The interaction network of the GroEL chaperonin

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Bibliographic Details
Other Authors: Hartl, F. Ulrich. (Speaker)
Format: Electronic
Language:English
Published: London : Henry Stewart Talks, 2012.
Series:Henry Stewart talks. Biomedical & life sciences collection. Protein homeostasis.
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035 |a (HSTalks)HST3277_1_2_20141204 
040 |a UKHST  |c UKHST 
040 |a HSTalks  |b eng  |c HSTalks 
100 1 |a Hartl, F. Ulrich.  |4 spk 
245 1 4 |a The interaction network of the GroEL chaperonin  |h [electronic resource] /  |c F. Ulrich Hartl. 
260 |a London :  |b Henry Stewart Talks,  |c 2012. 
300 |a 1 streaming video file (30 min.) :  |b digital, mono., SWF file, sd., col. 
490 1 |a Protein homeostasis : folding proteins and maintaining the protein-protein interaction networks 
500 |a Animated audio-visual presentation with synchronized narration. 
500 |a Title from title frames. 
505 0 |a Contents: De novo protein folding and proteome maintenance critically depend on molecular chaperones -- Transitions during protein folding -- Chaperone assisted protein folding -- Productive protein folding is often competed by aggregation -- Reconstitution of GroEL-assisted folding -- GroEL and GroES function as a folding cage for proteins up to 60 kDa -- GroEL structure -- Which proteins need GroEL/GroES for folding? -- Identification of the GroEL interaction proteome -- Class III substrates are of relatively low cellular abundance but occupy most of the GroEL capacity -- Chaperonins provide a specialized folding environment with two functional elements: sequestration and steric confinement in a hydrophilic cage -- GroEL as part of the cytosolic chaperone network. 
650 0 0 |a Molecular chaperones. 
650 0 0 |a Protein folding. 
650 0 2 |a Chaperonin 10  |x metabolism. 
650 0 2 |a Chaperonin 60  |x metabolism. 
650 0 2 |a Chaperonins  |x metabolism. 
650 0 2 |a Molecular Chaperones. 
650 0 2 |a Protein Folding. 
830 0 |a Henry Stewart talks.  |p Biomedical & life sciences collection.  |p Protein homeostasis. 
988 |a 20141204 
906 |0 OCLC