| pubmed-article:8710175 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8710175 | lifeskim:mentions | umls-concept:C0085979 | lld:lifeskim |
| pubmed-article:8710175 | lifeskim:mentions | umls-concept:C0005854 | lld:lifeskim |
| pubmed-article:8710175 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
| pubmed-article:8710175 | lifeskim:mentions | umls-concept:C0175630 | lld:lifeskim |
| pubmed-article:8710175 | lifeskim:mentions | umls-concept:C0243144 | lld:lifeskim |
| pubmed-article:8710175 | lifeskim:mentions | umls-concept:C1100714 | lld:lifeskim |
| pubmed-article:8710175 | pubmed:issue | 2-3 | lld:pubmed |
| pubmed-article:8710175 | pubmed:dateCreated | 1996-9-12 | lld:pubmed |
| pubmed-article:8710175 | pubmed:abstractText | An intracarotid brain infusion/capillary depletion technique was used in guinea pigs to examine cerebral capillary sequestration and transport into brain parenchyma of sA beta 1-40 and sA beta 1-42, synthetic peptides identical to two forms of the amyloid beta peptide found in Alzheimer's disease lesions: the 40 residue form, found primarily in vascular deposits, and the 42 residue form, found primarily in senile plaques. The peptides crossed well into the brain parenchyma via a specific transport mechanism for which sA beta 1-40 had an approximately two-fold greater affinity than sA beta 1-42. There was significant capillary sequestration of sA beta 1-40, but retention by the microvasculature of sA beta 1-42 was negligible. These data suggest that the level of the 40 residue peptide in cerebral vasculature and of the 42 residue peptide in parenchyma could be regulated by blood-brain barrier sequestration and transport of their respective circulating precursors. | lld:pubmed |
| pubmed-article:8710175 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8710175 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8710175 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8710175 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8710175 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8710175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8710175 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8710175 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8710175 | pubmed:issn | 0304-3940 | lld:pubmed |
| pubmed-article:8710175 | pubmed:author | pubmed-author:McCombJ GJG | lld:pubmed |
| pubmed-article:8710175 | pubmed:author | pubmed-author:GhisoJJ | lld:pubmed |
| pubmed-article:8710175 | pubmed:author | pubmed-author:ZlokovicB VBV | lld:pubmed |
| pubmed-article:8710175 | pubmed:author | pubmed-author:MackicJ BJB | lld:pubmed |
| pubmed-article:8710175 | pubmed:author | pubmed-author:MartelC LCL | lld:pubmed |
| pubmed-article:8710175 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8710175 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8710175 | pubmed:volume | 206 | lld:pubmed |
| pubmed-article:8710175 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8710175 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8710175 | pubmed:pagination | 157-60 | lld:pubmed |
| pubmed-article:8710175 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:8710175 | pubmed:meshHeading | pubmed-meshheading:8710175-... | lld:pubmed |
| pubmed-article:8710175 | pubmed:meshHeading | pubmed-meshheading:8710175-... | lld:pubmed |
| pubmed-article:8710175 | pubmed:meshHeading | pubmed-meshheading:8710175-... | lld:pubmed |
| pubmed-article:8710175 | pubmed:meshHeading | pubmed-meshheading:8710175-... | lld:pubmed |
| pubmed-article:8710175 | pubmed:meshHeading | pubmed-meshheading:8710175-... | lld:pubmed |
| pubmed-article:8710175 | pubmed:meshHeading | pubmed-meshheading:8710175-... | lld:pubmed |
| pubmed-article:8710175 | pubmed:meshHeading | pubmed-meshheading:8710175-... | lld:pubmed |
| pubmed-article:8710175 | pubmed:meshHeading | pubmed-meshheading:8710175-... | lld:pubmed |
| pubmed-article:8710175 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8710175 | pubmed:articleTitle | Blood-brain barrier uptake of the 40 and 42 amino acid sequences of circulating Alzheimer's amyloid beta in guinea pigs. | lld:pubmed |
| pubmed-article:8710175 | pubmed:affiliation | Department of Neurological Surgery, Childrens Hospital Los Angeles, USC School of Medicine 90033, USA. | lld:pubmed |
| pubmed-article:8710175 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8710175 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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