Linked Life Data

18656475

Source:http://linkedlifedata.com/resource/pubmed/id/18656475

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2008-8-12
pubmed:abstractText
We report the amyloid-like properties of Escherichia coli transthyretin-like protein (TLP). TLP is 32% homologous to human transthyretin (hTTR), and is also tetrameric. In contrast to hTTR, TLP does not bind thyroxine. TLP orthologues are found in several prokaryotes, lower eukaryotes and vertebrates. TLP carries a signal peptide that targets the protein to the periplasmic space. We found that TLP and hTTR tetramers dissociate into monomers under similar conditions, although TLP monomers have different association properties. Like hTTR, TLP forms aggregates, small fibrillar structures of 8 nm width, and annular structures of 8 nm diameter which present amyloid-like properties and are toxic to cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
582
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2893-8
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Amyloidogenic properties of transthyretin-like protein (TLP) from Escherichia coli.
pubmed:affiliation
Molecular Neurobiology Unit, Institute for Molecular and Cell Biology, Rua do Campo Alegre 823, Porto, Portugal.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural