Pages that link to "Q24791943"
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The following pages link to Unscrambling an egg: protein disaggregation by AAA+ proteins (Q24791943):
Displaying 37 items.
- The small heat-shock proteins IbpA and IbpB reduce the stress load of recombinant Escherichia coli and delay degradation of inclusion bodies (Q24798023) (← links)
- Keeping up with protein folding (Q24803553) (← links)
- Genome-wide analysis of rice ClpB/HSP100, ClpC and ClpD genes (Q33530234) (← links)
- The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia (Q33556224) (← links)
- Linking amyloid protein aggregation and yeast survival (Q33794914) (← links)
- TorsinA in the nuclear envelope (Q34336308) (← links)
- Localization of chaperones DnaK and GroEL in bacterial inclusion bodies (Q34557283) (← links)
- Loss of Hsp70 in Drosophila is pleiotropic, with effects on thermotolerance, recovery from heat shock and neurodegeneration (Q34587222) (← links)
- Co-production of GroELS discriminates between intrinsic and thermally-induced recombinant protein aggregation during substrate quality control (Q35520931) (← links)
- Recombinant protein folding and misfolding in Escherichia coli (Q35940945) (← links)
- Invertebrate models of dystonia (Q36634138) (← links)
- Dual role of the metalloprotease FtsH in biogenesis of the DrrAB drug transporter (Q36796824) (← links)
- Studies on bacterial inclusion bodies (Q37225671) (← links)
- Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase (Q37406494) (← links)
- Cryo electron microscopy structures of Hsp100 proteins: crowbars in or out? (Q37687108) (← links)
- Protein folding and aggregation in bacteria (Q37722588) (← links)
- Biological role of bacterial inclusion bodies: a model for amyloid aggregation (Q37875227) (← links)
- Life cycle of cytosolic prions (Q38136055) (← links)
- The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells. (Q38253736) (← links)
- Yeast prions help identify and define chaperone interaction networks. (Q38265363) (← links)
- Structural and functional features of self-assembling protein nanoparticles produced in endotoxin-free Escherichia coli. (Q38779740) (← links)
- Intrinsic tensile properties of cocoon silk fibres can be estimated by removing flaws through repeated tensile tests (Q39010102) (← links)
- Protein trafficking, ergosterol biosynthesis and membrane physics impact recombinant protein secretion in Pichia pastoris (Q39206701) (← links)
- Rehosting of bacterial chaperones for high-quality protein production. (Q41857772) (← links)
- The [PSI+] prion of Saccharomyces cerevisiae can be propagated by an Hsp104 orthologue from Candida albicans (Q42176668) (← links)
- Coordinated synthesis of the two ClpB isoforms improves the ability of Escherichia coli to survive thermal stress (Q42481588) (← links)
- Reversion of protein aggregation mediated by Sso7d in cell extracts of Sulfolobus solfataricus (Q42806264) (← links)
- The scientific impact of microbial cell factories. (Q43194023) (← links)
- A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. (Q43233938) (← links)
- Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. (Q44885001) (← links)
- VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase (Q46763702) (← links)
- Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. (Q50770803) (← links)
- The N-terminal domain of Escherichia coli ClpB enhances chaperone function. (Q51386123) (← links)
- Inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular chaperone causes growth retardation, leaf chlorosis, lower photosynthetic activity, and a specific reduction in photosystem content. (Q52085460) (← links)
- Conformational stability of the full-atom hexameric model of the ClpB chaperone from Escherichia coli. (Q54399538) (← links)
- Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system (Q81295871) (← links)
- Molecular Aspects and Clinical Relevance of GDF9 and BMP15 in Ovarian Function (Q88070917) (← links)