<p>EcClpB (A) or EhClpB (B, C) was incubated with the native (N) or aggregated G6PDH (A, B) or luciferase, Luc (C) in the presence of the indicated nucleotides. The solutions were passed through a 0.1- µm filter and the fractions retained on the filter were analyzed by SDS-PAGE with Coomassie stain. The first lane in (A) shows EcClpB incubated with the native G6PDH and ATPγS, in (B, C) it shows EhClpB incubated with the native G6PDH or luciferase and ATP.</p
Doctor of PhilosophyGraduate Biochemistry GroupMichal ZolkiewskiClpB, a bacterial chaperone that bel...
ClpB cooperates with the DnaK chaperone system in the reactivation of protein from aggregates and is...
The chaperone ClpB in bacteria is responsible for the reactivation of aggregated proteins in collabo...
<p>(A) ClpB<sub>Li</sub> was incubated with aggregates of G6PDH (Agg) in the presence of 5 mM ATP or...
<p>(<b>A</b>) ClpB (0.25 µM monomer) was incubated for 10 min with ATP (1 mM) and varying concentrat...
<p>(<b>A</b>) Using the bioluminescence-based luciferase complementation assay (LCA) to measure prot...
ClpB belongs to the Hsp100 family and assists de-aggregation of protein aggregates by DnaK chaperone...
ClpB belongs to the Hsp100 family and assists de-aggregation of protein aggregates by DnaK chaperone...
(A) CLPB complexes purified from HEK293 cells form double-oligomeric state. Representative nsEM imag...
The molecular chaperones ClpB (Hsp104) and DnaK (Hsp70) co−operate in the ATP−dependent resolubiliza...
The bacterial AAA+ chaperone ClpB provides thermotolerance by disaggregating aggregated proteins in ...
The molecular chaperones ClpB (Hsp104) and DnaK (Hsp70) co-operate in the ATP-dependent resolubiliza...
Hsp104 and ClpB are hexameric ATPases that resolubilize aggregated proteins in collaboration with th...
Initiation of headful packaging of SPP1 DNA concatemers involves the interaction of the terminase, G...
<p>(<b>A, B</b>) Urea-denatured luciferase aggregates (50 nM) (<b>A</b>) or heat-denatured GFP aggre...
Doctor of PhilosophyGraduate Biochemistry GroupMichal ZolkiewskiClpB, a bacterial chaperone that bel...
ClpB cooperates with the DnaK chaperone system in the reactivation of protein from aggregates and is...
The chaperone ClpB in bacteria is responsible for the reactivation of aggregated proteins in collabo...
<p>(A) ClpB<sub>Li</sub> was incubated with aggregates of G6PDH (Agg) in the presence of 5 mM ATP or...
<p>(<b>A</b>) ClpB (0.25 µM monomer) was incubated for 10 min with ATP (1 mM) and varying concentrat...
<p>(<b>A</b>) Using the bioluminescence-based luciferase complementation assay (LCA) to measure prot...
ClpB belongs to the Hsp100 family and assists de-aggregation of protein aggregates by DnaK chaperone...
ClpB belongs to the Hsp100 family and assists de-aggregation of protein aggregates by DnaK chaperone...
(A) CLPB complexes purified from HEK293 cells form double-oligomeric state. Representative nsEM imag...
The molecular chaperones ClpB (Hsp104) and DnaK (Hsp70) co−operate in the ATP−dependent resolubiliza...
The bacterial AAA+ chaperone ClpB provides thermotolerance by disaggregating aggregated proteins in ...
The molecular chaperones ClpB (Hsp104) and DnaK (Hsp70) co-operate in the ATP-dependent resolubiliza...
Hsp104 and ClpB are hexameric ATPases that resolubilize aggregated proteins in collaboration with th...
Initiation of headful packaging of SPP1 DNA concatemers involves the interaction of the terminase, G...
<p>(<b>A, B</b>) Urea-denatured luciferase aggregates (50 nM) (<b>A</b>) or heat-denatured GFP aggre...
Doctor of PhilosophyGraduate Biochemistry GroupMichal ZolkiewskiClpB, a bacterial chaperone that bel...
ClpB cooperates with the DnaK chaperone system in the reactivation of protein from aggregates and is...
The chaperone ClpB in bacteria is responsible for the reactivation of aggregated proteins in collabo...