Source:http://linkedlifedata.com/resource/pubmed/id/10856932
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2000-8-17
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pubmed:abstractText |
Several proteins can traverse biological membranes through protein transduction. Small sections of these proteins (10-16 residues long) are responsible for this. Linking these domains covalently to compounds, peptides, antisense peptide nucleic acids or 40-nm iron beads, or as in-frame fusions with full-length proteins, lets them enter any cell type in a receptor- and transporter-independent fashion. Moreover, several of these fusions, introduced into mice, were delivered to all tissues, even crossing the blood-brain barrier. These domains thus might let us address new questions and even help in the treatment of human disease.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0962-8924
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
290-5
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading |
pubmed-meshheading:10856932-Amino Acid Sequence,
pubmed-meshheading:10856932-Animals,
pubmed-meshheading:10856932-Biological Transport,
pubmed-meshheading:10856932-Blood-Brain Barrier,
pubmed-meshheading:10856932-Cell Membrane,
pubmed-meshheading:10856932-Humans,
pubmed-meshheading:10856932-Molecular Sequence Data,
pubmed-meshheading:10856932-Peptide Fragments,
pubmed-meshheading:10856932-Recombinant Fusion Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
Protein transduction: unrestricted delivery into all cells?
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pubmed:affiliation |
Howard Hughes Medical Institute, Depts of Pathology and Medicine, and Barnes-Jewish Hospital, Washington University School of Medicine, 4940 Parkview Place, Campus Box 8022, St Louis, MO 63110, USA.
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pubmed:publicationType |
Journal Article,
Review
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