Linked Life Data

8262196

Source:http://linkedlifedata.com/resource/pubmed/id/8262196

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-1-26
pubmed:abstractText
Deletion mutants of a synthetic human erythropoietin-cDNA were transiently expressed in COS-7 cells and products analyzed using Western blots and a cell proliferation assay. Only two mutants with deletions affecting the N-terminal portion and the amino acid sequence 115-121 displayed biological activity. The exchange of hydrophilic, charged amino acids by alanine in two potential alpha-helical regions, the internal amino acid sequence 102-106 and the C-terminal sequence 154-159, causes a 2-11-fold loss of activity. The results suggest that both regions are involved in either maintaining the active structure of the hormone or interacting with the receptor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
336
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Structural and functional characterisation of recombinant human erythropoietin analogues.
pubmed:affiliation
Institut für Medizinische Biochemie der Medizinischen Fakultät der Universität Rostock, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't