Matches in DBpedia 2014 for { <http://dbpedia.org/resource/Autochaperone> ?p ?o. }
Showing items 1 to 25 of
25
with 100 items per page.
- Autochaperone abstract "Autotransporter proteins are proteins secreted out the Gram-negative bacteria. These beta helixes require a domain which is called the intramolecular autochaperone domain. It shows similarities with other intramolecular chaperone sequences and has a folding-associated function. This increases the efficiency, either by stabilizing the beta-barrel, or by promoting the folding of the passenger domain.The autochaperone domain is usually located between the HSF and the passenger domain. When the passenger domain is translocated, starting with its C terminus, the autochaperone domain is first out. This would result in the formation of a hairpin structure.".
- Autochaperone wikiPageExternalLink 489.
- Autochaperone wikiPageExternalLink doaj?func=abstract&id=175033.
- Autochaperone wikiPageExternalLink science?_ob=ArticleURL&_udi=B6VN3-4J9MWS9-1&_user=499882&_coverDate=06%2F30%2F2006&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_searchStrId=1470198162&_rerunOrigin=scholar.google&_acct=C000024498&_version=1&_urlVersion=0&_userid=499882&md5=2c1a1e0d466b5eb2c0955b5397c4402c&searchtype=a.
- Autochaperone wikiPageID "28916502".
- Autochaperone wikiPageRevisionID "601834805".
- Autochaperone hasPhotoCollection Autochaperone.
- Autochaperone subject Category:Protein_domains.
- Autochaperone subject Category:Protein_structural_motifs.
- Autochaperone type Artifact100021939.
- Autochaperone type Decoration103169390.
- Autochaperone type Design103178782.
- Autochaperone type Motif103789014.
- Autochaperone type Object100002684.
- Autochaperone type PhysicalEntity100001930.
- Autochaperone type ProteinStructuralMotifs.
- Autochaperone type Whole100003553.
- Autochaperone comment "Autotransporter proteins are proteins secreted out the Gram-negative bacteria. These beta helixes require a domain which is called the intramolecular autochaperone domain. It shows similarities with other intramolecular chaperone sequences and has a folding-associated function. This increases the efficiency, either by stabilizing the beta-barrel, or by promoting the folding of the passenger domain.The autochaperone domain is usually located between the HSF and the passenger domain.".
- Autochaperone label "Autochaperone".
- Autochaperone sameAs m.0dgpnw9.
- Autochaperone sameAs Q4826192.
- Autochaperone sameAs Q4826192.
- Autochaperone sameAs Autochaperone.
- Autochaperone wasDerivedFrom Autochaperone?oldid=601834805.
- Autochaperone isPrimaryTopicOf Autochaperone.