Pages that link to "Q33947193"
Jump to navigation
Jump to search
The following pages link to Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding (Q33947193):
Displaying 25 items.
- Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling (Q24674537) (← links)
- Chaperonins (Q28276039) (← links)
- Observing structure, function and assembly of single proteins by AFM. (Q30847493) (← links)
- Molecular chaperones--cellular machines for protein folding (Q34165962) (← links)
- GroEL-mediated protein folding: making the impossible, possible (Q36539816) (← links)
- beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange (Q37229567) (← links)
- Chaperones GroEL/GroES accelerate the refolding of a multidomain protein through modulating on-pathway intermediates (Q37428643) (← links)
- Reconciling theories of chaperonin accelerated folding with experimental evidence (Q37620229) (← links)
- Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage (Q37642068) (← links)
- Evolution of Escherichia coli for growth at high temperatures (Q41046825) (← links)
- GroEL-mediated protein folding (Q41429098) (← links)
- Structural and mechanistic consequences of polypeptide binding by GroEL. (Q41679938) (← links)
- Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release (Q43695967) (← links)
- Quorum signaling via AI-2 communicates the "Metabolic Burden" associated with heterologous protein production in Escherichia coli (Q43773407) (← links)
- GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivation (Q43790536) (← links)
- Partitioning of rhodanese onto GroEL. Chaperonin binds a reversibly oxidized form derived from the native protein (Q51094020) (← links)
- How GroES regulates binding of nonnative protein to GroEL. (Q54565510) (← links)
- Interaction with GroEL destabilises non-amphiphilic secondary structure in a peptide (Q73196301) (← links)
- GroEL/GroES promote dissociation/reassociation cycles of a heterodimeric intermediate during alpha(2)beta(2) protein assembly. Iterative annealing at the quaternary structure level (Q73378011) (← links)
- Insight into the Conformation of Protein Folding Intermediate(s) Trapped by GroEL (Q74167580) (← links)
- Chaperonins (Q74664372) (← links)
- GroEL/GroES-dependent reconstitution of alpha2 beta2 tetramers of humanmitochondrial branched chain alpha-ketoacid decarboxylase. Obligatory interaction of chaperonins with an alpha beta dimeric intermediate (Q77206410) (← links)
- Changing the nature of the initial chaperonin capture complex influences the substrate folding efficiency (Q77300049) (← links)
- Role of adenine nucleotides, molecular chaperones and chaperonins in stabilization of DnaA initiator protein of Escherichia coli (Q77393192) (← links)
- GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase (Q77630922) (← links)