Type I Chaperonins: Mechanism and Beyond

Type I chaperonins are key players in maintaining the proteome of bacteria and organelles of bacterial origin. They are well known for their crucial role in mediating protein folding. For almost three decades, the molecular mechanism of chaperonin function has been the subject of intensive research....

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Main Author: Adina Breiman (auth)
Other Authors: Abdussalam Azem (auth)
Format: Book Chapter
Published: Frontiers Media SA 2018
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Online Access:Get Fullteks
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005 20210212
020 |a 978-2-88945-575-1 
020 |a 9782889455751 
024 7 |a 10.3389/978-2-88945-575-1  |c doi 
041 0 |a English 
042 |a dc 
100 1 |a Adina Breiman  |4 auth 
700 1 |a Abdussalam Azem  |4 auth 
245 1 0 |a Type I Chaperonins: Mechanism and Beyond 
260 |b Frontiers Media SA  |c 2018 
300 |a 1 electronic resource (104 p.) 
506 0 |a Open Access  |2 star  |f Unrestricted online access 
520 |a Type I chaperonins are key players in maintaining the proteome of bacteria and organelles of bacterial origin. They are well known for their crucial role in mediating protein folding. For almost three decades, the molecular mechanism of chaperonin function has been the subject of intensive research. Still, surprising new mechanistic discoveries are constantly reported. It seems that we are far from having a full understanding of the chaperonin mode of action. Chaperonins are not simply protein folding machines. They also perform diverse extramitochondrial tasks, mainly related to inflammatory and signal transduction processes. This eBook constitutes ten articles highlighting the latest developments related to the divers functions of Type I chaperonins. As its title, mechanism and beyond, the collection starts with mechanistic view, continues with extracellular functions and ends with biotechnological applications of Type I chaperonins. 
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546 |a English 
653 |a Hsp60 
653 |a GroEL 
653 |a chaperonin 
653 |a Hsp10 
653 |a GroES 
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856 4 0 |a www.oapen.org  |u https://directory.doabooks.org/handle/20.500.12854/61436  |7 0  |z DOAB: description of the publication