| pubmed-article:7722513 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7722513 | lifeskim:mentions | umls-concept:C0441635 | lld:lifeskim |
| pubmed-article:7722513 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
| pubmed-article:7722513 | lifeskim:mentions | umls-concept:C0036720 | lld:lifeskim |
| pubmed-article:7722513 | lifeskim:mentions | umls-concept:C0041491 | lld:lifeskim |
| pubmed-article:7722513 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:7722513 | pubmed:dateCreated | 1995-5-23 | lld:pubmed |
| pubmed-article:7722513 | pubmed:abstractText | A synthetic peptide corresponding to residues 32-47 of rat tyrosine hydroxylase (TH) was phosphorylated by protein kinase A at Ser40 and used to generate antibodies in rabbits. Reactivity of the anti-pTH32-47 antibodies with phospho- and dephospho-Ser40 forms of TH protein and peptide TH32-47 was compared with reactivity of antibodies to nonphosphorylated peptide and to native TH protein. In antibody-capture ELISAs, anti-pTH32-47 was more reactive with the phospho-TH than with the dephospho-TH forms. Conversely, antibodies against the nonphosphorylated peptide reacted preferentially with the dephospho-TH forms. In western blots, labeling of the approximately 60-kDa TH band by anti-pTH32-47 was readily detectable in lanes containing protein kinase A-phosphorylated native TH at 10-100 ng/lane. In blots of supernatants prepared from striatal synaptosomes, addition of a phosphatase inhibitor was necessary to discern labeling of the TH band with anti-pTH32-47. Similarly, anti-pTH32-47 failed to immunoprecipitate TH activity from supernatants prepared from untreated tissues, whereas prior treatment with either 8-bromoadenosine 3',5'-cyclic monophosphate or forskolin enabled removal of TH activity by anti-pTH32-47. Lastly, in immunohistochemical studies, anti-pTH32-47 selectively labeled catecholaminergic cells in tissue sections from perfusion-fixed rat brain. | lld:pubmed |
| pubmed-article:7722513 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7722513 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7722513 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7722513 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7722513 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7722513 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7722513 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7722513 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7722513 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7722513 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7722513 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7722513 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7722513 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7722513 | pubmed:month | May | lld:pubmed |
| pubmed-article:7722513 | pubmed:issn | 0022-3042 | lld:pubmed |
| pubmed-article:7722513 | pubmed:author | pubmed-author:GoldsteinMM | lld:pubmed |
| pubmed-article:7722513 | pubmed:author | pubmed-author:LeeK YKY | lld:pubmed |
| pubmed-article:7722513 | pubmed:author | pubmed-author:HaycockJ WJW | lld:pubmed |
| pubmed-article:7722513 | pubmed:author | pubmed-author:LewJ YJY | lld:pubmed |
| pubmed-article:7722513 | pubmed:author | pubmed-author:HaradaKK | lld:pubmed |
| pubmed-article:7722513 | pubmed:author | pubmed-author:WuJJ | lld:pubmed |
| pubmed-article:7722513 | pubmed:author | pubmed-author:HokfeltTT | lld:pubmed |
| pubmed-article:7722513 | pubmed:author | pubmed-author:DeutchA YAY | lld:pubmed |
| pubmed-article:7722513 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7722513 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:7722513 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7722513 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7722513 | pubmed:pagination | 2281-7 | lld:pubmed |
| pubmed-article:7722513 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:7722513 | pubmed:meshHeading | pubmed-meshheading:7722513-... | lld:pubmed |
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| pubmed-article:7722513 | pubmed:meshHeading | pubmed-meshheading:7722513-... | lld:pubmed |
| pubmed-article:7722513 | pubmed:meshHeading | pubmed-meshheading:7722513-... | lld:pubmed |
| pubmed-article:7722513 | pubmed:meshHeading | pubmed-meshheading:7722513-... | lld:pubmed |
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| pubmed-article:7722513 | pubmed:meshHeading | pubmed-meshheading:7722513-... | lld:pubmed |
| pubmed-article:7722513 | pubmed:meshHeading | pubmed-meshheading:7722513-... | lld:pubmed |
| pubmed-article:7722513 | pubmed:meshHeading | pubmed-meshheading:7722513-... | lld:pubmed |
| pubmed-article:7722513 | pubmed:meshHeading | pubmed-meshheading:7722513-... | lld:pubmed |
| pubmed-article:7722513 | pubmed:meshHeading | pubmed-meshheading:7722513-... | lld:pubmed |
| pubmed-article:7722513 | pubmed:meshHeading | pubmed-meshheading:7722513-... | lld:pubmed |
| pubmed-article:7722513 | pubmed:meshHeading | pubmed-meshheading:7722513-... | lld:pubmed |
| pubmed-article:7722513 | pubmed:meshHeading | pubmed-meshheading:7722513-... | lld:pubmed |
| pubmed-article:7722513 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7722513 | pubmed:articleTitle | Antibodies to a segment of tyrosine hydroxylase phosphorylated at serine 40. | lld:pubmed |
| pubmed-article:7722513 | pubmed:affiliation | Neurochemistry Research Laboratories, New York University Medical Center, NY 10016, USA. | lld:pubmed |
| pubmed-article:7722513 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7722513 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7722513 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
