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Entity

Name
protein refolding
Namespace
go
Namespace Version
20180921
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

Appears in Networks 1

In-Edges 5

act(p(FPLX:HSP90)) association bp(GO:"protein refolding") View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

act(p(FPLX:HSPA)) association bp(GO:"protein refolding") View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

act(p(FPLX:HSPA)) association bp(GO:"protein refolding") View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

complex(p(HGNC:HSPD1), p(HGNC:HSPE1)) increases bp(GO:"protein refolding") View Subject | View Object

Binding to GroEL prevents aggregation of these flexible folding intermediates, and subsequent folding depends critically on the global encapsulation of the substrate in the chaperonin cavity by the cochaperone GroES (7, 132–135). PubMed:23746257

act(p(HGNCGENEFAMILY:Chaperonins)) association bp(GO:"protein refolding") View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

Out-Edges 4

bp(GO:"protein refolding") association act(p(HGNCGENEFAMILY:Chaperonins)) View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

bp(GO:"protein refolding") association act(p(FPLX:HSPA)) View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

bp(GO:"protein refolding") association act(p(FPLX:HSPA)) View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

bp(GO:"protein refolding") association act(p(FPLX:HSP90)) View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.