Abstract:
:The role of Hsp70 (heat-shock protein 70) chaperones in assisting protein-folding processes relies on their ability to associate with short peptide stretches of protein substrates in a transient and ATP-controlled manner. In the present study, we review the molecular details of the mechanism behind substrate recognition by Hsp70 proteins.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Erbse A,Mayer MP,Bukau Bdoi
10.1042/BST0320617keywords:
subject
Has Abstractpub_date
2004-08-01 00:00:00pages
617-21issue
Pt 4eissn
0300-5127issn
1470-8752pii
BST0320617journal_volume
32pub_type
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journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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abstract::The FG (female gametophyte) of flowering plants (angiosperms) is a simple highly polar structure composed of only a few cell types. The FG develops from a single cell through mitotic divisions to generate, depending on the species, four to 16 nuclei in a syncytium. These nuclei are then partitioned into three or four ...
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journal_title:Biochemical Society transactions
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abstract::The secretin receptor is prototypic of Class II GPCRs (G-protein-coupled receptors), based on its structural and functional characteristics and those of its natural agonist ligand. Secretin represents a linear 27-residue peptide with diffuse pharmacophoric domain. The secretin receptor includes the typical signature s...
journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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更新日期:2009-02-01 00:00:00
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journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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更新日期:2012-04-01 00:00:00
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journal_title:Biochemical Society transactions
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更新日期:1991-08-01 00:00:00
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journal_title:Biochemical Society transactions
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更新日期:2001-08-01 00:00:00
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journal_title:Biochemical Society transactions
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