folding machines fueled by ATP binding and hydrolysis. C...
AbstractTwo classes of chaperonins are known in all groups of organisms to participate in the foldin...
Tesis Doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departament...
AbstractChaperonins are molecular machines that use ATP-driven cycles to assist misfolded substrate ...
AbstractEfficient de novo folding of actins and tubulins requires two molecular chaperones, the chap...
The crystal structure of the substrate binding domain of the thermosome, the archaeal group II chape...
The thermosome, a chaperonin from the archaebacterium Thermoplasma acidophilum, consists of two subu...
hat were found to be variable in length and/or amino acid sequence were localized primarily to the e...
AbstractThe thermosome, the chaperonin of the archaea, and its homologue from the cytosol of eukaryo...
The thermosome, the chaperonin of the archaea, and its homologue from the cytosol of eukaryotes, kno...
AbstractWe have determined to 2.6 Å resolution the crystal structure of the thermosome, the archaeal...
AbstractThe crystal structure of the substrate binding domain of the thermosome, the archaeal group ...
In the past decade, the eubacterial group I chaperonin GroEL became the paradigm of a protein foldin...
AbstractChaperonins are large oligomers made up of two superimposed rings, each enclosing a cavity u...
Two classes of chaperonins are known in all groups of organisms to participate in the folding of new...
AbstractChaperonins are double-ring protein folding machines fueled by ATP binding and hydrolysis. C...
AbstractTwo classes of chaperonins are known in all groups of organisms to participate in the foldin...
Tesis Doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departament...
AbstractChaperonins are molecular machines that use ATP-driven cycles to assist misfolded substrate ...
AbstractEfficient de novo folding of actins and tubulins requires two molecular chaperones, the chap...
The crystal structure of the substrate binding domain of the thermosome, the archaeal group II chape...
The thermosome, a chaperonin from the archaebacterium Thermoplasma acidophilum, consists of two subu...
hat were found to be variable in length and/or amino acid sequence were localized primarily to the e...