(A) Residual densities around the ANK domains, extending towards the central channel of the CLPBE425Q complex in the substrate-bound state. The extra densities are highlighted by a dotted ellipse. The density of the substrate is shown in yellow. (B) SDS-PAGE analysis of the purified proteins. (C–E) Purification of CLPB, CLPBΔ201–232, and CLPBisoform1 complexes using size-exclusion chromatography. (TIF)</p
In Escherichia coli, protein degradation is performed by several proteolytic machines, including Clp...
In Escherichia coli, protein degradation is performed by several proteolytic machines, including Clp...
ClpB from Thermus thermophilus belongs to the Clp/Hsp100 protein family and reactivates protein aggr...
(A, B) Rigid-body fitting of the crystal structure of the ANK domain into the density maps of the do...
(A) X-ray crystallography structure and AlphaFold predicted model of the ANK domain. The RMSD betwee...
(A) Domain organization of H. sapiens CLPB. CLPB is composed of an MTS, a short hydrophobic stretch ...
(A) The purification of CLPB-N92, analyzing by size-exclusion chromatography (left) and SDS-PAGE (ri...
The molecular chaperones ClpB (Hsp104) and DnaK (Hsp70) co−operate in the ATP−dependent resolubiliza...
(A) HEK-293F cells expressing the MTS-ANK-HA or MTS-ANK-Strep constructs were subjected to pulldown ...
The chaperone ClpB in bacteria is responsible for the reactivation of aggregated proteins in collabo...
ClpB is a bacterial Hsp 100 chaperone that has been shown to cooperate with the DnaKfJ (Hsp70/40) ch...
The molecular chaperones ClpB (Hsp104) and DnaK (Hsp70) co-operate in the ATP-dependent resolubiliza...
Doctor of PhilosophyGraduate Biochemistry GroupMichal ZolkiewskiClpB, a bacterial chaperone that bel...
ClpB from Thermus thermophilus belongs to the Clp/Hsp100 protein family and reactivates protein aggr...
The 580 kDa hexameric ClpB molecular chaperone is a bacterial ATP-dependent protein-remodeling machi...
In Escherichia coli, protein degradation is performed by several proteolytic machines, including Clp...
In Escherichia coli, protein degradation is performed by several proteolytic machines, including Clp...
ClpB from Thermus thermophilus belongs to the Clp/Hsp100 protein family and reactivates protein aggr...
(A, B) Rigid-body fitting of the crystal structure of the ANK domain into the density maps of the do...
(A) X-ray crystallography structure and AlphaFold predicted model of the ANK domain. The RMSD betwee...
(A) Domain organization of H. sapiens CLPB. CLPB is composed of an MTS, a short hydrophobic stretch ...
(A) The purification of CLPB-N92, analyzing by size-exclusion chromatography (left) and SDS-PAGE (ri...
The molecular chaperones ClpB (Hsp104) and DnaK (Hsp70) co−operate in the ATP−dependent resolubiliza...
(A) HEK-293F cells expressing the MTS-ANK-HA or MTS-ANK-Strep constructs were subjected to pulldown ...
The chaperone ClpB in bacteria is responsible for the reactivation of aggregated proteins in collabo...
ClpB is a bacterial Hsp 100 chaperone that has been shown to cooperate with the DnaKfJ (Hsp70/40) ch...
The molecular chaperones ClpB (Hsp104) and DnaK (Hsp70) co-operate in the ATP-dependent resolubiliza...
Doctor of PhilosophyGraduate Biochemistry GroupMichal ZolkiewskiClpB, a bacterial chaperone that bel...
ClpB from Thermus thermophilus belongs to the Clp/Hsp100 protein family and reactivates protein aggr...
The 580 kDa hexameric ClpB molecular chaperone is a bacterial ATP-dependent protein-remodeling machi...
In Escherichia coli, protein degradation is performed by several proteolytic machines, including Clp...
In Escherichia coli, protein degradation is performed by several proteolytic machines, including Clp...
ClpB from Thermus thermophilus belongs to the Clp/Hsp100 protein family and reactivates protein aggr...